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Volumn 270, Issue 1 14-1, 1996, Pages

Extracellular matrix biology in the lung

Author keywords

basement membrane; cell shape; cellular differentiation; connective tissue; integrins; pulmonary compliance

Indexed keywords

COLLAGEN; ENTACTIN; FIBRONECTIN; INTEGRIN; LAMININ; PLASMIN; PLASMINOGEN ACTIVATOR; PROTEOGLYCAN; TENASCIN;

EID: 0030041083     PISSN: 10400605     EISSN: None     Source Type: Journal    
DOI: 10.1152/ajplung.1996.270.1.l3     Document Type: Review
Times cited : (207)

References (493)
  • 1
    • 0027230170 scopus 로고
    • Regulation of development and differentiation by the extracellular matrix
    • Adams, J. C., and F. M. Watt. Regulation of development and differentiation by the extracellular matrix. Development 117: 1183-1198, 1993.
    • (1993) Development , vol.117 , pp. 1183-1198
    • Adams, J.C.1    Watt, F.M.2
  • 3
    • 0015992802 scopus 로고
    • The type 2 cell as progenitor of alveolar epithelial regeneration: A cytodynamic study in mice after exposure to oxygen
    • Adamson, I. Y. R., and D. H. Bowden. The type 2 cell as progenitor of alveolar epithelial regeneration: a cytodynamic study in mice after exposure to oxygen. Lab. Invest. 30: 35-42, 1974.
    • (1974) Lab. Invest. , vol.30 , pp. 35-42
    • Adamson, I.Y.R.1    Bowden, D.H.2
  • 4
    • 0016742681 scopus 로고
    • Derivation of type I epithelium from type II cells in the developing rat lung
    • Adamson, I. Y. R., and D. H. Bowden. Derivation of type I epithelium from type II cells in the developing rat lung. Lab. Invest. 32: 736-745, 1975.
    • (1975) Lab. Invest. , vol.32 , pp. 736-745
    • Adamson, I.Y.R.1    Bowden, D.H.2
  • 5
    • 0022531990 scopus 로고
    • Epithelial-interstitial cell interactions in fetal rat lung development accelerated by steroids
    • Adamson, I. Y. R., and G. M. King. Epithelial-interstitial cell interactions in fetal rat lung development accelerated by steroids. Lab. Invest. 55: 145-152, 1986.
    • (1986) Lab. Invest. , vol.55 , pp. 145-152
    • Adamson, I.Y.R.1    King, G.M.2
  • 6
    • 0024327633 scopus 로고
    • Influence of extracellular matrix and collagen components on alveolar type 2 cell morphology and function
    • Adamson, I. Y. R., G. M. King, and L. Young. Influence of extracellular matrix and collagen components on alveolar type 2 cell morphology and function. In Vitro Cell. Dev. Biol. 25: 494-502, 1989.
    • (1989) In Vitro Cell. Dev. Biol. , vol.25 , pp. 494-502
    • Adamson, I.Y.R.1    King, G.M.2    Young, L.3
  • 7
    • 0025823541 scopus 로고
    • Cross-linking of lamininnidogen complexes by tissue transglutaminase: A novel mechanism for basement membrane stabilization
    • Aeschlimann, D., and M. Paulsson. Cross-linking of lamininnidogen complexes by tissue transglutaminase: a novel mechanism for basement membrane stabilization. J. Biol. Chem. 266: 15308-15317, 1991.
    • (1991) J. Biol. Chem. , vol.266 , pp. 15308-15317
    • Aeschlimann, D.1    Paulsson, M.2
  • 8
    • 0026468487 scopus 로고
    • Electron-microscopic evidence for cytochrome P-450 in Clara cells and type I pneumocytes of the rat lung
    • Aida, S., Y. Takahashi, E. Suzuki, Y. Kimula, Y. Ito, and T. Miura. Electron-microscopic evidence for cytochrome P-450 in Clara cells and type I pneumocytes of the rat lung. Respiration 59: 201-210, 1992.
    • (1992) Respiration , vol.59 , pp. 201-210
    • Aida, S.1    Takahashi, Y.2    Suzuki, E.3    Kimula, Y.4    Ito, Y.5    Miura, T.6
  • 9
    • 0023819775 scopus 로고
    • Extracellular matrix assembly of cell-derived and plasma-derived fibronectins by substrate-attached fibroblasts
    • Allio, A. E., and P. J. McKeown-Longo. Extracellular matrix assembly of cell-derived and plasma-derived fibronectins by substrate-attached fibroblasts. J. Cell. Physiol. 135: 459-466, 1988.
    • (1988) J. Cell. Physiol. , vol.135 , pp. 459-466
    • Allio, A.E.1    McKeown-Longo, P.J.2
  • 10
    • 0023794955 scopus 로고
    • Connective tissue of rat lung. II. Ultrastructural localization of collagen types III, IV, and VT
    • Amenta, P. S., J. Gil, and A. Martinez-Hernadez. Connective tissue of rat lung. II. Ultrastructural localization of collagen types III, IV, and VT. J. Histochem. Cytochem. 36: 1167-1173, 1988.
    • (1988) J. Histochem. Cytochem. , vol.36 , pp. 1167-1173
    • Amenta, P.S.1    Gil, J.2    Martinez-Hernadez, A.3
  • 11
    • 0023738917 scopus 로고
    • Enhanced synthesis and secretion of type IV collagen and entactin during adipose conversion of 3T3-L1 cells and production of unorthodox laminin
    • Aratani, Y., and Y. Kitagawa. Enhanced synthesis and secretion of type IV collagen and entactin during adipose conversion of 3T3-L1 cells and production of unorthodox laminin. J. Biol. Chem. 263: 16163-16169, 1988.
    • (1988) J. Biol. Chem. , vol.263 , pp. 16163-16169
    • Aratani, Y.1    Kitagawa, Y.2
  • 12
    • 0025950630 scopus 로고
    • Cell interactions with laminin and its proteolytic fragments during outgrowth of mouse primary trophoblast cells
    • Armant, D. R. Cell interactions with laminin and its proteolytic fragments during outgrowth of mouse primary trophoblast cells. Biol. Reprod. 45: 664-672, 1991.
    • (1991) Biol. Reprod. , vol.45 , pp. 664-672
    • Armant, D.R.1
  • 13
    • 0019423586 scopus 로고
    • A difference between plasma and cellular fibronectin located with monoclonal antibodies
    • Atherton, B. T., and R. O. Hynes. A difference between plasma and cellular fibronectin located with monoclonal antibodies. Cell 25: 133-141, 1981.
    • (1981) Cell , vol.25 , pp. 133-141
    • Atherton, B.T.1    Hynes, R.O.2
  • 14
    • 0023375129 scopus 로고
    • Epithelial-mesenchymal interactions in the developing kidney lead to expression of tenascin in the mesenchyme
    • Aufderheide, E., R. Chiquet-Ehrismann, and P. Ekblom. Epithelial-mesenchymal interactions in the developing kidney lead to expression of tenascin in the mesenchyme. J. Cell Biol. 105: 599-608, 1987.
    • (1987) J. Cell Biol. , vol.105 , pp. 599-608
    • Aufderheide, E.1    Chiquet-Ehrismann, R.2    Ekblom, P.3
  • 15
    • 0024205512 scopus 로고
    • Tenascin during gut development: Appearance in the mesenchyme, shift in molecular forms, and dependence on epithelial-mesenchymal interactions
    • Auferheide, E., and P. Ekblom. Tenascin during gut development: appearance in the mesenchyme, shift in molecular forms, and dependence on epithelial-mesenchymal interactions. J. Cell Biol. 107: 2341-2349, 1988.
    • (1988) J. Cell Biol. , vol.107 , pp. 2341-2349
    • Auferheide, E.1    Ekblom, P.2
  • 17
    • 0023664920 scopus 로고
    • The cellular interactions of laminin fragments. Cell adhesion correlates with two fragment-specific high affinity binding sites
    • Aumailley, M., V. Nurcombe, D. Edgar, M. Paulsson, and R. Timpl. The cellular interactions of laminin fragments. Cell adhesion correlates with two fragment-specific high affinity binding sites. J. Biol. Chem. 262: 11532-11538, 1987.
    • (1987) J. Biol. Chem. , vol.262 , pp. 11532-11538
    • Aumailley, M.1    Nurcombe, V.2    Edgar, D.3    Paulsson, M.4    Timpl, R.5
  • 18
    • 0024460533 scopus 로고
    • Binding of nidogen and the laminin-nidogen complex to basement membrane collagen type IV
    • Aumailley, M., H. Wiedemann, K. Mann, and R. Timpl. Binding of nidogen and the laminin-nidogen complex to basement membrane collagen type IV Eur. J. Biochem. 184: 241-248, 1989.
    • (1989) Eur. J. Biochem. , vol.184 , pp. 241-248
    • Aumailley, M.1    Wiedemann, H.2    Mann, K.3    Timpl, R.4
  • 19
    • 0024457599 scopus 로고
    • Binding of thrombin to subendothelial extracellular matrix. Protection and expression of functional properties
    • Bar-Shavit, R., A. Eldor, and I. Vlodavsky. Binding of thrombin to subendothelial extracellular matrix. Protection and expression of functional properties. J. Clin. Invest. 84: 1096-1104, 1989.
    • (1989) J. Clin. Invest. , vol.84 , pp. 1096-1104
    • Bar-Shavit, R.1    Eldor, A.2    Vlodavsky, I.3
  • 20
    • 0023805668 scopus 로고
    • Factor XIII cross-linking of fibronectin at cellular matrix assembly sites
    • Barry, E. L. R., and D. F. Mosher. Factor XIII cross-linking of fibronectin at cellular matrix assembly sites. J. Biol. Chem. 263: 10464-10469, 1988.
    • (1988) J. Biol. Chem. , vol.263 , pp. 10464-10469
    • Barry, E.L.R.1    Mosher, D.F.2
  • 21
    • 0024593415 scopus 로고
    • Factor XIIIa-mediated cross-linking of fibronectin in fibroblast cell layers
    • Barry, E. L. R., and D. F. Mosher. Factor XIIIa-mediated cross-linking of fibronectin in fibroblast cell layers. J. Biol. Chem. 264: 4179-4185, 1989.
    • (1989) J. Biol. Chem. , vol.264 , pp. 4179-4185
    • Barry, E.L.R.1    Mosher, D.F.2
  • 22
    • 0025837326 scopus 로고
    • Tissue (type II) transglutaminase covalently incorporates itself, fibrinogen, or fibronectin into high molecular weight complexes on the extracellular surface of isolated hepatocytes. Use of 2-[(2-oxopropyl)-thio] imidazolium derivatives as cellular transglutaminase inactivators
    • Barsigian, C., A. M. Stern, and J. Martinez. Tissue (type II) transglutaminase covalently incorporates itself, fibrinogen, or fibronectin into high molecular weight complexes on the extracellular surface of isolated hepatocytes. Use of 2-[(2-oxopropyl)-thio] imidazolium derivatives as cellular transglutaminase inactivators. J. Biol. Chem. 266: 22501-22509, 1991.
    • (1991) J. Biol. Chem. , vol.266 , pp. 22501-22509
    • Barsigian, C.1    Stern, A.M.2    Martinez, J.3
  • 25
    • 0025370901 scopus 로고
    • Degranulating mast cells secrete an endoglycosidase that degrades heparan sulfate in subendothelial extracellular matrix
    • Bashkin, P., E. Razin, A. Eldor, and I. Vlodavsky. Degranulating mast cells secrete an endoglycosidase that degrades heparan sulfate in subendothelial extracellular matrix. Blood 75: 2204-2212, 1990.
    • (1990) Blood , vol.75 , pp. 2204-2212
    • Bashkin, P.1    Razin, E.2    Eldor, A.3    Vlodavsky, I.4
  • 27
    • 0026703151 scopus 로고
    • Basement-membrane heparan sulfate proteoglycan binds to laminin by its heparan sulfate chains and to nidogen by sites in the protein core
    • Battaglia, C., U. Mayer, M. Aumailley, and R. Timpl. Basement-membrane heparan sulfate proteoglycan binds to laminin by its heparan sulfate chains and to nidogen by sites in the protein core. Eur. J. Biochem. 208: 359-366, 1992.
    • (1992) Eur. J. Biochem. , vol.208 , pp. 359-366
    • Battaglia, C.1    Mayer, U.2    Aumailley, M.3    Timpl, R.4
  • 29
    • 0025165018 scopus 로고
    • Structure and function of laminin: Anatomy of a multidomain glyeoprotein
    • Beck, K., I. Hunter, and J. Engel. Structure and function of laminin: anatomy of a multidomain glyeoprotein. FASEB J. 4: 148-160, 1990.
    • (1990) FASEB J. , vol.4 , pp. 148-160
    • Beck, K.1    Hunter, I.2    Engel, J.3
  • 30
    • 0023682996 scopus 로고
    • Hydrocortisone-induced accumulation of fibronectin mRNA and cell surface-associated fibronectin
    • Begemann, M., B. Voss, and D. Paul. Hydrocortisone-induced accumulation of fibronectin mRNA and cell surface-associated fibronectin. J. Cancer Res. Clin. Oncol. 114: 477-481, 1988.
    • (1988) J. Cancer Res. Clin. Oncol. , vol.114 , pp. 477-481
    • Begemann, M.1    Voss, B.2    Paul, D.3
  • 33
    • 0021717070 scopus 로고
    • Kinetics of proteoheparan sulfate synthesis, secretion, endocytosis, and catabolism by ahepatocyte cell line
    • Bienkowski, M. J., and H. E. Conrad. Kinetics of proteoheparan sulfate synthesis, secretion, endocytosis, and catabolism by ahepatocyte cell line. J. Biol. Chem. 259: 12989-12996, 1984.
    • (1984) J. Biol. Chem. , vol.259 , pp. 12989-12996
    • Bienkowski, M.J.1    Conrad, H.E.2
  • 34
    • 0023873382 scopus 로고
    • Collagen type I and V are present in the same fibril in the avian corneal stroma
    • Birk, D. E., J. M. Fitch, J. P. Babiarz, and T. F. Linsenmayer. Collagen type I and V are present in the same fibril in the avian corneal stroma. J. Cell Biol. 106: 999-1008, 1988.
    • (1988) J. Cell Biol. , vol.106 , pp. 999-1008
    • Birk, D.E.1    Fitch, J.M.2    Babiarz, J.P.3    Linsenmayer, T.F.4
  • 36
    • 0023857748 scopus 로고
    • Induction of fibronectin gene transcription and mRNA is a primary response to growth-factor stimulation of AKR-2B cells
    • Blatti, S. P., D. N. Foster, G. Ranganathan, H. L. Moses, and M. J. Getz. Induction of fibronectin gene transcription and mRNA is a primary response to growth-factor stimulation of AKR-2B cells. Proc. Natl. Acad. Sci. USA 85: 1119-1123, 1988.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 1119-1123
    • Blatti, S.P.1    Foster, D.N.2    Ranganathan, G.3    Moses, H.L.4    Getz, M.J.5
  • 37
    • 0023806959 scopus 로고
    • Fetal type 2 pneumocytes form alveolarlike structures and maintain long-term differentiation on extracellular matrix
    • Blau, H., D. E. Guzowski, Z. A. Siddiqi, E. M. Scarpelli, and R. S. Bienkowski. Fetal type 2 pneumocytes form alveolarlike structures and maintain long-term differentiation on extracellular matrix. J. Cell. Physiol. 136: 203-214, 1988.
    • (1988) J. Cell. Physiol. , vol.136 , pp. 203-214
    • Blau, H.1    Guzowski, D.E.2    Siddiqi, Z.A.3    Scarpelli, E.M.4    Bienkowski, R.S.5
  • 38
    • 0023656006 scopus 로고
    • Steady-state levels of mRNAs coding for the type IV collagen and laminin polypeptide chains for basement membranes exhibit marked tissue-specific stoichiometric variations in the rat
    • Boot-Handford, R. P., M. Kurkinen, and D. J. Prockop. Steady-state levels of mRNAs coding for the type IV collagen and laminin polypeptide chains for basement membranes exhibit marked tissue-specific stoichiometric variations in the rat. J. Biol. Chem. 262: 12475-12478, 1987.
    • (1987) J. Biol. Chem. , vol.262 , pp. 12475-12478
    • Boot-Handford, R.P.1    Kurkinen, M.2    Prockop, D.J.3
  • 39
    • 0024368075 scopus 로고
    • Regulation of collagen gene expression
    • Bornstein, P., and H. Sage. Regulation of collagen gene expression. Prog. Nucleic Acid Res. 37: 67-106, 1989.
    • (1989) Prog. Nucleic Acid Res. , vol.37 , pp. 67-106
    • Bornstein, P.1    Sage, H.2
  • 41
    • 0025100249 scopus 로고
    • Spreading of B16 F1 cells on laminin and its proteolytic fragments P1 and E8: Involvement of laminin carbohydrate chains
    • Bouzon, M., C. Dussert, J. C. Lissitzky, and P. M. Martin. Spreading of B16 F1 cells on laminin and its proteolytic fragments P1 and E8: involvement of laminin carbohydrate chains. Exp. Cell Res. 190: 47-56, 1990.
    • (1990) Exp. Cell Res. , vol.190 , pp. 47-56
    • Bouzon, M.1    Dussert, C.2    Lissitzky, J.C.3    Martin, P.M.4
  • 42
    • 0026072631 scopus 로고
    • Syndecan, a cell surface proteoglycan, exhibits a molecular polymorphism during lung development
    • Brauker, J. H., M. S. Trautman, and M. Bernfield. Syndecan, a cell surface proteoglycan, exhibits a molecular polymorphism during lung development. Dev. Biol. 147: 285-292, 1991.
    • (1991) Dev. Biol. , vol.147 , pp. 285-292
    • Brauker, J.H.1    Trautman, M.S.2    Bernfield, M.3
  • 43
  • 44
    • 0027252762 scopus 로고
    • Type I collagen gene regulation and the molecular pathogenesis of cirrhosis
    • Gastrointest. Liver Physiol. 27
    • Brenner, D. A., J. Westwick, and M. Breindl. Type I collagen gene regulation and the molecular pathogenesis of cirrhosis. Am. J. Physiol. 264 (Gastrointest. Liver Physiol. 27): G589-G595, 1993.
    • (1993) Am. J. Physiol. , vol.264
    • Brenner, D.A.1    Westwick, J.2    Breindl, M.3
  • 45
    • 0027231385 scopus 로고
    • Tenascin-X: A novel extracellular matrix protein encoded by the human XB gene overlapping p450c21B
    • Bristow, J., M. K. Tee, S. E. Gitelman, S. H. Mellon, and W. L. Miller. Tenascin-X: a novel extracellular matrix protein encoded by the human XB gene overlapping p450c21B. J. Cell Biol. 122: 265-278, 1993.
    • (1993) J. Cell Biol. , vol.122 , pp. 265-278
    • Bristow, J.1    Tee, M.K.2    Gitelman, S.E.3    Mellon, S.H.4    Miller, W.L.5
  • 46
    • 0020362272 scopus 로고
    • Alterations in alveolar basement membranes during postnatal lung growth
    • Brody, J. S., C. A. Vaccaro, P. J. Gill, and J. E. Silbert. Alterations in alveolar basement membranes during postnatal lung growth. J. Cell Biol. 90: 394-402, 1982.
    • (1982) J. Cell Biol. , vol.90 , pp. 394-402
    • Brody, J.S.1    Vaccaro, C.A.2    Gill, P.J.3    Silbert, J.E.4
  • 47
    • 0022547414 scopus 로고
    • Type VI collagen in extracellular, 100-nm periodic filaments and fibrils: Identification by immunoelectron microscopy
    • Bruns, R. R., W. Press, E. Engvall, R. Timpl, and J. Gross. Type VI collagen in extracellular, 100-nm periodic filaments and fibrils: identification by immunoelectron microscopy. J. Cell Biol. 103: 393-404, 1986.
    • (1986) J. Cell Biol. , vol.103 , pp. 393-404
    • Bruns, R.R.1    Press, W.2    Engvall, E.3    Timpl, R.4    Gross, J.5
  • 48
    • 0027296584 scopus 로고
    • Type VII collagen, anchoring fibrils, and epidermolysis bullosa
    • Burgeson, R. E. Type VII collagen, anchoring fibrils, and epidermolysis bullosa. J. Invest. Dermatol. 101: 252-255, 1993.
    • (1993) J. Invest. Dermatol. , vol.101 , pp. 252-255
    • Burgeson, R.E.1
  • 50
    • 0026673475 scopus 로고
    • Collagen types. Molecular structure and tissue distribution
    • Burgeson, R. E., and M. E. Nimni. Collagen types. Molecular structure and tissue distribution. Clin. Orthop. 282: 250-272, 1992.
    • (1992) Clin. Orthop. , vol.282 , pp. 250-272
    • Burgeson, R.E.1    Nimni, M.E.2
  • 51
    • 0024150623 scopus 로고
    • Focal adhesions: Transmembrane junctions between the extracellular matrix and the cytoskeleton
    • Burridge, K., K. Fath, T. Kelley, G. Nuckolls, and C. Turner. Focal adhesions: transmembrane junctions between the extracellular matrix and the cytoskeleton. Annu. Rev. Cell Biol. 4: 487-525, 1988.
    • (1988) Annu. Rev. Cell Biol. , vol.4 , pp. 487-525
    • Burridge, K.1    Fath, K.2    Kelley, T.3    Nuckolls, G.4    Turner, C.5
  • 53
    • 0027991270 scopus 로고
    • Domain-specific activation of neuronal migration and neurite outgrowth-promoting activities of laminin
    • Calof, A. L., M. R. Campanero, J. J. O'Rear, P. D. Yurchenco, and A. D. Lander. Domain-specific activation of neuronal migration and neurite outgrowth-promoting activities of laminin. Neuron 13: 117-130, 1994.
    • (1994) Neuron , vol.13 , pp. 117-130
    • Calof, A.L.1    Campanero, M.R.2    O'Rear, J.J.3    Yurchenco, P.D.4    Lander, A.D.5
  • 55
    • 0023237615 scopus 로고
    • Extracellular matrix injury during lung inflammation
    • Campbell, E. J., R. M. Senior, and H. G. Welgus. Extracellular matrix injury during lung inflammation. Chest 92: 161-167, 1987.
    • (1987) Chest , vol.92 , pp. 161-167
    • Campbell, E.J.1    Senior, R.M.2    Welgus, H.G.3
  • 56
    • 0028847673 scopus 로고
    • Differential expression of collagen-binding receptors in fetal rat lung cells
    • Lung Cell. Mol. Physiol. 12
    • Caniggia, I., R. Han, J. Liu, J. Wang, A. K. Tanswell, and M. Post. Differential expression of collagen-binding receptors in fetal rat lung cells. Am. J. Physiol. 268 (Lung Cell. Mol. Physiol. 12): L136-L148, 1995.
    • (1995) Am. J. Physiol. , vol.268
    • Caniggia, I.1    Han, R.2    Liu, J.3    Wang, J.4    Tanswell, A.K.5    Post, M.6
  • 57
    • 0019888064 scopus 로고
    • Entactin, a novel basal lamina-associated sulfated glycoprotein
    • Carlin, B., R. Jaffe, B. Bender, and A. E. Chung. Entactin, a novel basal lamina-associated sulfated glycoprotein. J. Biol. Chem. 256: 5209-5214, 1981.
    • (1981) J. Biol. Chem. , vol.256 , pp. 5209-5214
    • Carlin, B.1    Jaffe, R.2    Bender, B.3    Chung, A.E.4
  • 58
    • 0025058804 scopus 로고
    • Induction of albumin gene transcription in hepatocytes by extracellular matrix proteins
    • Caron, J. M. Induction of albumin gene transcription in hepatocytes by extracellular matrix proteins. Mol. Cell Biol. 10. 1239-1243, 1990.
    • (1990) Mol. Cell Biol. , vol.10 , pp. 1239-1243
    • Caron, J.M.1
  • 60
    • 0020980094 scopus 로고
    • Hyaluronic acid and proteoglycan synthesis by lung fibroblasts in basal and activated states
    • Castor, C. W., T. D. Fremuth, A. M. Furlong, and G. W. Jourdian. Hyaluronic acid and proteoglycan synthesis by lung fibroblasts in basal and activated states. In Vitro 19: 462-470, 1983.
    • (1983) In Vitro , vol.19 , pp. 462-470
    • Castor, C.W.1    Fremuth, T.D.2    Furlong, A.M.3    Jourdian, G.W.4
  • 62
    • 0028285478 scopus 로고
    • Lamina lucida of basement membrane: An artefact
    • Chan, F. L., and S. Inoue. Lamina lucida of basement membrane: an artefact. Microsc. Res. Tech. 28: 48-59, 1994.
    • (1994) Microsc. Res. Tech. , vol.28 , pp. 48-59
    • Chan, F.L.1    Inoue, S.2
  • 63
    • 0025822473 scopus 로고
    • Kinetics of plasma fibronectin: Increased lung tissue incorporation after postoperative bacteremia
    • Regulatory Integrative Comp. Physiol. 29
    • Charash, W. E., P. A. Vincent, P. J. McKeown-Longo, T. M. Saba, E. Lewis, and M. A. Lewis. Kinetics of plasma fibronectin: increased lung tissue incorporation after postoperative bacteremia. Am. J. Physiol. 260 (Regulatory Integrative Comp. Physiol. 29): R553-R562, 1991.
    • (1991) Am. J. Physiol. , vol.260
    • Charash, W.E.1    Vincent, P.A.2    McKeown-Longo, P.J.3    Saba, T.M.4    Lewis, E.5    Lewis, M.A.6
  • 67
    • 0023867657 scopus 로고
    • Arachidonic acid metabolism by rat alveolar epithelial cells
    • Chauncey, J. B., M. Peters-Golden, and R. H. Simon. Arachidonic acid metabolism by rat alveolar epithelial cells. Lab. Invest. 58: 133-140, 1988.
    • (1988) Lab. Invest. , vol.58 , pp. 133-140
    • Chauncey, J.B.1    Peters-Golden, M.2    Simon, R.H.3
  • 68
    • 0023228441 scopus 로고
    • Cellular events associated with lung branching morphogenesis including the deposition of collagen type IV
    • Chen, J. M., and C. D. Little. Cellular events associated with lung branching morphogenesis including the deposition of collagen type IV. Dev. Biol. 120: 311-321, 1987.
    • (1987) Dev. Biol. , vol.120 , pp. 311-321
    • Chen, J.M.1    Little, C.D.2
  • 69
    • 0027939187 scopus 로고
    • Integrin-mediated cell adhesion activates mitogenactivated protein kinases
    • Chen, Q., M. S. Kinch, T. H. Lin, K. Burridge, and R. Juliano. Integrin-mediated cell adhesion activates mitogenactivated protein kinases. J. Biol. Chem. 269: 26602-26605, 1994.
    • (1994) J. Biol. Chem. , vol.269 , pp. 26602-26605
    • Chen, Q.1    Kinch, M.S.2    Lin, T.H.3    Burridge, K.4    Juliano, R.5
  • 70
    • 0025730907 scopus 로고
    • Role of the I-9 and III-1 modules of fibronectin in formation of an extracellular fibronectin matrix
    • Chernousov, M. A., F. J. Fogerty, V. E. Koteliansky, and D. F. Mosher. Role of the I-9 and III-1 modules of fibronectin in formation of an extracellular fibronectin matrix. J. Biol. Chem. 266: 10851-10858, 1991.
    • (1991) J. Biol. Chem. , vol.266 , pp. 10851-10858
    • Chernousov, M.A.1    Fogerty, F.J.2    Koteliansky, V.E.3    Mosher, D.F.4
  • 71
    • 0022353379 scopus 로고
    • Stromelysin: A connective tissue-degrading metalloendopeptidase secreted by stimulated rabbit synovial fibroblasts in parallel with collagenase. Biosynthesis, isolation, characterization and substrates
    • Chin, J. R., G. Murphy, and Z. Werb. Stromelysin: a connective tissue-degrading metalloendopeptidase secreted by stimulated rabbit synovial fibroblasts in parallel with collagenase. Biosynthesis, isolation, characterization and substrates. J. Biol. Chem. 260: 12367-12376, 1985.
    • (1985) J. Biol. Chem. , vol.260 , pp. 12367-12376
    • Chin, J.R.1    Murphy, G.2    Werb, Z.3
  • 72
    • 0026597967 scopus 로고
    • Tenascin: An extracellular matrix protein involved in morphogenesis of epithelial organs
    • Chiquet, M. Tenascin: an extracellular matrix protein involved in morphogenesis of epithelial organs. Kidney Int. 41: 629-631, 1992.
    • (1992) Kidney Int. , vol.41 , pp. 629-631
    • Chiquet, M.1
  • 76
    • 0027279247 scopus 로고
    • Differential expression of transmembrane proteoglycans in vascular smooth muscle cells
    • Cizmeci-Smith, G., R. C. Stahl, L. J. Showalter, and D. J. Carey. Differential expression of transmembrane proteoglycans in vascular smooth muscle cells. J. Biol. Chem. 268: 18740-18747, 1993.
    • (1993) J. Biol. Chem. , vol.268 , pp. 18740-18747
    • Cizmeci-Smith, G.1    Stahl, R.C.2    Showalter, L.J.3    Carey, D.J.4
  • 78
    • 0025472644 scopus 로고
    • 3H]thymidine incorporation does not correlate with growth state in cultured alveolar type II cells
    • 3H]thymidine incorporation does not correlate with growth state in cultured alveolar type II cells. Am. J. Respir. Cell Mol. Biol. 3: 159-164, 1990.
    • (1990) Am. J. Respir. Cell Mol. Biol. , vol.3 , pp. 159-164
    • Clement, A.1    Reidel, N.2    Brody, J.S.3
  • 79
    • 0023919959 scopus 로고
    • H-ras oncogene-transformed human bronchial epithelial cells (TBE-1) secrete a single metalloprotease capable of degrading basement membrane collagen
    • Collier, I. E., S. M. Wilhelm, A. Z. Eisen, B. L. Marmer, G. A. Grant, J. L. Seltzer, A. Kronberger, C. He, E. A. Bauer, and G. I. Goldberg. H-ras oncogene-transformed human bronchial epithelial cells (TBE-1) secrete a single metalloprotease capable of degrading basement membrane collagen. J. Biol. Chem. 263: 6579-6587, 1988.
    • (1988) J. Biol. Chem. , vol.263 , pp. 6579-6587
    • Collier, I.E.1    Wilhelm, S.M.2    Eisen, A.Z.3    Marmer, B.L.4    Grant, G.A.5    Seltzer, J.L.6    Kronberger, A.7    He, C.8    Bauer, E.A.9    Goldberg, G.I.10
  • 80
    • 0020549281 scopus 로고
    • Subunits of laminin are differentially synthesized in mouse eggs and early embryos
    • Cooper, A. R., and H. A. McQueen. Subunits of laminin are differentially synthesized in mouse eggs and early embryos. Dev. Biol. 96: 467-471, 1983.
    • (1983) Dev. Biol. , vol.96 , pp. 467-471
    • Cooper, A.R.1    McQueen, H.A.2
  • 81
    • 0024433474 scopus 로고
    • Modulation of bioelectric properties across alveolar type II cells by substratum
    • Cell Physiol. 26
    • Cott, G. R. Modulation of bioelectric properties across alveolar type II cells by substratum. Am. J. Physiol. 257 (Cell Physiol. 26): C678-C688, 1989.
    • (1989) Am. J. Physiol. , vol.257
    • Cott, G.R.1
  • 82
    • 0023551907 scopus 로고
    • The effect of substratum and serum on the lipid synthesis and morphology of alveolar type II cells in vitro
    • Cott, G. R., S. R. Walker, and R. J. Mason. The effect of substratum and serum on the lipid synthesis and morphology of alveolar type II cells in vitro. Exp. Lung Res. 13: 427-447, 1987.
    • (1987) Exp. Lung Res. , vol.13 , pp. 427-447
    • Cott, G.R.1    Walker, S.R.2    Mason, R.J.3
  • 85
    • 0025089518 scopus 로고
    • Pathobiology of pulmonary fibrosis
    • Lung Cell. Mol. Physiol. 3
    • Crouch, E. Pathobiology of pulmonary fibrosis. Am. J. Physiol. 259 (Lung Cell. Mol. Physiol. 3): L159-L184, 1990.
    • (1990) Am. J. Physiol. , vol.259
    • Crouch, E.1
  • 86
    • 0023091674 scopus 로고
    • Collagen-binding proteins secreted by type II pneumocytes in culture
    • Crouch, E., and W. Longmorc. Collagen-binding proteins secreted by type II pneumocytes in culture. Biochim. Biophys. Acta 924: 81-86, 1987.
    • (1987) Biochim. Biophys. Acta , vol.924 , pp. 81-86
    • Crouch, E.1    Longmorc, W.2
  • 87
    • 0023635442 scopus 로고
    • Synthesis of collagenous proteins by pulmonary type II epithelial cells
    • Crouch, E. C., M. A. Moxley, and W. Longmore. Synthesis of collagenous proteins by pulmonary type II epithelial cells. Am. Rev. Respir. Dis. 135: 1118-1123, 1987.
    • (1987) Am. Rev. Respir. Dis. , vol.135 , pp. 1118-1123
    • Crouch, E.C.1    Moxley, M.A.2    Longmore, W.3
  • 88
    • 0001290263 scopus 로고
    • Alveolar macrophages
    • edited by R. G. Crystal and J. B. West. New York: Raven
    • Crystal, R. G. Alveolar macrophages. In: The Lung, edited by R. G. Crystal and J. B. West. New York: Raven, 1991, p. 527-538.
    • (1991) The Lung , pp. 527-538
    • Crystal, R.G.1
  • 89
    • 0023471992 scopus 로고
    • Differential effects of γ-interferon on collagen and fibronectin gene expression
    • Czaja, M. J., F. R. Weiner, M. Eghbali, M.-A. Giambrone, M. Eghbali, and M. Zern. Differential effects of γ-interferon on collagen and fibronectin gene expression. J. Biol. Chem. 262: 13348-13351, 1987.
    • (1987) J. Biol. Chem. , vol.262 , pp. 13348-13351
    • Czaja, M.J.1    Weiner, F.R.2    Eghbali, M.3    Giambrone, M.-A.4    Eghbali, M.5    Zern, M.6
  • 90
    • 0026810547 scopus 로고
    • Distribution of integrin cell adhesion receptors in normal and malignant lung tissue
    • Damjanovich, L., S. M. Albeda, S. A. Mette, and C. A. Buck. Distribution of integrin cell adhesion receptors in normal and malignant lung tissue. Am. J. Respir. Cell Mol. Biol. 6: 197-206, 1992.
    • (1992) Am. J. Respir. Cell Mol. Biol. , vol.6 , pp. 197-206
    • Damjanovich, L.1    Albeda, S.M.2    Mette, S.A.3    Buck, C.A.4
  • 91
    • 0027490178 scopus 로고
    • Extracellular matrix 5: Adhesive interactions in early mammalian embryogenesis, implantation, and placentation
    • Damsky, C., A. Sutherland, and S. Fisher. Extracellular matrix 5: adhesive interactions in early mammalian embryogenesis, implantation, and placentation. FASEB J. 7: 1320-1329, 1993.
    • (1993) FASEB J. , vol.7 , pp. 1320-1329
    • Damsky, C.1    Sutherland, A.2    Fisher, S.3
  • 92
    • 0026938957 scopus 로고
    • Signal transduction by integrin receptors for extracellular matrix: Cooperative processing of extracellular information
    • Damsky, C. H., and Z. Werb. Signal transduction by integrin receptors for extracellular matrix: cooperative processing of extracellular information. Curr. Opin. Cell Biol. 4: 772-781, 1992.
    • (1992) Curr. Opin. Cell Biol. , vol.4 , pp. 772-781
    • Damsky, C.H.1    Werb, Z.2
  • 93
    • 0026826191 scopus 로고
    • Reactivity of alveolar epithelial cells in primary culture with type I monoclonal antibodies
    • Danto, S. I., S. M. Zabski, and E. D. Crandall. Reactivity of alveolar epithelial cells in primary culture with type I monoclonal antibodies. Am. J. Respir. Cell Mol. Biol. 6: 296-306, 1992.
    • (1992) Am. J. Respir. Cell Mol. Biol. , vol.6 , pp. 296-306
    • Danto, S.I.1    Zabski, S.M.2    Crandall, E.D.3
  • 94
    • 0028170987 scopus 로고
    • Late appearance of a type I alveolar epithelial cell marker during fetal rat lung development
    • Danto, S. I., S. M. Zabski, and E. D. Crandall. Late appearance of a type I alveolar epithelial cell marker during fetal rat lung development. Histochemistry 102: 297-304, 1994.
    • (1994) Histochemistry , vol.102 , pp. 297-304
    • Danto, S.I.1    Zabski, S.M.2    Crandall, E.D.3
  • 95
    • 0025614982 scopus 로고
    • Biochemistry and turnover of lung interstitium
    • Davidson, J. M. Biochemistry and turnover of lung interstitium. Eur. Respir. J. 3: 1048-1068, 1990.
    • (1990) Eur. Respir. J. , vol.3 , pp. 1048-1068
    • Davidson, J.M.1
  • 96
    • 0024693796 scopus 로고
    • Expression of the fibronectin gene
    • Dean, D. C. Expression of the fibronectin gene. Am. J. Respir. Cell Mol. Biol. 1: 5-10, 1989.
    • (1989) Am. J. Respir. Cell Mol. Biol. , vol.1 , pp. 5-10
    • Dean, D.C.1
  • 97
    • 0023729789 scopus 로고
    • Regulation of fibronectin biosynthesis by dexamethasone, transforming growth factor-β, and cAMP in human cell lines
    • Dean, D. C., R. F. Newby, and S. F. Bourgeois. Regulation of fibronectin biosynthesis by dexamethasone, transforming growth factor-β, and cAMP in human cell lines. J. Cell Biol. 106: 2159-2170, 1988.
    • (1988) J. Cell Biol. , vol.106 , pp. 2159-2170
    • Dean, D.C.1    Newby, R.F.2    Bourgeois, S.F.3
  • 98
    • 0025315789 scopus 로고
    • Cell adhesion, spreading and neunte stimulation by laminin fragment E8 depends on maintenance of secondary and tertiary structure in its rod and globular domain
    • Deutzmann, R., M. Aumailley, H. Wiedemann, W. Pysny, R. Timpl, and D. Edgar. Cell adhesion, spreading and neunte stimulation by laminin fragment E8 depends on maintenance of secondary and tertiary structure in its rod and globular domain. Eur. J. Biochem. 191: 513-522, 1990.
    • (1990) Eur. J. Biochem. , vol.191 , pp. 513-522
    • Deutzmann, R.1    Aumailley, M.2    Wiedemann, H.3    Pysny, W.4    Timpl, R.5    Edgar, D.6
  • 99
    • 0019444668 scopus 로고
    • Xenobiotic metabolism by alveolar type II cells isolated from rabbit lung
    • Devereux, T. R., and J. R. Fouts. Xenobiotic metabolism by alveolar type II cells isolated from rabbit lung. Biochem. Pharmacol. 30: 1231-1237, 1981.
    • (1981) Biochem. Pharmacol. , vol.30 , pp. 1231-1237
    • Devereux, T.R.1    Fouts, J.R.2
  • 100
    • 0019831185 scopus 로고
    • Identification of eytochrome P-450 lysozymes in nonciliated bronchiolar epithelial (Clara) and alveolar type 11 cells isolated from rabbit lung
    • Devereux, T. R., C. J. Serabjit-Singh, S. R. Slaughter, C. R. Wolf, R. M. Philpot, and J. R. Fouts. Identification of eytochrome P-450 lysozymes in nonciliated bronchiolar epithelial (Clara) and alveolar type 11 cells isolated from rabbit lung. Exp. Lung Res. 2: 221-230, 1981.
    • (1981) Exp. Lung Res. , vol.2 , pp. 221-230
    • Devereux, T.R.1    Serabjit-Singh, C.J.2    Slaughter, S.R.3    Wolf, C.R.4    Philpot, R.M.5    Fouts, J.R.6
  • 101
    • 0028446566 scopus 로고
    • The dynamic regulation of integrin adhesiveness
    • Diamond, M. S., and T. A. Springer. The dynamic regulation of integrin adhesiveness. Curr. Biol. 4: 506-517, 1994.
    • (1994) Curr. Biol. , vol.4 , pp. 506-517
    • Diamond, M.S.1    Springer, T.A.2
  • 102
    • 0017666978 scopus 로고
    • The type II epithelial cells of the lung. IV. Adaptation and behavior of isolated type II cells in culture
    • Diglio, C. A., and Y. Kikkawa. The type II epithelial cells of the lung. IV. Adaptation and behavior of isolated type II cells in culture. Lab. Invest. 37: 622-631, 1977.
    • (1977) Lab. Invest. , vol.37 , pp. 622-631
    • Diglio, C.A.1    Kikkawa, Y.2
  • 103
    • 0023676511 scopus 로고
    • The neurite-promoting domain of human laminin promotes attachment and induces characteristic morphology in non-neuronal cells
    • Dillner, L., K. Dickerson, M. Manthorpe, E. Ruoslahti, and E. Engvall. The neurite-promoting domain of human laminin promotes attachment and induces characteristic morphology in non-neuronal cells. Exp. Cell Res. 177: 186-198, 1988.
    • (1988) Exp. Cell Res. , vol.177 , pp. 186-198
    • Dillner, L.1    Dickerson, K.2    Manthorpe, M.3    Ruoslahti, E.4    Engvall, E.5
  • 104
    • 0025813282 scopus 로고
    • The extracellular matrix coordinately modulates liver transcription factors and hepatocyte morphology
    • DiPersio, C. M., D. A. Jackson, and K. S. Zaret. The extracellular matrix coordinately modulates liver transcription factors and hepatocyte morphology. Mol. Cell Biol. 11: 4405-4414, 1991.
    • (1991) Mol. Cell Biol. , vol.11 , pp. 4405-4414
    • DiPersio, C.M.1    Jackson, D.A.2    Zaret, K.S.3
  • 105
    • 0025231434 scopus 로고
    • Isolation and culture of alveolar type II cells
    • Lung Cell. MoL Physiol. 2
    • Dobbs, L. G. Isolation and culture of alveolar type II cells. Am. J. Physiol. 258 (Lung Cell. MoL Physiol. 2): L134-L137, 1990.
    • (1990) Am. J. Physiol. , vol.258
    • Dobbs, L.G.1
  • 106
    • 0021858647 scopus 로고
    • Changes in biochemical characteristics and pattern of lectin binding of alveolar type II cells with time in culture
    • Dobbs, L. G., M. C. Williams, and A. E. Brandt. Changes in biochemical characteristics and pattern of lectin binding of alveolar type II cells with time in culture. Biochim. Biophys. Acta 846: 155-166, 1985.
    • (1985) Biochim. Biophys. Acta , vol.846 , pp. 155-166
    • Dobbs, L.G.1    Williams, M.C.2    Brandt, A.E.3
  • 107
    • 0023938081 scopus 로고
    • Monoclonal antibodies specific to apical surfaces of rat alveolar type I cells bind to surfaces of cultured, but not freshly isolated, type II cells
    • Dobbs, L. G., M. C. Williams, and R. Gonzalez. Monoclonal antibodies specific to apical surfaces of rat alveolar type I cells bind to surfaces of cultured, but not freshly isolated, type II cells. Biochim. Biophys. Acta 970: 146-156, 1988.
    • (1988) Biochim. Biophys. Acta , vol.970 , pp. 146-156
    • Dobbs, L.G.1    Williams, M.C.2    Gonzalez, R.3
  • 108
    • 0026318443 scopus 로고
    • The expression of the genes for entactin, laminin A, laminin B1 and laminin B2 in murine lens morphogenesis and eye development
    • Dong, L. J., and A. E. Chung. The expression of the genes for entactin, laminin A, laminin B1 and laminin B2 in murine lens morphogenesis and eye development. Differentiation 48: 157-172, 1991.
    • (1991) Differentiation , vol.48 , pp. 157-172
    • Dong, L.J.1    Chung, A.E.2
  • 109
    • 0028925241 scopus 로고
    • Turnover of extracellular matrix by type II pulmonary epithelial cells
    • Lung Cell. Mol. Physiol. 12
    • Dunsmore, S. E., and D. E. Rannels. Turnover of extracellular matrix by type II pulmonary epithelial cells. Am. J. Physiol. 268 (Lung Cell. Mol. Physiol. 12): L336-L346, 1995.
    • (1995) Am. J. Physiol. , vol.268
    • Dunsmore, S.E.1    Rannels, D.E.2
  • 110
    • 0023016638 scopus 로고
    • Control of laminin synthesis during differentiation of F9 embryonal carcinoma cells. A study using cDNA clones complementary to the mRNA species for the A, B1, and B2 subunits
    • Durkin, M. E., S. L. Phillips, and A. E. Chung. Control of laminin synthesis during differentiation of F9 embryonal carcinoma cells. A study using cDNA clones complementary to the mRNA species for the A, B1, and B2 subunits. Differentiation 32: 260-266, 1986.
    • (1986) Differentiation , vol.32 , pp. 260-266
    • Durkin, M.E.1    Phillips, S.L.2    Chung, A.E.3
  • 111
    • 0022135312 scopus 로고
    • Identification and interaction repertoire of large forms of the basement membrane protein nidogen
    • Dziadek, M., M. Paulsson, and R. Timpl. Identification and interaction repertoire of large forms of the basement membrane protein nidogen. EMBO J. 4: 2513-2518, 1985.
    • (1985) EMBO J. , vol.4 , pp. 2513-2518
    • Dziadek, M.1    Paulsson, M.2    Timpl, R.3
  • 112
    • 0023696879 scopus 로고
    • Alkaline phosphatase: A marker of alveolar type II cell differentiation
    • Edelson, J. D., J. M. Shannon, and R. J. Mason. Alkaline phosphatase: a marker of alveolar type II cell differentiation. Am. Rev. Respir. Dis. 138: 1268-1275, 1988.
    • (1988) Am. Rev. Respir. Dis. , vol.138 , pp. 1268-1275
    • Edelson, J.D.1    Shannon, J.M.2    Mason, R.J.3
  • 113
    • 0024414531 scopus 로고
    • Effects of two extracellular matrices on morphologic and biochemical properties of human type II cells in vitro
    • Edelson, J. D., J. M. Shannon, and R. J. Mason. Effects of two extracellular matrices on morphologic and biochemical properties of human type II cells in vitro. Am. Rev. Respir. Dis. 140: 1398-1404, 1989.
    • (1989) Am. Rev. Respir. Dis. , vol.140 , pp. 1398-1404
    • Edelson, J.D.1    Shannon, J.M.2    Mason, R.J.3
  • 116
    • 0023869858 scopus 로고
    • Regulation of human lung fibroblast glycosaminoglycan production by recombinant interferons, tumor necrosis factor, and lymphotoxin
    • Elias, J. A., R. C. Krol, B. Freundlich, and P. M. Sampson. Regulation of human lung fibroblast glycosaminoglycan production by recombinant interferons, tumor necrosis factor, and lymphotoxin. J. Clin. Invest. 81: 326-333, 1986.
    • (1986) J. Clin. Invest. , vol.81 , pp. 326-333
    • Elias, J.A.1    Krol, R.C.2    Freundlich, B.3    Sampson, P.M.4
  • 117
    • 0026442649 scopus 로고
    • Laminins and other strange proteins
    • Engel, J. Laminins and other strange proteins. Biochemistry 31: 10643-10651, 1992.
    • (1992) Biochemistry , vol.31 , pp. 10643-10651
    • Engel, J.1
  • 118
    • 0019888221 scopus 로고
    • Shapes, domain organization and flexibility of laminin and fibronectin, two multifunctional proteins of the extracellular matrix
    • Engel, J., E. Odermat, A. Engel, J.A. Madri, H. Furthmayr, H. Rohde, and R. Timpl. Shapes, domain organization and flexibility of laminin and fibronectin, two multifunctional proteins of the extracellular matrix. J. Mol. Biol. 150: 97-120, 1981.
    • (1981) J. Mol. Biol. , vol.150 , pp. 97-120
    • Engel, J.1    Odermat, E.2    Engel, A.3    Madri, J.A.4    Furthmayr, H.5    Rohde, H.6    Timpl, R.7
  • 119
    • 0023033082 scopus 로고
    • Mapping of domains in human laminin using monoclonal antibodies: Localization of the neuritepromoting site
    • Engvall, E., G. E. Davis, K. Dickerson, E. Ruoslahti, S. Varon, and M. Manthorpe. Mapping of domains in human laminin using monoclonal antibodies: localization of the neuritepromoting site. J. Cell Biol. 103: 2457-2465, 1986.
    • (1986) J. Cell Biol. , vol.103 , pp. 2457-2465
    • Engvall, E.1    Davis, G.E.2    Dickerson, K.3    Ruoslahti, E.4    Varon, S.5    Manthorpe, M.6
  • 120
    • 0025494189 scopus 로고
    • Distribution and isolation of four laminin variants; tissue restricted distribution of heterotrimers assembled from five different subunits
    • Engvall, E., D. Earwicker, T. Haaparanta, E. Ruoslahti, and J. R. Sanes. Distribution and isolation of four laminin variants; tissue restricted distribution of heterotrimers assembled from five different subunits. Cell Regul. 1: 731-740, 1990.
    • (1990) Cell Regul. , vol.1 , pp. 731-740
    • Engvall, E.1    Earwicker, D.2    Haaparanta, T.3    Ruoslahti, E.4    Sanes, J.R.5
  • 121
    • 0024441046 scopus 로고
    • Tenascin: An extracellular matrix protein prominent in specialized embryonic tissues and tumors
    • Erikson, H. P. Tenascin: an extracellular matrix protein prominent in specialized embryonic tissues and tumors. Annu. Rev. Cell Biol. 5: 71-92, 1989.
    • (1989) Annu. Rev. Cell Biol. , vol.5 , pp. 71-92
    • Erikson, H.P.1
  • 122
    • 0027685702 scopus 로고
    • Tenascin-C, tenascin-R and tenascin-X: A family of talented proteins in search of functions
    • Erickson, H. P. Tenascin-C, tenascin-R and tenascin-X: a family of talented proteins in search of functions. Curr. Opin. Cell Biol. 5: 869-876, 1993.
    • (1993) Curr. Opin. Cell Biol. , vol.5 , pp. 869-876
    • Erickson, H.P.1
  • 126
    • 0023696859 scopus 로고
    • Cloning of full-length elastin cDNAs from a human skin fibroblast recombinant cDNA library: Further elucidation of alternative splicing using exon-specific probes
    • Fazio, M. J., D. R. Olsen, E. A. Kauh, C. T. Baldwin, Z. Indik, N. Ornstein-Goldstein, H. Yeh, J. Rosenbloom, and J. Uitto. Cloning of full-length elastin cDNAs from a human skin fibroblast recombinant cDNA library: further elucidation of alternative splicing using exon-specific probes. J. Invest. Dermatol. 91: 458-464, 1988.
    • (1988) J. Invest. Dermatol. , vol.91 , pp. 458-464
    • Fazio, M.J.1    Olsen, D.R.2    Kauh, E.A.3    Baldwin, C.T.4    Indik, Z.5    Ornstein-Goldstein, N.6    Yeh, H.7    Rosenbloom, J.8    Uitto, J.9
  • 127
    • 0023948122 scopus 로고
    • Isolation and characterization of human elastin cDNAs, and age-associated variation in elastin gene expression in cultured skin fibroblasts
    • Fazio, M. J., D. R. Olsen, H. Kuivaniemi, M. L. Chu, J. M. Davidson, J. Rosenbloom, and J. Uitto. Isolation and characterization of human elastin cDNAs, and age-associated variation in elastin gene expression in cultured skin fibroblasts. Lab. Invest. 58: 270-277, 1988.
    • (1988) Lab. Invest. , vol.58 , pp. 270-277
    • Fazio, M.J.1    Olsen, D.R.2    Kuivaniemi, H.3    Chu, M.L.4    Davidson, J.M.5    Rosenbloom, J.6    Uitto, J.7
  • 128
    • 0025039113 scopus 로고
    • Extracellular matrix biosynthesis by cultured fetal rat lung epithelial cells II. Effects of acute exposure to epidermal growth factor and retinoic acid on collagen biosynthesis
    • Federspiel, S. J., S. J. DiMari, M. L. Guerry-Force, and M. A. Haralson. Extracellular matrix biosynthesis by cultured fetal rat lung epithelial cells II. Effects of acute exposure to epidermal growth factor and retinoic acid on collagen biosynthesis. Lab. Invest. 63: 455-466, 1990.
    • (1990) Lab. Invest. , vol.63 , pp. 455-466
    • Federspiel, S.J.1    DiMari, S.J.2    Guerry-Force, M.L.3    Haralson, M.A.4
  • 129
    • 0026376742 scopus 로고
    • Extracellular matrix biosynthesis by cultured fetal rat lung epithelial cells. III. Effects of chronic exposure to epidermal growth factor on growth, differentiation, and collagen biosynthesis
    • Federspiel, S. J., S. J. DiMari, A. M. Howe, M. L. Guerry-Force, and M. A. Haralson. Extracellular matrix biosynthesis by cultured fetal rat lung epithelial cells. III. Effects of chronic exposure to epidermal growth factor on growth, differentiation, and collagen biosynthesis. Lab. Invest. 64: 463-473, 1991.
    • (1991) Lab. Invest. , vol.64 , pp. 463-473
    • Federspiel, S.J.1    Dimari, S.J.2    Howe, A.M.3    Guerry-Force, M.L.4    Haralson, M.A.5
  • 130
    • 0025837364 scopus 로고
    • Extracellular matrix biosynthesis by cultured fetal rat lung epithelial cells. IV. Effects of chronic exposure to retinoic acid on growth, differentiation, and collagen biosynthesis
    • Federspiel, S. J., S. J. DiMari, A. M. Howe, M. L. Guerry-Force, and M. A. Haralson. Extracellular matrix biosynthesis by cultured fetal rat lung epithelial cells. IV. Effects of chronic exposure to retinoic acid on growth, differentiation, and collagen biosynthesis. Lab. Invest. 65: 441-450, 1991.
    • (1991) Lab. Invest. , vol.65 , pp. 441-450
    • Federspiel, S.J.1    Dimari, S.J.2    Howe, A.M.3    Guerry-Force, M.L.4    Haralson, M.A.5
  • 132
    • 0025650939 scopus 로고
    • Mechanisms for organization of fibronectin matrix
    • Fogerty, F. J., and D. F. Mosher. Mechanisms for organization of fibronectin matrix. Cell Differ. Dev. 32: 439-450, 1990.
    • (1990) Cell Differ. Dev. , vol.32 , pp. 439-450
    • Fogerty, F.J.1    Mosher, D.F.2
  • 133
    • 0023831047 scopus 로고
    • A heparin-binding angiogenic protein - Basic fibroblast growth factor - is stored within basement membrane
    • Folkman, J., M. Klagsburn, J. Sasse, M. Wadzinski, D. Ingber, and I. Vlodavsky. A heparin-binding angiogenic protein - basic fibroblast growth factor - is stored within basement membrane. Am. J. Pathol. 130: 393-400, 1988.
    • (1988) Am. J. Pathol. , vol.130 , pp. 393-400
    • Folkman, J.1    Klagsburn, M.2    Sasse, J.3    Wadzinski, M.4    Ingber, D.5    Vlodavsky, I.6
  • 136
    • 0027156258 scopus 로고
    • Fetal rat lung type II cell differentiation in serum-free isolated cell culture, modulation and inhibition
    • Lung Cell. Mol. Physiol. 8
    • Fraslon, C., T. Lacaze-Masmonteil, V. Zupan, B. Chailley-Heu, and J. R. Bourbon. Fetal rat lung type II cell differentiation in serum-free isolated cell culture, modulation and inhibition. Am. J. Physiol. 264 (Lung Cell. Mol. Physiol. 8): L504-L516, 1993.
    • (1993) Am. J. Physiol. , vol.264
    • Fraslon, C.1    Lacaze-Masmonteil, T.2    Zupan, V.3    Chailley-Heu, B.4    Bourbon, J.R.5
  • 137
    • 0028322352 scopus 로고
    • Molecular cloning and expression of collagenase-3, a novel human matrix metalloproteinase produced by breast carcinomas
    • Freije, J. M., I. Diez-Itza, M. Balbin, L. M. Sanchez, R. Blasco, J. Tolivia, and C. Lopez-Otin. Molecular cloning and expression of collagenase-3, a novel human matrix metalloproteinase produced by breast carcinomas. J. Biol. Chem. 269: 16766-16773, 1994.
    • (1994) J. Biol. Chem. , vol.269 , pp. 16766-16773
    • Freije, J.M.1    Diez-Itza, I.2    Balbin, M.3    Sanchez, L.M.4    Blasco, R.5    Tolivia, J.6    Lopez-Otin, C.7
  • 138
    • 0024344620 scopus 로고
    • Reappearance of an embryonic pattern of fibronectin splicing during wound healing in the adult rat
    • French-Constant, C., L. Van de Water, H. F. Dvorak, and R. O. Hynes. Reappearance of an embryonic pattern of fibronectin splicing during wound healing in the adult rat. J. Cell Biol. 109: 903-914, 1989.
    • (1989) J. Cell Biol. , vol.109 , pp. 903-914
    • French-Constant, C.1    Van De Water, L.2    Dvorak, H.F.3    Hynes, R.O.4
  • 139
    • 0023112112 scopus 로고
    • Soluble antigen induces T lymphocytes to secrete an endoglycosidase that degrades the heparan sulfate moiety of subendothelial extracellular matrix
    • Fridman, R., O. Lider, Y. Naparstek, Z. Fuks, I. Vlodavsky, and I. R. Cohen. Soluble antigen induces T lymphocytes to secrete an endoglycosidase that degrades the heparan sulfate moiety of subendothelial extracellular matrix. J. Cell. Physiol. 130: 85-92, 1987.
    • (1987) J. Cell. Physiol. , vol.130 , pp. 85-92
    • Fridman, R.1    Lider, O.2    Naparstek, Y.3    Fuks, Z.4    Vlodavsky, I.5    Cohen, I.R.6
  • 140
    • 0028817083 scopus 로고
    • Significance of early intra-alveolar fibrotic lesions and integrin expression in lung biopsy specimens from patients with idiopathic pulmonary fibrosis
    • Fukuda, Y., F. Basset, V. J. Ferrans, and N. Yamanaka. Significance of early intra-alveolar fibrotic lesions and integrin expression in lung biopsy specimens from patients with idiopathic pulmonary fibrosis. Hum. Pathol. 26: 53-61, 1995.
    • (1995) Hum. Pathol. , vol.26 , pp. 53-61
    • Fukuda, Y.1    Basset, F.2    Ferrans, V.J.3    Yamanaka, N.4
  • 141
    • 0025796896 scopus 로고
    • The p146 type II alveolar epithelial cell antigen is identical to aminopeptidase N
    • Lung Cell. Mol. Physiol. 4
    • Funkhouser, J. D., S. D. Tangada, M. Jones, S.-J. O, and R. D. A. Peterson. The p146 type II alveolar epithelial cell antigen is identical to aminopeptidase N. Am. J. Physiol. 260 (Lung Cell. Mol. Physiol. 4): L274-L279, 1991.
    • (1991) Am. J. Physiol. , vol.260
    • Funkhouser, J.D.1    Tangada, S.D.2    Jones, M.3    O., S.-J.4    Peterson, R.D.A.5
  • 142
    • 0025799399 scopus 로고
    • Ectopeptidases of the alveolar epithelium: Candidates for roles in alveolar regulatory mechanisms
    • Lung Cell. Mol. Physiol. 4
    • Funkhouser, J. D., S. D. Tangada, and R. D. A. Peterson. Ectopeptidases of the alveolar epithelium: candidates for roles in alveolar regulatory mechanisms. Am. J. Physiol. 260 (Lung Cell. Mol. Physiol. 4): L381-L385, 1991.
    • (1991) Am. J. Physiol. , vol.260
    • Funkhouser, J.D.1    Tangada, S.D.2    Peterson, R.D.A.3
  • 143
    • 0027397492 scopus 로고
    • Molecular characterization and in situ mRNA localization of the neural recognition molecule JI-160/180: A modular structure similar to tenascin
    • Fuss, B., E.-S. Wintergerst, U. Bartsch, and M. Schachner. Molecular characterization and in situ mRNA localization of the neural recognition molecule JI-160/180: a modular structure similar to tenascin. J. Cell Biol. 120: 1237-1249, 1993.
    • (1993) J. Cell Biol. , vol.120 , pp. 1237-1249
    • Fuss, B.1    Wintergerst, E.-S.2    Bartsch, U.3    Schachner, M.4
  • 144
    • 0020560675 scopus 로고
    • Cells of the lung: Biology and clinical implications
    • Gail, D. B., and C. J. M. Lenfant. Cells of the lung: biology and clinical implications. Am. Rev. Respir. Dis. 127: 366-387, 1983.
    • (1983) Am. Rev. Respir. Dis. , vol.127 , pp. 366-387
    • Gail, D.B.1    Lenfant, C.J.M.2
  • 145
    • 0027990415 scopus 로고
    • Wound repair in the context of extracellular matrix
    • Gailit, J., and R. A. Clark. Wound repair in the context of extracellular matrix. Curr. Opin. Cell Biol. 6: 717-725, 1994.
    • (1994) Curr. Opin. Cell Biol. , vol.6 , pp. 717-725
    • Gailit, J.1    Clark, R.A.2
  • 146
    • 0026351954 scopus 로고
    • EGF and TGF-α influence in vitro lung development by the induction of matrix-degrading metalloproteinases
    • Ganser, G. L., G. P. Stricklin, and L. M. Matrisian. EGF and TGF-α influence in vitro lung development by the induction of matrix-degrading metalloproteinases. Int. J. Dev. Biol. 35: 453-461, 1991.
    • (1991) Int. J. Dev. Biol. , vol.35 , pp. 453-461
    • Ganser, G.L.1    Stricklin, G.P.2    Matrisian, L.M.3
  • 147
    • 0019180191 scopus 로고
    • Primary culture of rat alveolar type II cells on floating collagen membranes
    • Geppert, E. F., M. C. Williams, and R. J. Mason. Primary culture of rat alveolar type II cells on floating collagen membranes. Exp. Cell Res. 128: 363-374, 1980.
    • (1980) Exp. Cell Res. , vol.128 , pp. 363-374
    • Geppert, E.F.1    Williams, M.C.2    Mason, R.J.3
  • 148
    • 0025887137 scopus 로고
    • Complementary DNA cloning establishes microfibril-associated glycoprotein (MAGP) to be a discrete component of the elastin-associated microfibrils
    • Gibson, M. A., L. B. Sandberg, L. E. Grosso, and E. G. Cleary. Complementary DNA cloning establishes microfibril-associated glycoprotein (MAGP) to be a discrete component of the elastin-associated microfibrils. J. Biol. Chem. 266: 7596-7601, 1991.
    • (1991) J. Biol. Chem. , vol.266 , pp. 7596-7601
    • Gibson, M.A.1    Sandberg, L.B.2    Grosso, L.E.3    Cleary, E.G.4
  • 149
    • 0021328415 scopus 로고
    • The connective tissue of the rat lung: Electron immunohistochemical studies
    • Gil, J., and A. Martinez-Hernadez. The connective tissue of the rat lung: electron immunohistochemical studies. J. Histochem. Cytochem. 32: 230-238, 1984.
    • (1984) J. Histochem. Cytochem. , vol.32 , pp. 230-238
    • Gil, J.1    Martinez-Hernadez, A.2
  • 150
    • 0021088441 scopus 로고
    • Receptor-mediated endocytosis of proteoglycans by human fibroblasts involves recognition of the protein core
    • Glossl, J., R. Schubert-Prinz, J. D. Gregory, S. P. Damle, K. von Figura, and H. Kresse. Receptor-mediated endocytosis of proteoglycans by human fibroblasts involves recognition of the protein core. Biochem. J. 215: 295-301, 1983.
    • (1983) Biochem. J. , vol.215 , pp. 295-301
    • Glossl, J.1    Schubert-Prinz, R.2    Gregory, J.D.3    Damle, S.P.4    Von Figura, K.5    Kresse, H.6
  • 152
    • 0014249634 scopus 로고
    • The demonstration of acid hydrolase activities in the inclusion bodies of type II alveolar cells and other lysosomes in the rabbit lung
    • Goldfisher, S., Y. Kikkawa, and L. Hoffman. The demonstration of acid hydrolase activities in the inclusion bodies of type II alveolar cells and other lysosomes in the rabbit lung. J. Histochem. Cytochem. 16: 102-109, 1968.
    • (1968) J. Histochem. Cytochem. , vol.16 , pp. 102-109
    • Goldfisher, S.1    Kikkawa, Y.2    Hoffman, L.3
  • 153
    • 0023666132 scopus 로고
    • Identification of an amino acid sequence in laminin mediating cell attachment, chemotaxis and receptor binding
    • Graf, J., Y. Iwamoto, M. Sasaki, G. R. Martin, H. K. Kleinman, F. A. Robey, and Y. Yamada. Identification of an amino acid sequence in laminin mediating cell attachment, chemotaxis and receptor binding. Cell 48: 989-996, 1987.
    • (1987) Cell , vol.48 , pp. 989-996
    • Graf, J.1    Iwamoto, Y.2    Sasaki, M.3    Martin, G.R.4    Kleinman, H.K.5    Robey, F.A.6    Yamada, Y.7
  • 154
    • 0024543811 scopus 로고
    • Incubation of laminin, collagen IV, and heparan sulfate proteoglycan at 35°C yields basement membrane-like structures
    • Grant, D. S., C. P. Leblond, H. K. Kleinman, S. Inoue, and J. R. Hassell. Incubation of laminin, collagen IV, and heparan sulfate proteoglycan at 35°C yields basement membrane-like structures. J. Cell Biol. 108: 1567-1574, 1989.
    • (1989) J. Cell Biol. , vol.108 , pp. 1567-1574
    • Grant, D.S.1    Leblond, C.P.2    Kleinman, H.K.3    Inoue, S.4    Hassell, J.R.5
  • 155
    • 0020537152 scopus 로고
    • Alterations in lung basement membrane during fetal growth and type 2 cell development
    • Grant, M. M., N. R. Cutts, and J. S. Brody. Alterations in lung basement membrane during fetal growth and type 2 cell development. Dev. Biol. 97: 173-183, 1983.
    • (1983) Dev. Biol. , vol.97 , pp. 173-183
    • Grant, M.M.1    Cutts, N.R.2    Brody, J.S.3
  • 156
    • 0026748853 scopus 로고
    • Requirements for extracellular metabolism of pulmonary surfactant: Tentative identification of serine protease
    • Lung Cell. Mol. Physiol. 6
    • Gross, N. J., and R. M. Schultz. Requirements for extracellular metabolism of pulmonary surfactant: tentative identification of serine protease. Am. J. Physiol. 262 (Lung Cell. Mol. Physiol. 6): L446-L453, 1992.
    • (1992) Am. J. Physiol. , vol.262
    • Gross, N.J.1    Schultz, R.M.2
  • 157
    • 0025513634 scopus 로고
    • Expression of urokinase-type plasminogen activator by rat pulmonary epithelial cells
    • Gross, T. J., R. H. Simon, and R. G. Sitrin. Expression of urokinase-type plasminogen activator by rat pulmonary epithelial cells. Am. J. Respir. Cell Mol. Biol. 3: 449-456, 1990.
    • (1990) Am. J. Respir. Cell Mol. Biol. , vol.3 , pp. 449-456
    • Gross, T.J.1    Simon, R.H.2    Sitrin, R.G.3
  • 158
    • 0025911199 scopus 로고
    • Rat alveolar epithelial cells concomitantly express plasminogen activator inhibitor-1 and urokinase
    • Lung Cell. Mol. Physiol. 4
    • Gross, T. J., R. H. Simon, C. J. Kelly, and R. G. Sitrin. Rat alveolar epithelial cells concomitantly express plasminogen activator inhibitor-1 and urokinase. Am. J. Physiol. 260 (Lung Cell. Mol. Physiol. 4): L286-L295, 1991.
    • (1991) Am. J. Physiol. , vol.260
    • Gross, T.J.1    Simon, R.H.2    Kelly, C.J.3    Sitrin, R.G.4
  • 159
    • 0028349213 scopus 로고
    • ICAM-1 and integrin expression on isolated human alveolar type II pneumocytes
    • Guzman, J., T. Isumi, S. Nagai, and U. Costabel. ICAM-1 and integrin expression on isolated human alveolar type II pneumocytes. Eur. Respir. J. 7: 736-739, 1994.
    • (1994) Eur. Respir. J. , vol.7 , pp. 736-739
    • Guzman, J.1    Isumi, T.2    Nagai, S.3    Costabel, U.4
  • 160
    • 0028142840 scopus 로고
    • Integrin-ligand interactions: A year in review
    • Haas, T. A., and E. F. Plow. Integrin-ligand interactions: a year in review. Curr. Opin. Cell Biol. 6. 656-662, 1994.
    • (1994) Curr. Opin. Cell Biol. , vol.6 , pp. 656-662
    • Haas, T.A.1    Plow, E.F.2
  • 162
    • 0017237086 scopus 로고
    • Lung collagen heterogeneity. II. Synthesis of type I and 111 collagen by rabbit and human lung cells in culture
    • Hance, A. J., K. Bradley, and R. G. Crystal. Lung collagen heterogeneity. II. Synthesis of type I and 111 collagen by rabbit and human lung cells in culture. J. Clin. Invest. 57: 102-111, 1976.
    • (1976) J. Clin. Invest. , vol.57 , pp. 102-111
    • Hance, A.J.1    Bradley, K.2    Crystal, R.G.3
  • 163
    • 0016712601 scopus 로고
    • The connective tissue of the lung
    • Hance, A. J., and R. G. Crystal. The connective tissue of the lung. Am. Rev. Respir. Dis. 112: 657-709, 1975.
    • (1975) Am. Rev. Respir. Dis. , vol.112 , pp. 657-709
    • Hance, A.J.1    Crystal, R.G.2
  • 164
    • 0026507880 scopus 로고
    • Proteoglycans: Many forms and many functions
    • Hardingham, T. E., and A. J. Fosang. Proteoglycans: many forms and many functions. FASEB J. 6: 861-870, 1992.
    • (1992) FASEB J. , vol.6 , pp. 861-870
    • Hardingham, T.E.1    Fosang, A.J.2
  • 165
    • 0028323227 scopus 로고
    • The structure, function and turnover of aggrecan, the large aggregating proteoglycan from cartilage
    • Hardingham, T. E., A. J. Fosang, and J. Dudhia. The structure, function and turnover of aggrecan, the large aggregating proteoglycan from cartilage. Eur. J. Clin. Chem. Clin. Biochem. 32: 249-257, 1994.
    • (1994) Eur. J. Clin. Chem. Clin. Biochem. , vol.32 , pp. 249-257
    • Hardingham, T.E.1    Fosang, A.J.2    Dudhia, J.3
  • 166
    • 0026113636 scopus 로고
    • Rat lung type I epithelial cell injury and response to hyperoxia
    • Harris, J. B., L.-Y. Chang, and J. D. Crapo. Rat lung type I epithelial cell injury and response to hyperoxia. Am. J. Respir. Cell Mol. Biol. 4: 115-125, 1991.
    • (1991) Am. J. Respir. Cell Mol. Biol. , vol.4 , pp. 115-125
    • Harris, J.B.1    Chang, L.-Y.2    Crapo, J.D.3
  • 167
    • 0024276076 scopus 로고
    • The N terminus of laminin A chain is homologous to the B chains
    • Hartl, L., I. Oberbaumer, and R. Deutzmann. The N terminus of laminin A chain is homologous to the B chains. Eur. J. Biochem. 173: 629-635, 1988.
    • (1988) Eur. J. Biochem. , vol.173 , pp. 629-635
    • Hartl, L.1    Oberbaumer, I.2    Deutzmann, R.3
  • 168
    • 0028241699 scopus 로고
    • Laminin peptides stimulate human neutrophil motility
    • Harvath, L., N. E. Brownson, G. B. Fields, and A. P. Skubitz. Laminin peptides stimulate human neutrophil motility. J. Immunol. 152: 5447-5456, 1994.
    • (1994) J. Immunol. , vol.152 , pp. 5447-5456
    • Harvath, L.1    Brownson, N.E.2    Fields, G.B.3    Skubitz, A.P.4
  • 169
    • 0026764872 scopus 로고
    • Endocytosis of different members of the small chondroitin/dermatan sulfate proteoglycan family
    • Hausser, H., B. Ober, E. Quentin-Hoffmann, B. Schmidt, and H. Kresse. Endocytosis of different members of the small chondroitin/dermatan sulfate proteoglycan family. J. Biol. Chem. 267: 11559-11564, 1992.
    • (1992) J. Biol. Chem. , vol.267 , pp. 11559-11564
    • Hausser, H.1    Ober, B.2    Quentin-Hoffmann, E.3    Schmidt, B.4    Kresse, H.5
  • 170
    • 0027421896 scopus 로고
    • Influence of membrane-associated heparan sulfate on the internalization of the small proteoglycan decorin
    • Hausser, H., O. Witt, and H. Kresse. Influence of membrane-associated heparan sulfate on the internalization of the small proteoglycan decorin. Exp. Cell Res. 208: 398-406, 1993.
    • (1993) Exp. Cell Res. , vol.208 , pp. 398-406
    • Hausser, H.1    Witt, O.2    Kresse, H.3
  • 171
    • 0025323820 scopus 로고
    • Colocalization of TGF-β 1 and collagen I and III, fibronectin, and glycosaminoglycans during lung branching morphogenesis
    • Heine, U. L., E. F. Munoz, K. C. Flanders, A. B. Roberts, and M. B. Sporn. Colocalization of TGF-β 1 and collagen I and III, fibronectin, and glycosaminoglycans during lung branching morphogenesis. Development 109: 29-36, 1990.
    • (1990) Development , vol.109 , pp. 29-36
    • Heine, U.L.1    Munoz, E.F.2    Flanders, K.C.3    Roberts, A.B.4    Sporn, M.B.5
  • 172
    • 0020031151 scopus 로고
    • Covalent crosslinking between molecules of type I and type III collagen
    • Henkel, W., and R. W. Glanville. Covalent crosslinking between molecules of type I and type III collagen. Eur. J. Biochem. 122: 205-213, 1982.
    • (1982) Eur. J. Biochem. , vol.122 , pp. 205-213
    • Henkel, W.1    Glanville, R.W.2
  • 174
    • 0023935698 scopus 로고
    • Heparan sulfate proteoglycan from the extracellular matrix of human lung fibroblasts. Isolation, purification, and core protein characterization
    • Heremans, A., J. J. Cassiman, H. van den Berghe, and G. David. Heparan sulfate proteoglycan from the extracellular matrix of human lung fibroblasts. Isolation, purification, and core protein characterization. J. Biol. Chem. 263: 4731-4739, 1988.
    • (1988) J. Biol. Chem. , vol.263 , pp. 4731-4739
    • Heremans, A.1    Cassiman, J.J.2    Van Den Berghe, H.3    David, G.4
  • 175
    • 0017855668 scopus 로고
    • Extracellular hydrolases of the lung
    • Hook, G. E. R. Extracellular hydrolases of the lung. Biochemistry 17: 520-528, 1978.
    • (1978) Biochemistry , vol.17 , pp. 520-528
    • Hook, G.E.R.1
  • 176
    • 0020315229 scopus 로고
    • Hydrolases of pulmonary lysosomes and lamellar bodies
    • Hook, G. E. R., and L. B. Gilmore. Hydrolases of pulmonary lysosomes and lamellar bodies. J. Biol. Chem. 257: 9211-9220, 1982.
    • (1982) J. Biol. Chem. , vol.257 , pp. 9211-9220
    • Hook, G.E.R.1    Gilmore, L.B.2
  • 177
    • 0023875706 scopus 로고
    • Degradation of endocytosed dermatan sulfate in human fibroblasts
    • Hoppe, W., U. Rauch, and H. Kresse. Degradation of endocytosed dermatan sulfate in human fibroblasts. J. Biol. Chem. 263: 5926-5932, 1988.
    • (1988) J. Biol. Chem. , vol.263 , pp. 5926-5932
    • Hoppe, W.1    Rauch, U.2    Kresse, H.3
  • 178
    • 0018114089 scopus 로고
    • Composite epithelial and endothelial basal laminas in human lungs
    • Huang, T. W. Composite epithelial and endothelial basal laminas in human lungs. Am. J. Pathol. 93: 681-687, 1978.
    • (1978) Am. J. Pathol. , vol.93 , pp. 681-687
    • Huang, T.W.1
  • 179
    • 0026740073 scopus 로고
    • The collagen superfamily-diverse structures and assemblies
    • Hulmes, D. J. S. The collagen superfamily-diverse structures and assemblies. Essays Biochem. 27: 49-67, 1992.
    • (1992) Essays Biochem. , vol.27 , pp. 49-67
    • Hulmes, D.J.S.1
  • 180
    • 0024535958 scopus 로고
    • A laminin-like adhesive protein concentrated in the synaptic cleft of the neuromuscular junction
    • Hunter, D. D., V. Shah, J. P. Merlie, and J. R. Sanes. A laminin-like adhesive protein concentrated in the synaptic cleft of the neuromuscular junction. Nature Lond. 338: 229-234, 1989.
    • (1989) Nature Lond. , vol.338 , pp. 229-234
    • Hunter, D.D.1    Shah, V.2    Merlie, J.P.3    Sanes, J.R.4
  • 181
    • 0026770377 scopus 로고
    • Integrins: Versatility, modulation, and signaling in cell adhesion
    • Hynes, R. O. Integrins: versatility, modulation, and signaling in cell adhesion. Cell 69: 11-25, 1992.
    • (1992) Cell , vol.69 , pp. 11-25
    • Hynes, R.O.1
  • 182
    • 0023742946 scopus 로고
    • Epithelial induction of stromal tenascin in the mouse mammary gland: From embryogenesis to carcinogenesis
    • Inaguma, Y., M. Kusakabe, E. J. Mackie, C. A. Pearson, R. Chiquet-Ehrismann, and T. Sakakura. Epithelial induction of stromal tenascin in the mouse mammary gland: from embryogenesis to carcinogenesis. Dev. Biol. 128: 245-255, 1988.
    • (1988) Dev. Biol. , vol.128 , pp. 245-255
    • Inaguma, Y.1    Kusakabe, M.2    Mackie, E.J.3    Pearson, C.A.4    Chiquet-Ehrismann, R.5    Sakakura, T.6
  • 184
    • 0026245524 scopus 로고
    • Integrins as mechanochemical transducers
    • Ingber, D. Integrins as mechanochemical transducers. Curr. Opin. Cell Biol. 3: 841-848, 1991.
    • (1991) Curr. Opin. Cell Biol. , vol.3 , pp. 841-848
    • Ingber, D.1
  • 185
    • 0025998068 scopus 로고
    • Extracellular matrix and cell shape: Potential control points for inhibition of angiogenesis
    • Ingber, D. Extracellular matrix and cell shape: potential control points for inhibition of angiogenesis. J. Cell. Biochem. 47: 236-241, 1991.
    • (1991) J. Cell. Biochem. , vol.47 , pp. 236-241
    • Ingber, D.1
  • 186
    • 0026841943 scopus 로고
    • Extracellular matrix as a solid-state regulator in angiogenesis: Identification of new targets for anti-cancer therapy
    • Ingber, D. E. Extracellular matrix as a solid-state regulator in angiogenesis: identification of new targets for anti-cancer therapy. Semin. Cancer Biol. 3: 57-63, 1992.
    • (1992) Semin. Cancer Biol. , vol.3 , pp. 57-63
    • Ingber, D.E.1
  • 187
    • 0023896174 scopus 로고
    • Three-dimensional network of cords: The main component of basement membranes
    • Inoue, S., and C. P. Leblond. Three-dimensional network of cords: the main component of basement membranes. Am. J. Anat. 181: 341-358, 1988.
    • (1988) Am. J. Anat. , vol.181 , pp. 341-358
    • Inoue, S.1    Leblond, C.P.2
  • 188
    • 0028226346 scopus 로고
    • Perlecan: A gem of a proteoglycan
    • Iozzo, R. V. Perlecan: a gem of a proteoglycan. Matrix Biol. 14: 203-208, 1994.
    • (1994) Matrix Biol. , vol.14 , pp. 203-208
    • Iozzo, R.V.1
  • 189
    • 0027243231 scopus 로고
    • Altered proteoglycan gene expression and the tumor stroma
    • Iozzo, R. V., and I. Cohen. Altered proteoglycan gene expression and the tumor stroma. Experientia Basel 49: 447-455, 1993.
    • (1993) Experientia Basel , vol.49 , pp. 447-455
    • Iozzo, R.V.1    Cohen, I.2
  • 190
    • 0028102255 scopus 로고
    • The biology of perlecan: The multifaceted heparan sulphate proteoglycan of basement membranes and pericellular matrices
    • Iozzo, R. V., I. R. Cohen, S. Grassel, and A. D. Murdoch. The biology of perlecan: the multifaceted heparan sulphate proteoglycan of basement membranes and pericellular matrices. Biochem. J. 302: 625-639, 1994.
    • (1994) Biochem. J. , vol.302 , pp. 625-639
    • Iozzo, R.V.1    Cohen, I.R.2    Grassel, S.3    Murdoch, A.D.4
  • 191
    • 0025737789 scopus 로고
    • Changes in immunoreactivity for cathepsin H in rat type II alveolar epithelial cells and its proteolytic activity in bronchoalveolar lavage fluid over 24 hours
    • Ishii, Y., Y. Hashizume, E. Kominami, and Y. Uchiyama. Changes in immunoreactivity for cathepsin H in rat type II alveolar epithelial cells and its proteolytic activity in bronchoalveolar lavage fluid over 24 hours. Anat. Rec. 230: 519-523, 1991.
    • (1991) Anat. Rec. , vol.230 , pp. 519-523
    • Ishii, Y.1    Hashizume, Y.2    Kominami, E.3    Uchiyama, Y.4
  • 194
    • 0025972360 scopus 로고
    • Multiple elevations of cytosolic-free Ca2+ in human neutrophils: Initiation by adherence receptors of the integrin family
    • Jaconi, M. E., J. M. Thelev, W. Schlegel, R. D. Appel, S. D. Wright, and P. D. Lew. Multiple elevations of cytosolic-free Ca2+ in human neutrophils: initiation by adherence receptors of the integrin family. J. Cell Biol. 112: 1249-1257, 1991.
    • (1991) J. Cell Biol. , vol.112 , pp. 1249-1257
    • Jaconi, M.E.1    Thelev, J.M.2    Schlegel, W.3    Appel, R.D.4    Wright, S.D.5    Lew, P.D.6
  • 195
    • 0028596335 scopus 로고
    • Expression of variant fibronectins in wound healing: Cellular source and biological activity of the EIIIA segment in rat hepatic fibrogenesis
    • Jarnagin, W. R., D. C. Rockey, V. E. Koteliansky, S.-S. Wang, and D. M. Bissell. Expression of variant fibronectins in wound healing: cellular source and biological activity of the EIIIA segment in rat hepatic fibrogenesis. J. Cell Biol. 127: 2037-2048, 1994.
    • (1994) J. Cell Biol. , vol.127 , pp. 2037-2048
    • Jarnagin, W.R.1    Rockey, D.C.2    Koteliansky, V.E.3    Wang, S.-S.4    Bissell, D.M.5
  • 196
    • 0026352781 scopus 로고
    • Differential expression of small chondroitin/dermatan sulfate proteoglycans, PG-I/biglycan and PG-II/decorin by vascular smooth muscle and endothelial cells in culture
    • Jarvelainen, H. T., M. G. Kinsella, T. N. Wight, and L. J. Sandell. Differential expression of small chondroitin/dermatan sulfate proteoglycans, PG-I/biglycan and PG-II/decorin by vascular smooth muscle and endothelial cells in culture. J. Biol. Chem. 266: 23274-23281, 1991.
    • (1991) J. Biol. Chem. , vol.266 , pp. 23274-23281
    • Jarvelainen, H.T.1    Kinsella, M.G.2    Wight, T.N.3    Sandell, L.J.4
  • 197
    • 0021710228 scopus 로고
    • Ultrastructural and immunofluorescence studies of basal-lamina alterations during mouselung morphogenesis
    • Jaskoll, T. F., and H. C. Slavkin. Ultrastructural and immunofluorescence studies of basal-lamina alterations during mouselung morphogenesis. Differentiation 28: 36-48, 1984.
    • (1984) Differentiation , vol.28 , pp. 36-48
    • Jaskoll, T.F.1    Slavkin, H.C.2
  • 198
    • 0026348693 scopus 로고
    • Incorporation of circulating fibronectin into various tissues during sepsis: Colocalization with endogenous tissue fibronectin
    • Jin, H. M., P. A. Vincent, W. E. Charash, T. M. Saba, P. McKeown-Longo, P. A. Blumenstock, and E. Lewis. Incorporation of circulating fibronectin into various tissues during sepsis: colocalization with endogenous tissue fibronectin. Exp. Mol. Pathol 55: 203-216, 1991.
    • (1991) Exp. Mol. Pathol , vol.55 , pp. 203-216
    • Jin, H.M.1    Vincent, P.A.2    Charash, W.E.3    Saba, T.M.4    McKeown-Longo, P.5    Blumenstock, P.A.6    Lewis, E.7
  • 199
    • 0025019731 scopus 로고
    • Ontogeny of pulmonary alveolar epithelial markers of differentiation
    • Joyce-Brady, M. F., and J. S. Brody. Ontogeny of pulmonary alveolar epithelial markers of differentiation. Dev. Biol. 137: 331-348, 1990.
    • (1990) Dev. Biol. , vol.137 , pp. 331-348
    • Joyce-Brady, M.F.1    Brody, J.S.2
  • 200
    • 0027459771 scopus 로고
    • Signal transduction from the extracellular matrix
    • Juliano, R. L., and S. Haskill. Signal transduction from the extracellular matrix. J. Cell Biol. 120: 577-585, 1993.
    • (1993) J. Cell Biol. , vol.120 , pp. 577-585
    • Juliano, R.L.1    Haskill, S.2
  • 202
    • 0025834976 scopus 로고
    • Differential regulation of extracellular matrix proteoglycan (PG) gene expression
    • Kahari, V.-M., H. Laijava, and J. Uitto. Differential regulation of extracellular matrix proteoglycan (PG) gene expression. J. Biol. Chem. 266: 10608-10615, 1991.
    • (1991) J. Biol. Chem. , vol.266 , pp. 10608-10615
    • Kahari, V.-M.1    Laijava, H.2    Uitto, J.3
  • 204
    • 0027686111 scopus 로고
    • Intercellular adhesion molecule-1 expression on the alveolar epithelium and its modification by hyperoxia
    • Kang, B. H., J. D. Crapo, C. D. Wegner, L. G. Letts, and L. Y. Chang. Intercellular adhesion molecule-1 expression on the alveolar epithelium and its modification by hyperoxia. Am. J. Respir. Cell Mol. Biol. 9: 350-355, 1993.
    • (1993) Am. J. Respir. Cell Mol. Biol. , vol.9 , pp. 350-355
    • Kang, B.H.1    Crapo, J.D.2    Wegner, C.D.3    Letts, L.G.4    Chang, L.Y.5
  • 205
    • 0027169731 scopus 로고
    • Heterogeneity in the immunolocalization of cytokeratin-specific monoclonal antibodies in the rat lungs: Evaluation of three different alveolar epithelial cell types
    • Kasper, M., T. Rudolf, A. A. Verhofstad, D. Schuh, and M. Muller. Heterogeneity in the immunolocalization of cytokeratin-specific monoclonal antibodies in the rat lungs: evaluation of three different alveolar epithelial cell types. Histochemistry 100: 65-71, 1993.
    • (1993) Histochemistry , vol.100 , pp. 65-71
    • Kasper, M.1    Rudolf, T.2    Verhofstad, A.A.3    Schuh, D.4    Muller, M.5
  • 206
    • 0017722990 scopus 로고
    • A cation-retaining layer in the alveolar-capillary membrane
    • Katsuyama, T., and S. S. Spicer. A cation-retaining layer in the alveolar-capillary membrane. Lab. Invest. 36: 428-435, 1977.
    • (1977) Lab. Invest. , vol.36 , pp. 428-435
    • Katsuyama, T.1    Spicer, S.S.2
  • 207
    • 0028220769 scopus 로고
    • Entactin/nidogen: Synthesis by bovine corneal endothelial cells and distribution in the human cornea
    • Katz, A., A. J. Fish, J. Pe'er, J. Frucht-Pery, N. Ron, and I. Vlodavsky. Entactin/nidogen: synthesis by bovine corneal endothelial cells and distribution in the human cornea. Invest. Opthalmol. Vis. Sci. 35: 495-502, 1994.
    • (1994) Invest. Opthalmol. Vis. Sci. , vol.35 , pp. 495-502
    • Katz, A.1    Fish, A.J.2    Pe'er, J.3    Frucht-Pery, J.4    Ron, N.5    Vlodavsky, I.6
  • 208
    • 0025454787 scopus 로고
    • Improved maintenance of adult rat alveolar type II cell differentiation in vitro: Effect of serum-free, hormonally defined medium and a reconstituted basement membrane
    • Kawada, H., J. M. Shannon, and R. J. Mason. Improved maintenance of adult rat alveolar type II cell differentiation in vitro: effect of serum-free, hormonally defined medium and a reconstituted basement membrane. Am. J. Respir. Cell Mol. Biol. 3: 33-43, 1990.
    • (1990) Am. J. Respir. Cell Mol. Biol. , vol.3 , pp. 33-43
    • Kawada, H.1    Shannon, J.M.2    Mason, R.J.3
  • 210
    • 0028556511 scopus 로고
    • Transforming growth factor-α enhances alveolar epithelial cell repair in a new in vitro model
    • Lung Cell. Mol. Physiol. 11
    • Kheradmand, F., H. G. Folkesson, L. Shum, R. Derynk, R. Pytela, and M. A. Matthay. Transforming growth factor-α enhances alveolar epithelial cell repair in a new in vitro model. Am. J. Physiol. 267 (Lung Cell. Mol. Physiol. 11): L728-L738, 1994.
    • (1994) Am. J. Physiol. , vol.267
    • Kheradmand, F.1    Folkesson, H.G.2    Shum, L.3    Derynk, R.4    Pytela, R.5    Matthay, M.A.6
  • 212
    • 0015950230 scopus 로고
    • The type II epithelial cell of the lung. I. Method of isolation
    • Kikkawa, Y., and K. Yoneda. The type II epithelial cell of the lung. I. Method of isolation. Lab. Invest. 30: 76-84, 1974.
    • (1974) Lab. Invest. , vol.30 , pp. 76-84
    • Kikkawa, Y.1    Yoneda, K.2
  • 213
    • 0028170187 scopus 로고
    • Primary structure of the α1 chain of human type XV collagen and exon-intron organization in the 3′ region of the corresponding gene
    • Kivirikko, S., P. Heinamaki, M. Rehn, N. Honkanen, J. C. Myers, and T. Pihlajaniemi. Primary structure of the α1 chain of human type XV collagen and exon-intron organization in the 3′ region of the corresponding gene. J. Biol. Chem. 269: 4773-4779, 1994.
    • (1994) J. Biol. Chem. , vol.269 , pp. 4773-4779
    • Kivirikko, S.1    Heinamaki, P.2    Rehn, M.3    Honkanen, N.4    Myers, J.C.5    Pihlajaniemi, T.6
  • 215
    • 0023389792 scopus 로고
    • Genes for basement membrane proteins are coordinately expressed in differentiating F9 cells but not in normal adult murine tissues
    • Kleinman, H. K., I. Ebihara, P. D. Killen, M. Sasaki, F. B. Cannon, Y. Yamada, and G. R. Martin. Genes for basement membrane proteins are coordinately expressed in differentiating F9 cells but not in normal adult murine tissues. Dev. Biol. 122: 373-378, 1987.
    • (1987) Dev. Biol. , vol.122 , pp. 373-378
    • Kleinman, H.K.1    Ebihara, I.2    Killen, P.D.3    Sasaki, M.4    Cannon, F.B.5    Yamada, Y.6    Martin, G.R.7
  • 216
    • 0024356683 scopus 로고
    • Identification of a second active site in laminin for promotion of cell adhesion and migration and inhibition of in vivo melanoma lung colonization
    • Kleinman, H. K., J. Graf, Y. Iwamoto, M. Sasaki, C. S. Schasteen, Y. Yamada, G. R. Martin, and F. A. Robey. Identification of a second active site in laminin for promotion of cell adhesion and migration and inhibition of in vivo melanoma lung colonization. Arch. Biochem. Biophys. 272: 39-45, 1989.
    • (1989) Arch. Biochem. Biophys. , vol.272 , pp. 39-45
    • Kleinman, H.K.1    Graf, J.2    Iwamoto, Y.3    Sasaki, M.4    Schasteen, C.S.5    Yamada, Y.6    Martin, G.R.7    Robey, F.A.8
  • 217
    • 0023572111 scopus 로고
    • Plasminogen activator inhibitor is associated with the extracellular matrix of cultured bovine smooth muscle cells
    • Knudsen, B., P. Harpel, and R. Nachman. Plasminogen activator inhibitor is associated with the extracellular matrix of cultured bovine smooth muscle cells. J. Clin. Invest. 80: 1082-1089, 1987.
    • (1987) J. Clin. Invest. , vol.80 , pp. 1082-1089
    • Knudsen, B.1    Harpel, P.2    Nachman, R.3
  • 220
    • 0022102304 scopus 로고
    • Primary structure of human fibronectin: Differential splicing may generate at least 10 polypeptide from a single gene
    • Kornblihtt, A. R., K. Umezawa, K. Vibe-Pedersen, and F. E. Baralle. Primary structure of human fibronectin: differential splicing may generate at least 10 polypeptide from a single gene. EMBO J. 4: 1755-1759, 1985.
    • (1985) EMBO J. , vol.4 , pp. 1755-1759
    • Kornblihtt, A.R.1    Umezawa, K.2    Vibe-Pedersen, K.3    Baralle, F.E.4
  • 221
    • 0027403048 scopus 로고
    • Extracellular matrix produced by cultured corneal and aortic endothelial cells contains active tissue-type and urokinase-type plasminogen activators
    • Korner, G., T. D. Bjornsson, and I. Vlodavsky. Extracellular matrix produced by cultured corneal and aortic endothelial cells contains active tissue-type and urokinase-type plasminogen activators. J. Cell. Physiol. 154: 456-465, 1993.
    • (1993) J. Cell. Physiol. , vol.154 , pp. 456-465
    • Korner, G.1    Bjornsson, T.D.2    Vlodavsky, I.3
  • 222
    • 0022620297 scopus 로고
    • Endocytosis of proteoheparan sulfate by cultured skin fibroblasts
    • Kruger, U., and H. Kresse. Endocytosis of proteoheparan sulfate by cultured skin fibroblasts. Biol. Chem. Hoppe Seyler 367: 465-471, 1986.
    • (1986) Biol. Chem. Hoppe Seyler , vol.367 , pp. 465-471
    • Kruger, U.1    Kresse, H.2
  • 223
    • 0026784413 scopus 로고
    • Differential expression of keratan sulphate proteoglycans fibromodulin, lumican and aggrecan in normal and fibrotic rat liver
    • Krull, N. B., and A. M. Gressner. Differential expression of keratan sulphate proteoglycans fibromodulin, lumican and aggrecan in normal and fibrotic rat liver. FEBS Lett. 312: 47-52, 1992.
    • (1992) FEBS Lett. , vol.312 , pp. 47-52
    • Krull, N.B.1    Gressner, A.M.2
  • 224
    • 0024822235 scopus 로고
    • An immunohistochemical study of architectural remodeling and connective tissue synthesis in pulmonary fibrosis
    • Kuhn, C., J. Boldt, T. E. King, Jr., E. Crouch, T. Vartio, and J. A. McDonald. An immunohistochemical study of architectural remodeling and connective tissue synthesis in pulmonary fibrosis. Am. Rev. Respir. Dis. 140: 1693-1703, 1989.
    • (1989) Am. Rev. Respir. Dis. , vol.140 , pp. 1693-1703
    • Kuhn, C.1    Boldt, J.2    King Jr., T.E.3    Crouch, E.4    Vartio, T.5    McDonald, J.A.6
  • 225
    • 0019405033 scopus 로고
    • Macromolecular structure of basement collagens. Identification of 7S collagen as a crosslinking domain of type IV collagen
    • Kuhn, K., H. Wiedemann, R. Timpl, J. Risteli, H. Dievinger, T. Voss, and R. W. Glanville. Macromolecular structure of basement collagens. Identification of 7S collagen as a crosslinking domain of type IV collagen. FEBS Lett. 125: 123-128, 1981.
    • (1981) FEBS Lett. , vol.125 , pp. 123-128
    • Kuhn, K.1    Wiedemann, H.2    Timpl, R.3    Risteli, J.4    Dievinger, H.5    Voss, T.6    Glanville, R.W.7
  • 226
    • 0025826879 scopus 로고
    • Macromolecular organization of chicken type X collagen m vitro
    • Kwan, A. P. L., C. E. Cummings, J. A. Chapman, and M. E. Grant. Macromolecular organization of chicken type X collagen m vitro. J. Cell Biol. 114: 597-604, 1991
    • (1991) J. Cell Biol. , vol.114 , pp. 597-604
    • Kwan, A.P.L.1    Cummings, C.E.2    Chapman, J.A.3    Grant, M.E.4
  • 227
    • 0025195764 scopus 로고
    • Structure and function of leukocyte integrins
    • Larson, R. S., and T. A. Springer. Structure and function of leukocyte integrins. Immunol. Rev. 114: 181-217, 1990.
    • (1990) Immunol. Rev. , vol.114 , pp. 181-217
    • Larson, R.S.1    Springer, T.A.2
  • 229
    • 0028247142 scopus 로고
    • Differential laminin gene expression in dorsal root ganglion neurons and nonneuronal cells
    • LeBeau, J. M., F. J. Liuzzi, A. S. Depto, and A. I. Vinik. Differential laminin gene expression in dorsal root ganglion neurons and nonneuronal cells. Exp. Neurol. 127: 1-8, 1994.
    • (1994) Exp. Neurol. , vol.127 , pp. 1-8
    • LeBeau, J.M.1    Liuzzi, F.J.2    Depto, A.S.3    Vinik, A.I.4
  • 231
    • 0028130398 scopus 로고
    • Extracellular matrix synthesis by coal dust-exposed type II epithelial cells
    • Lung Cell. Mol. Physiol. 11
    • Lee, Y. C., R. Hogg, and D. E. Rannels. Extracellular matrix synthesis by coal dust-exposed type II epithelial cells. Am. J. Physiol. 267 (Lung Cell. Mol. Physiol. 11): L365-L374, 1994.
    • (1994) Am. J. Physiol. , vol.267
    • Lee, Y.C.1    Hogg, R.2    Rannels, D.E.3
  • 232
    • 0024345563 scopus 로고
    • Extracellular matrix biosynthesis by cultured fetal rat lung epithelial cells. I. Characterization of the clone and the major genetic types of collagen produced
    • Leheup, B. P., S. J. Federspiel, M. L. Guerry-Force, N. T. Wetherall, P. A. Commers, S. J. DiMari, and M. A. Haralson. Extracellular matrix biosynthesis by cultured fetal rat lung epithelial cells. I. Characterization of the clone and the major genetic types of collagen produced. Lab. Invest. 60: 791-807, 1989.
    • (1989) Lab. Invest. , vol.60 , pp. 791-807
    • Leheup, B.P.1    Federspiel, S.J.2    Guerry-Force, M.L.3    Wetherall, N.T.4    Commers, P.A.5    DiMari, S.J.6    Haralson, M.A.7
  • 233
    • 0022396480 scopus 로고
    • Macrophages stimulate DNA synthesis in rat alveolar type II cells
    • Leslie, C. C., K. McCormick, J. L. Cook, and R. J. Mason. Macrophages stimulate DNA synthesis in rat alveolar type II cells. Am. Rev. Respir. Dis. 132: 1246-1252, 1985.
    • (1985) Am. Rev. Respir. Dis. , vol.132 , pp. 1246-1252
    • Leslie, C.C.1    McCormick, K.2    Cook, J.L.3    Mason, R.J.4
  • 235
    • 0023553695 scopus 로고
    • Association of plasminogen activator inhibitor (PAI-1) with the growth substratum and membrane of human endothelial cells
    • Levin, E., and L. Santell. Association of plasminogen activator inhibitor (PAI-1) with the growth substratum and membrane of human endothelial cells. J. Cell Biol. 105: 2543-2549, 1987.
    • (1987) J. Cell Biol. , vol.105 , pp. 2543-2549
    • Levin, E.1    Santell, L.2
  • 236
    • 0026671132 scopus 로고
    • Localization and synthesis of entactin in seminiferous tubules of the mouse
    • Lian, G., K. A. Miller, and G. C. Enders. Localization and synthesis of entactin in seminiferous tubules of the mouse. Biol. Reprod. 47: 316-325, 1992.
    • (1992) Biol. Reprod. , vol.47 , pp. 316-325
    • Lian, G.1    Miller, K.A.2    Enders, G.C.3
  • 237
    • 0024562011 scopus 로고
    • Identification of a neurite outgrowth-promoting domain of laminin using synthetic peptides
    • Liesi, P., A. Narvanen, J. Soos, H. Sariola, and G. Snounou. Identification of a neurite outgrowth-promoting domain of laminin using synthetic peptides. FEBS Lett. 244: 141-148, 1989.
    • (1989) FEBS Lett. , vol.244 , pp. 141-148
    • Liesi, P.1    Narvanen, A.2    Soos, J.3    Sariola, H.4    Snounou, G.5
  • 238
    • 0026640668 scopus 로고
    • Neuronal migration in cerebellar microcultures is inhibited by antibodies against a neurite outgrowth domain of laminin
    • Liesi, P., I. Seppala, and E. Trenkner. Neuronal migration in cerebellar microcultures is inhibited by antibodies against a neurite outgrowth domain of laminin. J. Neurosci. Res. 33: 170-176, 1992.
    • (1992) J. Neurosci. Res. , vol.33 , pp. 170-176
    • Liesi, P.1    Seppala, I.2    Trenkner, E.3
  • 239
    • 0027256508 scopus 로고
    • Multi-faceted regulation of cell differentiation by extracellular matrix
    • Lin, C. Q., and M. J. Bissell. Multi-faceted regulation of cell differentiation by extracellular matrix. FASEB J. 7: 737-743, 1993.
    • (1993) FASEB J. , vol.7 , pp. 737-743
    • Lin, C.Q.1    Bissell, M.J.2
  • 240
    • 0024987655 scopus 로고
    • Arachidonate metabolism increases as rat alveolar type II cells differentiate in vitro
    • Lung Cell. Mol. Physiol. 3
    • Lipchik, R. J., J. B. Chauncey, R. Paine, R. H. Simon, and M. Peters-Golden. Arachidonate metabolism increases as rat alveolar type II cells differentiate in vitro. Am. J. Physiol. 259 (Lung Cell. Mol. Physiol. 3): L73-L80, 1990.
    • (1990) Am. J. Physiol. , vol.259
    • Lipchik, R.J.1    Chauncey, J.B.2    Paine, R.3    Simon, R.H.4    Peters-Golden, M.5
  • 242
    • 0026388908 scopus 로고
    • Matrix-driven pneumocyte differentiation
    • Lwebuga-Mukasa, J. S. Matrix-driven pneumocyte differentiation. Am. Rev. Respir. Dis. 144: 452-457, 1991.
    • (1991) Am. Rev. Respir. Dis. , vol.144 , pp. 452-457
    • Lwebuga-Mukasa, J.S.1
  • 243
    • 0022608759 scopus 로고
    • Repopulation of a human alveolar matrix by adult rat type II pneumocytes in vitro. A novel system for type II pneumocyte culture
    • Lwebuga-Mukasa, J. S., D. H. Ingbar, and J. A. Madri. Repopulation of a human alveolar matrix by adult rat type II pneumocytes in vitro. A novel system for type II pneumocyte culture. Exp. Cell Res. 162: 423-435, 1986.
    • (1986) Exp. Cell Res. , vol.162 , pp. 423-435
    • Lwebuga-Mukasa, J.S.1    Ingbar, D.H.2    Madri, J.A.3
  • 244
    • 0021195638 scopus 로고
    • An acellular human amnionic membrane model for in vitro culture of type II pneumocytes: The role of the basement membrane in cell morphology and function
    • Lwebuga-Mukasa, J. S., G. Thulin, J. A. Madri, C. Barrett, and J. B. Warshaw. An acellular human amnionic membrane model for in vitro culture of type II pneumocytes: the role of the basement membrane in cell morphology and function. J. Cell. Physiol. 121: 215-225, 1984.
    • (1984) J. Cell. Physiol. , vol.121 , pp. 215-225
    • Lwebuga-Mukasa, J.S.1    Thulin, G.2    Madri, J.A.3    Barrett, C.4    Warshaw, J.B.5
  • 245
    • 0020549413 scopus 로고
    • Latent and active human polymorphonuclear leukocyte collagenases. Isolation, purification and characterization
    • Macartney, H. W., and H. Tschesche. Latent and active human polymorphonuclear leukocyte collagenases. Isolation, purification and characterization. Eur: J. Biochem. 130: 71-78, 1983.
    • (1983) Eur: J. Biochem. , vol.130 , pp. 71-78
    • Macartney, H.W.1    Tschesche, H.2
  • 247
    • 0024215607 scopus 로고
    • Induction of tenascin in healing wounds
    • Mackie, E. J., W. Halfter, and D. Liverani. Induction of tenascin in healing wounds. J. Cell Biol. 107: 2757-2767, 1988.
    • (1988) J. Cell Biol. , vol.107 , pp. 2757-2767
    • Mackie, E.J.1    Halfter, W.2    Liverani, D.3
  • 248
    • 0023603372 scopus 로고
    • Tenascin is associated with chondrogenic and osteogenic differentiation in vivo and promotes chondrogenesis in vitro
    • Mackie, E. J., I. Thesleff, and R. Chiquet-Ehrismann. Tenascin is associated with chondrogenic and osteogenic differentiation in vivo and promotes chondrogenesis in vitro. J. Cell Biol. 105: 2569-2579, 1987.
    • (1987) J. Cell Biol. , vol.105 , pp. 2569-2579
    • Mackie, E.J.1    Thesleff, I.2    Chiquet-Ehrismann, R.3
  • 249
    • 0018344983 scopus 로고
    • Isolation and tissue localization of type AB2 collagen from normal lung parenchyma
    • Madri, J. A., and H. Furthmayr. Isolation and tissue localization of type AB2 collagen from normal lung parenchyma. Am. J. Pathol 94: 323-332, 1979.
    • (1979) Am. J. Pathol , vol.94 , pp. 323-332
    • Madri, J.A.1    Furthmayr, H.2
  • 250
    • 0018936847 scopus 로고
    • Collagen polymorphism in the lung. An immunochemical study of pulmonary fibrosis
    • Madri, J. A., and H. Furthmayr. Collagen polymorphism in the lung. An immunochemical study of pulmonary fibrosis. Hum. Pathol. 11: 353-366, 1980.
    • (1980) Hum. Pathol. , vol.11 , pp. 353-366
    • Madri, J.A.1    Furthmayr, H.2
  • 251
    • 0026801479 scopus 로고
    • Alveolar type II cells synthesize hydrophobic cell-associated proteoglycans with multiple core proteins
    • Lung Cell. Mol. Physiol. 7
    • Maniscalco, W. M., and M. H. Campbell. Alveolar type II cells synthesize hydrophobic cell-associated proteoglycans with multiple core proteins. Am. J. Physiol. 263 (Lung Cell. Mol. Physiol. 7): L348-L356, 1992.
    • (1992) Am. J. Physiol. , vol.263
    • Maniscalco, W.M.1    Campbell, M.H.2
  • 252
    • 0028339010 scopus 로고
    • Transforming growth factor-β induces a chondroitin sulfate/dermatan sulfate proteoglycan in alveolar type II cells
    • Lung Cell. Mol. Physiol. 10
    • Manisealco, W. M., and M. H. Campbell. Transforming growth factor-β induces a chondroitin sulfate/dermatan sulfate proteoglycan in alveolar type II cells. Am. J. Physiol. 266 (Lung Cell. Mol. Physiol. 10): L672-L680, 1994.
    • (1994) Am. J. Physiol. , vol.266
    • Manisealco, W.M.1    Campbell, M.H.2
  • 253
    • 0028152330 scopus 로고
    • Transforming growth factor-β1 modulates type II cell fibronectin and surfactant protein C expression
    • Lung Cell. Mol. Physiol. 11
    • Maniscalco, W. M., R. A. Sinkin, R. H. Watkins, and M. H. Campbell. Transforming growth factor-β1 modulates type II cell fibronectin and surfactant protein C expression. Am. J. Physiol. 267 (Lung Cell. Mol. Physiol. 11): L569-L577, 1994.
    • (1994) Am. J. Physiol. , vol.267
    • Maniscalco, W.M.1    Sinkin, R.A.2    Watkins, R.H.3    Campbell, M.H.4
  • 254
    • 0024243999 scopus 로고
    • Characterization of proteolytic fragments of the laminin-nidogen complex and their activity in ligand-binding assays
    • Mann, K., R. Deutzmann, and R. Timpl. Characterization of proteolytic fragments of the laminin-nidogen complex and their activity in ligand-binding assays. Eur. J. Biochem. 178: 71-80, 1988.
    • (1988) Eur. J. Biochem. , vol.178 , pp. 71-80
    • Mann, K.1    Deutzmann, R.2    Timpl, R.3
  • 255
    • 0026629850 scopus 로고
    • The dermal-epidermal junction of human skin contains a novel laminin variant
    • Marinkovich, M. P., G. P. Lunstrum, D. R. Keene, and R. E. Burgeson. The dermal-epidermal junction of human skin contains a novel laminin variant. J. Cell Biol. 119: 695-703, 1992.
    • (1992) J. Cell Biol. , vol.119 , pp. 695-703
    • Marinkovich, M.P.1    Lunstrum, G.P.2    Keene, D.R.3    Burgeson, R.E.4
  • 258
    • 0028231735 scopus 로고
    • Transglutaminase-mediated processing of fibronectin by endothelial cell monolayers
    • Martinez, J., D. G. Chalupowicz, R. K. Roush, A. Sheth, and C. Barsigian. Transglutaminase-mediated processing of fibronectin by endothelial cell monolayers. Biochemistry 33: 2538-2545, 1994.
    • (1994) Biochemistry , vol.33 , pp. 2538-2545
    • Martinez, J.1    Chalupowicz, D.G.2    Roush, R.K.3    Sheth, A.4    Barsigian, C.5
  • 259
    • 0019305203 scopus 로고
    • Synthesis of phosphatidylcholine and phosphatidylglycerol by alveolar type II cells in primary culture
    • Mason, R. J., and L. G. Dobbs. Synthesis of phosphatidylcholine and phosphatidylglycerol by alveolar type II cells in primary culture. J. Biol. Chem. 255: 5101-5107, 1980.
    • (1980) J. Biol. Chem. , vol.255 , pp. 5101-5107
    • Mason, R.J.1    Dobbs, L.G.2
  • 261
    • 0025230509 scopus 로고
    • Metalloproteinases and their inhibitors in matrix remodeling
    • Matrisian, L. M. Metalloproteinases and their inhibitors in matrix remodeling. Trends Genet. 6: 121-125, 1990.
    • (1990) Trends Genet. , vol.6 , pp. 121-125
    • Matrisian, L.M.1
  • 262
    • 0028302929 scopus 로고
    • A novel laminin E8 cell adhesion site required for lung alveolar formation in vitro
    • Matter, M. L., and G. W. Laurie. A novel laminin E8 cell adhesion site required for lung alveolar formation in vitro. J. Cell Biol. 124: 1083-1090, 1994.
    • (1994) J. Cell Biol. , vol.124 , pp. 1083-1090
    • Matter, M.L.1    Laurie, G.W.2
  • 263
    • 0022382680 scopus 로고
    • Degradation of heparan sulfate in the subendothelial extracellular matrix by a readily released heparanase from human neutrophils
    • Matzner, Y., M. Bar-Ner, J. Yahalom, R. Ishai-Michacli, Z. Fuks, and I. Vlodavsky. Degradation of heparan sulfate in the subendothelial extracellular matrix by a readily released heparanase from human neutrophils. J. Clin. Invest. 76: 1306-1313, 1985.
    • (1985) J. Clin. Invest. , vol.76 , pp. 1306-1313
    • Matzner, Y.1    Bar-Ner, M.2    Yahalom, J.3    Ishai-Michacli, R.4    Fuks, Z.5    Vlodavsky, I.6
  • 264
    • 0027489337 scopus 로고
    • Sites of nidogen cleavage by proteases involved in tissue humeostasis and remodelling
    • Mayer, U., K. Mann, R. Timpl, and G. Murphy. Sites of nidogen cleavage by proteases involved in tissue humeostasis and remodelling. Eur. J. Biochem. 217: 877-884, 1993.
    • (1993) Eur. J. Biochem. , vol.217 , pp. 877-884
    • Mayer, U.1    Mann, K.2    Timpl, R.3    Murphy, G.4
  • 265
    • 0027682593 scopus 로고
    • New members of the collagen superfamily
    • Mayne, R., and R. G. Brewton. New members of the collagen superfamily. Curr. Opin. Cell Biol. 5: 883-890, 1993.
    • (1993) Curr. Opin. Cell Biol. , vol.5 , pp. 883-890
    • Mayne, R.1    Brewton, R.G.2
  • 266
    • 0024150414 scopus 로고
    • Extracellular matrix assembly
    • McDonald, J. A. Extracellular matrix assembly. Annu. Rev. Cell Biol. 4: 183-207, 1988.
    • (1988) Annu. Rev. Cell Biol. , vol.4 , pp. 183-207
    • McDonald, J.A.1
  • 267
    • 0023178166 scopus 로고
    • Fibronectin's cell adhesive domain and an amino-terminal matrix assembly domain participate in its assembly in fibroblast pericellular matrix
    • McDonald, J. A., B. J. Quade, T. J. Broekelmann, R. LaChance, K. Forsman, E. Hasegawa, and S. Akiyama. Fibronectin's cell adhesive domain and an amino-terminal matrix assembly domain participate in its assembly in fibroblast pericellular matrix. J. Biol. Chem. 262: 2957-2967, 1987.
    • (1987) J. Biol. Chem. , vol.262 , pp. 2957-2967
    • McDonald, J.A.1    Quade, B.J.2    Broekelmann, T.J.3    LaChance, R.4    Forsman, K.5    Hasegawa, E.6    Akiyama, S.7
  • 268
    • 0028898826 scopus 로고
    • A type I cell-specific protein is a biochemical marker of epithelial injury in a rat model of pneumonia
    • Lung Cell. Mol. Physiol. 12
    • McElroy, M. C., J. F. Pittet, S. Washimoto, L. Allen, J. P. Wiener-Kronish, and L. G. Dobbs. A type I cell-specific protein is a biochemical marker of epithelial injury in a rat model of pneumonia. Am. J. Physiol. 268 (Lung Cell. Mol. Physiol. 12): L181-L186, 1995.
    • (1995) Am. J. Physiol. , vol.268
    • McElroy, M.C.1    Pittet, J.F.2    Washimoto, S.3    Allen, L.4    Wiener-Kronish, J.P.5    Dobbs, L.G.6
  • 269
    • 0026728248 scopus 로고
    • Extracellular matrix and the regulation of lung development and repair
    • McGowan, S. E. Extracellular matrix and the regulation of lung development and repair. FASEB J. 6: 2895-2904, 1992.
    • (1992) FASEB J. , vol.6 , pp. 2895-2904
    • McGowan, S.E.1
  • 270
    • 0021128653 scopus 로고
    • Mechanism of formation of disulfide-bonded multimers of plasma fibronectin in cell layers of cultured human fibroblasts
    • McKeown-Longo, P. J., and D. F. Mosher. Mechanism of formation of disulfide-bonded multimers of plasma fibronectin in cell layers of cultured human fibroblasts. J. Biol. Chem. 259: 12210-12215, 1984.
    • (1984) J. Biol. Chem. , vol.259 , pp. 12210-12215
    • McKeown-Longo, P.J.1    Mosher, D.F.2
  • 271
    • 0026379091 scopus 로고
    • Elastin synthesis and fiber assembly
    • Mecham, R. P. Elastin synthesis and fiber assembly. Ann. NY Acad. Sci. 624: 137-146, 1991.
    • (1991) Ann. NY Acad. Sci. , vol.624 , pp. 137-146
    • Mecham, R.P.1
  • 272
    • 0026093621 scopus 로고
    • Receptors for laminin on mammalian cells
    • Mecham, R. P. Receptors for laminin on mammalian cells. FASEB J. 5: 2538-2546, 1991.
    • (1991) FASEB J. , vol.5 , pp. 2538-2546
    • Mecham, R.P.1
  • 276
    • 0028360641 scopus 로고
    • Morphology of the basement membrane
    • Merker, H.-J. Morphology of the basement membrane. Microsc. Res. Tech. 28: 95-124, 1994.
    • (1994) Microsc. Res. Tech. , vol.28 , pp. 95-124
    • Merker, H.-J.1
  • 277
    • 0027209270 scopus 로고
    • The extracellular matrix proteins laminin and fibronectin contain binding domains for human plasminogen and tissue plasminogen activator
    • Moser, T. L., J. J. Enghild, S. V. Pizzo, and M. S. Stack. The extracellular matrix proteins laminin and fibronectin contain binding domains for human plasminogen and tissue plasminogen activator. J. Biol. Chem. 268: 18917-18923, 1993.
    • (1993) J. Biol. Chem. , vol.268 , pp. 18917-18923
    • Moser, T.L.1    Enghild, J.J.2    Pizzo, S.V.3    Stack, M.S.4
  • 280
    • 0028169716 scopus 로고
    • The human α1(XV) collagen chain contains a large amino-terminal non-triple helical domain with a tandem repeat structure and homology to α1(XVIII) collagen
    • Muragaki, Y., N. Abe, Y. Ninomiya, B. R. Olsen, and A. Ooshima. The human α1(XV) collagen chain contains a large amino-terminal non-triple helical domain with a tandem repeat structure and homology to α1(XVIII) collagen. J. Biol. Chem. 269: 4042-4046, 1994.
    • (1994) J. Biol. Chem. , vol.269 , pp. 4042-4046
    • Muragaki, Y.1    Abe, N.2    Ninomiya, Y.3    Olsen, B.R.4    Ooshima, A.5
  • 281
    • 0025895193 scopus 로고
    • Matrix metalloproteinase degradation of elastin, type IV collagen and proteoglycan. A quantitative comparison of the activities of 95 kDa and 72 kDa gelatinases, stromelysins-1 and -2 and punctuated metalloproteinase (PUMP)
    • Murphy, G., M. I. Cockett, R. V. Ward, and A. J. P. Docherty. Matrix metalloproteinase degradation of elastin, type IV collagen and proteoglycan. A quantitative comparison of the activities of 95 kDa and 72 kDa gelatinases, stromelysins-1 and -2 and punctuated metalloproteinase (PUMP). Biochem. J. 277: 277-279, 1991.
    • (1991) Biochem. J. , vol.277 , pp. 277-279
    • Murphy, G.1    Cockett, M.I.2    Ward, R.V.3    Docherty, A.J.P.4
  • 283
    • 0028238354 scopus 로고
    • The triple-helical region of human type XIX collagen consists of multiple collagenous subdomains and exhibits limited sequence homology to α1(XVI)
    • Myers, J. C., H. Yang, J. A. D'Ippolito, A. Presente, M. K. Miller, and A. S. Dion. The triple-helical region of human type XIX collagen consists of multiple collagenous subdomains and exhibits limited sequence homology to α1(XVI). J. Biol. Chem. 269: 18549-18557, 1994.
    • (1994) J. Biol. Chem. , vol.269 , pp. 18549-18557
    • Myers, J.C.1    Yang, H.2    D'Ippolito, J.A.3    Presente, A.4    Miller, M.K.5    Dion, A.S.6
  • 285
    • 0021249299 scopus 로고
    • Activated T lymphocytes produce a matrix-degrading heparan sulphate endoglycosidase
    • Naparstek, Y., I. R. Cohen, Z. Fuks, and I. Vlodavsky. Activated T lymphocytes produce a matrix-degrading heparan sulphate endoglycosidase. Nature Lond. 310: 241-244, 1984.
    • (1984) Nature Lond. , vol.310 , pp. 241-244
    • Naparstek, Y.1    Cohen, I.R.2    Fuks, Z.3    Vlodavsky, I.4
  • 286
    • 0025741870 scopus 로고
    • Calcium signaling capacity of the CD11b/CD18 integrin on human neutrophils
    • Ng-Sikorski, J., R. Andersson, M. Patarroyo, and T. Andersson. Calcium signaling capacity of the CD11b/CD18 integrin on human neutrophils. Exp. Cell Res. 195: 504-508, 1991.
    • (1991) Exp. Cell Res. , vol.195 , pp. 504-508
    • Ng-Sikorski, J.1    Andersson, R.2    Patarroyo, M.3    Andersson, T.4
  • 287
    • 0024377846 scopus 로고
    • Human and rat malignant-tumor-associated mRNAs encode stromelysinlike metalloproteinases
    • Nicholson, R., G. Murphy, and R. Breathnach. Human and rat malignant-tumor-associated mRNAs encode stromelysinlike metalloproteinases. Biochemistry 28: 5195-5203, 1989.
    • (1989) Biochemistry , vol.28 , pp. 5195-5203
    • Nicholson, R.1    Murphy, G.2    Breathnach, R.3
  • 288
    • 0023268507 scopus 로고
    • Role of glycosidases in human ovarian carcinoma cell mediated degradation of subendothelial extracellular matrix
    • Niedbala, M. J., R. Madiyalakan, K. Matta, K. Crickard, M. Sharma, and R. J. Bernacki. Role of glycosidases in human ovarian carcinoma cell mediated degradation of subendothelial extracellular matrix. Cancer Res. 47: 4634-4641, 1987.
    • (1987) Cancer Res. , vol.47 , pp. 4634-4641
    • Niedbala, M.J.1    Madiyalakan, R.2    Matta, K.3    Crickard, K.4    Sharma, M.5    Bernacki, R.J.6
  • 290
    • 0027229259 scopus 로고
    • Cytokines, and proteoglycons
    • Nietfeld, J. J. Cytokines, and proteoglycons. Experientia Basel 49: 456-469, 1993.
    • (1993) Experientia Basel , vol.49 , pp. 456-469
    • Nietfeld, J.J.1
  • 293
    • 0026633247 scopus 로고
    • The chicken neural extracellular matrix molecule restrictin: Similarity with EGF-, fibronectin type III-, and fibrinogen-like motifs
    • Norenberg, U., H. Wille, J. M. Wolff, R. Frank, and F. G. Rathjen. The chicken neural extracellular matrix molecule restrictin: similarity with EGF-, fibronectin type III-, and fibrinogen-like motifs. Neuron 8: 849-863, 1992.
    • (1992) Neuron , vol.8 , pp. 849-863
    • Norenberg, U.1    Wille, H.2    Wolff, J.M.3    Frank, R.4    Rathjen, F.G.5
  • 295
    • 0028210848 scopus 로고
    • Cloning of cDNA and genomic DNA encoding human type XVIII collagen and localization of the α1(XVIII) collagen gene to mouse chromosome 10 and human chromosome 21
    • Oh, S. P., M. L. Warman, M. F. Seldin, S. D. Cheng, J. H. Knoll, S. Timmons, and B. R. Olsen. Cloning of cDNA and genomic DNA encoding human type XVIII collagen and localization of the α1(XVIII) collagen gene to mouse chromosome 10 and human chromosome 21. Genomics 19: 494-499, 1994.
    • (1994) Genomics , vol.19 , pp. 494-499
    • Oh, S.P.1    Warman, M.L.2    Seldin, M.F.3    Cheng, S.D.4    Knoll, J.H.5    Timmons, S.6    Olsen, B.R.7
  • 297
    • 0028245094 scopus 로고
    • Immunocytochemical localization of extracellular superoxide disinutase in human lung
    • Oury, T. D., L.Y. Chang, S. L. Marklund, B. J. Day, and J. D. Crapo. Immunocytochemical localization of extracellular superoxide disinutase in human lung. Lab. Invest. 70: 889-898, 1994.
    • (1994) Lab. Invest. , vol.70 , pp. 889-898
    • Oury, T.D.1    Chang, L.Y.2    Marklund, S.L.3    Day, B.J.4    Crapo, J.D.5
  • 298
    • 0024550609 scopus 로고
    • Patterns of alternative splicing of fibronectin pre-mRNA in human adult and fetal tissues
    • Oyama, F., Y. Murata, N. Suganuma, T. Kimura, K. Titani, and K. Sekiguchi. Patterns of alternative splicing of fibronectin pre-mRNA in human adult and fetal tissues. Biochemistry 28: 1428-1434, 1989.
    • (1989) Biochemistry , vol.28 , pp. 1428-1434
    • Oyama, F.1    Murata, Y.2    Suganuma, N.3    Kimura, T.4    Titani, K.5    Sekiguchi, K.6
  • 300
    • 0025718766 scopus 로고
    • Tissue-specific splicing pattern of fibronectin messenger RNA precursor during development and aging in rat
    • Pagani, F., L. Zagato, C. Vergani, G. Casari, A. Sidoli, and F. E. Baralle. Tissue-specific splicing pattern of fibronectin messenger RNA precursor during development and aging in rat. J. Cell Biol. 113: 1223-1229, 1991.
    • (1991) J. Cell Biol. , vol.113 , pp. 1223-1229
    • Pagani, F.1    Zagato, L.2    Vergani, C.3    Casari, G.4    Sidoli, A.5    Baralle, F.E.6
  • 301
    • 0023786881 scopus 로고
    • The pattern of cytokeratin synthesis is a marker of type 2 cell differentiation in adult and maturing fetal lung alveolar cells
    • Paine, R., A. Ben-Zeev, S. R. Farmer, and J. S. Brody. The pattern of cytokeratin synthesis is a marker of type 2 cell differentiation in adult and maturing fetal lung alveolar cells. Dev. Biol. 129: 505-515, 1988.
    • (1988) Dev. Biol. , vol.129 , pp. 505-515
    • Paine, R.1    Ben-Zeev, A.2    Farmer, S.R.3    Brody, J.S.4
  • 302
    • 0028010178 scopus 로고
    • Regulation of alveolar epithelial cell ICAM-1 expression by cell shape and cell-cell interactions
    • Lung Cell. Mol. Physiol. 10
    • Paine, R., P. Christensen, G. B. Toews, and R. H. Simon. Regulation of alveolar epithelial cell ICAM-1 expression by cell shape and cell-cell interactions. Am. J. Physiol. 266 (Lung Cell. Mol. Physiol. 10): L476-L484, 1994.
    • (1994) Am. J. Physiol. , vol.266
    • Paine, R.1    Christensen, P.2    Toews, G.B.3    Simon, R.H.4
  • 303
    • 0026514466 scopus 로고
    • Mechanisms of neutrophil damage to human alveolar extracellular matrix: The role of serine and metalloproteases
    • Palmgren, M. S., R. D. deShazo, R. M. Carter, M. L. Zimny, and S. V. Shah. Mechanisms of neutrophil damage to human alveolar extracellular matrix: the role of serine and metalloproteases. J. Allergy Clin. Immunal. 89: 905-915, 1992.
    • (1992) J. Allergy Clin. Immunal. , vol.89 , pp. 905-915
    • Palmgren, M.S.1    Deshazo, R.D.2    Carter, R.M.3    Zimny, M.L.4    Shah, S.V.5
  • 304
    • 0026082034 scopus 로고
    • Transforming growth factor-β type I binds to collagen type IV of basement membrane matrix: Implications for development
    • Paralkar, V. M., S. Vukicevic, and A. H. Reddi. Transforming growth factor-β type I binds to collagen type IV of basement membrane matrix: implications for development. Dev. Biol. 143: 303-308, 1991.
    • (1991) Dev. Biol. , vol.143 , pp. 303-308
    • Paralkar, V.M.1    Vukicevic, S.2    Reddi, A.H.3
  • 305
    • 0027751890 scopus 로고
    • The vascular endothelial growth factor (VEGF) isoforms: Differential deposition into the subepithelial extracellular matrix and bioactivity of extracellular matrix-bound VEGF
    • Park, J. E., G. A. Keller, and N. Ferrara. The vascular endothelial growth factor (VEGF) isoforms: differential deposition into the subepithelial extracellular matrix and bioactivity of extracellular matrix-bound VEGF. Mol. Biol. Cell 4: 1317-1326, 1993.
    • (1993) Mol. Biol. Cell , vol.4 , pp. 1317-1326
    • Park, J.E.1    Keller, G.A.2    Ferrara, N.3
  • 306
    • 0025424630 scopus 로고
    • Tropoelastin heterogeneity: Implications for protein function and disease
    • Parks, W. C., and S. B. Deak. Tropoelastin heterogeneity: implications for protein function and disease. Am. J. Respir. Cell Mol. Biol. 2: 399-406, 1990.
    • (1990) Am. J. Respir. Cell Mol. Biol. , vol.2 , pp. 399-406
    • Parks, W.C.1    Deak, S.B.2
  • 307
    • 0023887474 scopus 로고
    • Developmental regulation of tropoelastin isoforms
    • Parks, W. C., H. Secrist, L. C. Wu, and R. P. Mecham. Developmental regulation of tropoelastin isoforms. J. Biol. Chem. 263: 4416-4423, 1988.
    • (1988) J. Biol. Chem. , vol.263 , pp. 4416-4423
    • Parks, W.C.1    Secrist, H.2    Wu, L.C.3    Mecham, R.P.4
  • 308
    • 0026813536 scopus 로고
    • Plasminogen activator inhibitor type 1 production by rat type II pneumocytes in culture
    • Parton, L. A., D. Warburton, and W. E. Laug. Plasminogen activator inhibitor type 1 production by rat type II pneumocytes in culture. Am. J. Respir. Cell Mol. Biol. 6: 133-139, 1992.
    • (1992) Am. J. Respir. Cell Mol. Biol. , vol.6 , pp. 133-139
    • Parton, L.A.1    Warburton, D.2    Laug, W.E.3
  • 309
    • 0023405931 scopus 로고
    • Organization of the fibronectin gene provides evidence for exon shuffling during evolution
    • Patel, R. S., E. Odermatt, J. E. Schwartzbauer, and R. O. Hynes. Organization of the fibronectin gene provides evidence for exon shuffling during evolution. EMBO J. 6: 2565-2572, 1987.
    • (1987) EMBO J. , vol.6 , pp. 2565-2572
    • Patel, R.S.1    Odermatt, E.2    Schwartzbauer, J.E.3    Hynes, R.O.4
  • 310
    • 0022972106 scopus 로고
    • Cell-type-specific fibronectin subunits generated by alternative splicing
    • Paul, J. I., J. E. Schwarzbauer, J. W. Tamkun, and R. O. Hynes. Cell-type-specific fibronectin subunits generated by alternative splicing. J. Biol. Chem. 261: 12258-12265, 1986.
    • (1986) J. Biol. Chem. , vol.261 , pp. 12258-12265
    • Paul, J.I.1    Schwarzbauer, J.E.2    Tamkun, J.W.3    Hynes, R.O.4
  • 312
    • 0343292988 scopus 로고
    • Transforming growth factor β increases mRNA for matrix proteins both in the presence and in the absence of changes in mRNA stability
    • Penttinen, R. P., S. Kobayashi, and P. Bornstein. Transforming growth factor β increases mRNA for matrix proteins both in the presence and in the absence of changes in mRNA stability. Proc. Natl. Acad. Sci. USA 85: 1105-1108, 1988.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 1105-1108
    • Penttinen, R.P.1    Kobayashi, S.2    Bornstein, P.3
  • 313
    • 0024066238 scopus 로고
    • Biosynthesis, secretion and extracellular localization of anchorin CII, a collagen-binding protein of the calpactin family
    • Pfaffle, M., F. Ruggiero, H. Hofmann, M. P. Fernadez, O. Selmin, Y. Yamada, R. Garrone, and K. von der Mark. Biosynthesis, secretion and extracellular localization of anchorin CII, a collagen-binding protein of the calpactin family. EMBO J. 1: 2335-2342, 1988.
    • (1988) EMBO J. , vol.1 , pp. 2335-2342
    • Pfaffle, M.1    Ruggiero, F.2    Hofmann, H.3    Fernadez, M.P.4    Selmin, O.5    Yamada, Y.6    Garrone, R.7    Von Der Mark, K.8
  • 314
    • 0023915420 scopus 로고
    • The platelet membrane glycoprotem IIb-IIIa complex
    • Phillips, D. R., I. F. Charo, L. V. Parise, and L. A. Fitzgerald. The platelet membrane glycoprotem IIb-IIIa complex. Blood 71: 831-843, 1988.
    • (1988) Blood , vol.71 , pp. 831-843
    • Phillips, D.R.1    Charo, I.F.2    Parise, L.V.3    Fitzgerald, L.A.4
  • 315
    • 0017817413 scopus 로고
    • The type I alveolar lining cell of the mammalian lung. I. Isolation and enrichment from dissociated adult rabbit lung
    • Picciano, P., and R. M. Rosenbaum. The type I alveolar lining cell of the mammalian lung. I. Isolation and enrichment from dissociated adult rabbit lung. Am. J. Pathol. 90: 99-122, 1978.
    • (1978) Am. J. Pathol. , vol.90 , pp. 99-122
    • Picciano, P.1    Rosenbaum, R.M.2
  • 316
    • 0025130777 scopus 로고
    • Heterogeneity of rat tropoelastin mRNA revealed by cDNA cloning
    • Pierce, R. A., S. B. Deak, S. A. Belsky, C. A. Stolle, and C. D. Boyd. Heterogeneity of rat tropoelastin mRNA revealed by cDNA cloning. Biochemistiy 29: 9677-9683, 1990.
    • (1990) Biochemistiy , vol.29 , pp. 9677-9683
    • Pierce, R.A.1    Deak, S.B.2    Belsky, S.A.3    Stolle, C.A.4    Boyd, C.D.5
  • 318
    • 0023924807 scopus 로고
    • Human laminin B2 chain comparison of the complete amino acid sequence with the B1 chain reveals variability in sequence homology between different structural domains
    • Pikkarainen, T., T. Kallunki, and K. Tryggvason. Human laminin B2 chain comparison of the complete amino acid sequence with the B1 chain reveals variability in sequence homology between different structural domains. J. Biol. Chem 263: 6751-6758, 1988.
    • (1988) J. Biol. Chem , vol.263 , pp. 6751-6758
    • Pikkarainen, T.1    Kallunki, T.2    Tryggvason, K.3
  • 319
    • 0028060044 scopus 로고
    • Host defence capacities of pulmonary surfactant: Evidence for "non-surfactant" functions of the surfactant system
    • Pison, U., M. Max, A. Neuendank, S. Weissbach, and S. Pietschmann. Host defence capacities of pulmonary surfactant: evidence for "non-surfactant" functions of the surfactant system Eur. J. Clin. Invest. 24: 586-599, 1994.
    • (1994) Eur. J. Clin. Invest. , vol.24 , pp. 586-599
    • Pison, U.1    Max, M.2    Neuendank, A.3    Weissbach, S.4    Pietschmann, S.5
  • 320
    • 0027105123 scopus 로고
    • Immunoelectron microscopic localization of type I plasminogen activator inhibitor in the extracellular matrix of transforming growth factor β-activated endothelial cells
    • Podor, T. J., and D. J. Loskutoff. Immunoelectron microscopic localization of type I plasminogen activator inhibitor in the extracellular matrix of transforming growth factor β-activated endothelial cells. Ann. NYAcad. Sci. 667: 46-49, 1992.
    • (1992) Ann. NYAcad. Sci. , vol.667 , pp. 46-49
    • Podor, T.J.1    Loskutoff, D.J.2
  • 321
    • 0027216613 scopus 로고
    • 7 integrin mediates B cell binding to fibronectin and vascular cell adhesion molecules-1. Expression and function of on integrins on human B lymphocytes
    • 7 integrin mediates B cell binding to fibronectin and vascular cell adhesion molecules-1. Expression and function of on integrins on human B lymphocytes. J. Immunol. 151: 2471-2483, 1993.
    • (1993) J. Immunol. , vol.151 , pp. 2471-2483
    • Postigo, A.A.1    Sanchez-Mateos, P.2    Lazarovits, A.I.3    Sanchez-Madrid, F.4    De Landazuri, M.O.5
  • 323
    • 0027364324 scopus 로고
    • Multiple integrins mediate cell attachment to cytotactin/tenascin
    • Prieto, A. L., G. M. Edelman, and K. L. Crossin. Multiple integrins mediate cell attachment to cytotactin/tenascin. Proc. Natl. Acad. Sci. USA 90: 10154-10158, 1993.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 10154-10158
    • Prieto, A.L.1    Edelman, G.M.2    Crossin, K.L.3
  • 324
    • 0018231553 scopus 로고
    • Endocytosis of sulphated proteoglycans by cultured skin fibroblasts
    • Prinz, R., J. Schwermann, E. Buddecke, and K. von Figura. Endocytosis of sulphated proteoglycans by cultured skin fibroblasts. Biochem. J. 176: 671-676, 1978.
    • (1978) Biochem. J. , vol.176 , pp. 671-676
    • Prinz, R.1    Schwermann, J.2    Buddecke, E.3    Von Figura, K.4
  • 325
    • 0024273065 scopus 로고
    • Fibronectin's amino-terminal matrix assembly site is located within the 29 kDa amino-terminal domain containing five type I repeats
    • Quade, B. J., and J. A. McDonald. Fibronectin's amino-terminal matrix assembly site is located within the 29 kDa amino-terminal domain containing five type I repeats. J. Biol. Chem. 263: 19602-19609, 1988.
    • (1988) J. Biol. Chem. , vol.263 , pp. 19602-19609
    • Quade, B.J.1    McDonald, J.A.2
  • 326
    • 0024318368 scopus 로고
    • PUMP-1 cDNA codes for a protein with characteristics similar to those of classical collagenase family members
    • Quantin, B., G. Murphy, and R. Breathnach. PUMP-1 cDNA codes for a protein with characteristics similar to those of classical collagenase family members. Biochemistry 28: 5327-5334, 1989.
    • (1989) Biochemistry , vol.28 , pp. 5327-5334
    • Quantin, B.1    Murphy, G.2    Breathnach, R.3
  • 327
    • 0027939832 scopus 로고
    • The role of extracellular matrix in postinflammatory wound healing and fibrosis
    • Raghow, R. The role of extracellular matrix in postinflammatory wound healing and fibrosis. FASBB J. 8: 823-831, 1994.
    • (1994) FASBB J. , vol.8 , pp. 823-831
    • Raghow, R.1
  • 328
    • 0024558210 scopus 로고
    • Molecular mechanisms of collagen gene expression
    • Raghow, R., and J. P. Thompson. Molecular mechanisms of collagen gene expression. Mol. Cell. Biochem. 86: 5-18, 1989.
    • (1989) Mol. Cell. Biochem. , vol.86 , pp. 5-18
    • Raghow, R.1    Thompson, J.P.2
  • 330
    • 0021823659 scopus 로고
    • Cytochemical localization and biochemical evaluation of a lysosomal serine protease in the lung: Dipeptidyl peptidase II in normal rat
    • Randell, S. H., and P. L. Sannes. Cytochemical localization and biochemical evaluation of a lysosomal serine protease in the lung: dipeptidyl peptidase II in normal rat. J. Histochem. Cytochem. 33: 677-686, 1985.
    • (1985) J. Histochem. Cytochem. , vol.33 , pp. 677-686
    • Randell, S.H.1    Sannes, P.L.2
  • 331
    • 0026633495 scopus 로고
    • Extracellular matrix synthesis and turnover by type II pulmonary epithelial cells
    • Lung Cell. Mol. Physiol. 6
    • Rannels, D. E., S. E. Dunsmore, and R. N. Grove. Extracellular matrix synthesis and turnover by type II pulmonary epithelial cells. Am. J. Physiol. 262 (Lung Cell. Mol. Physiol. 6): L582-L589, 1992.
    • (1992) Am. J. Physiol. , vol.262
    • Rannels, D.E.1    Dunsmore, S.E.2    Grove, R.N.3
  • 332
    • 0024393169 scopus 로고
    • Influence of the extracellular matrix on type 2 cell differentiation
    • Rannels, D. E., and S. R. Rannels. Influence of the extracellular matrix on type 2 cell differentiation. Chest 96: 165-173, 1989.
    • (1989) Chest , vol.96 , pp. 165-173
    • Rannels, D.E.1    Rannels, S.R.2
  • 333
    • 0023636043 scopus 로고
    • Culture of type II pneumocytes on a type II cell-derived fibronectin-rich matrix
    • Cell Physiol. 22
    • Rannels, S. R., C. S. Fisher, L. J. Heuser, and D. E. Rannels. Culture of type II pneumocytes on a type II cell-derived fibronectin-rich matrix. Am. J. Physiol. 253 (Cell Physiol. 22): C759-C765, 1987.
    • (1987) Am. J. Physiol. , vol.253
    • Rannels, S.R.1    Fisher, C.S.2    Heuser, L.J.3    Rannels, D.E.4
  • 334
    • 0024588184 scopus 로고
    • Matrix-derived soluble components influence type II pneumocytes in primary culture
    • Cell Physiol. 25
    • Rannels, S. R., R. N. Grove, and D. E. Rannels. Matrix-derived soluble components influence type II pneumocytes in primary culture. Am. J. Physiol. 256 (Cell Physiol. 25): C621-C629, 1989.
    • (1989) Am. J. Physiol. , vol.256
    • Rannels, S.R.1    Grove, R.N.2    Rannels, D.E.3
  • 335
    • 1542605739 scopus 로고
    • Isolation and culture of alveolar type II cells for toxicological studies
    • edited by D. E. Gardner, J. D. Crapo and E. J. Massaro. New York: Raven
    • Rannels, S. R., and D. E. Rannels. Isolation and culture of alveolar type II cells for toxicological studies. In: Toxicology of the Lung, edited by D. E. Gardner, J. D. Crapo and E. J. Massaro. New York: Raven, 1988, p. 219-238.
    • (1988) Toxicology of the Lung , pp. 219-238
    • Rannels, S.R.1    Rannels, D.E.2
  • 336
    • 0024554312 scopus 로고
    • The type II pneumocyte as a model of lung cell interaction with the extracellular matrix
    • Rannels, S. R., and D. E. Rannels. The type II pneumocyte as a model of lung cell interaction with the extracellular matrix. J. Mol. Cell. Cardiol. 21, Suppl. 1: 151-159, 1989.
    • (1989) J. Mol. Cell. Cardiol. , vol.21 , Issue.1 SUPPL. , pp. 151-159
    • Rannels, S.R.1    Rannels, D.E.2
  • 337
    • 0023610817 scopus 로고
    • Role of laminin in maintenance of type II pneumocyte morphology and function
    • Cell Physiol. 22
    • Rannels, S. R., J. A. Yarnell, C. S. Fisher, J. P. Fabisiak, and D. E. Rannels. Role of laminin in maintenance of type II pneumocyte morphology and function. Am. J. Physiol. 253 (Cell Physiol. 22): C835-C845, 1987.
    • (1987) Am. J. Physiol. , vol.253
    • Rannels, S.R.1    Yarnell, J.A.2    Fisher, C.S.3    Fabisiak, J.P.4    Rannels, D.E.5
  • 339
    • 0028174283 scopus 로고
    • Primary structure of the α1 chain of mouse type XVIII collagen, partial structure of the corresponding gene, and comparison of the α1(XVIII) chain with its homologue, the α1(XV) collagen chain
    • Rehn, M., E. Hintikka, and T. Pihlajaniemi. Primary structure of the α1 chain of mouse type XVIII collagen, partial structure of the corresponding gene, and comparison of the α1(XVIII) chain with its homologue, the α1(XV) collagen chain. J. Biol. Chem. 269: 13929-13935, 1994.
    • (1994) J. Biol. Chem. , vol.269 , pp. 13929-13935
    • Rehn, M.1    Hintikka, E.2    Pihlajaniemi, T.3
  • 340
    • 0002383668 scopus 로고
    • Biology of airway epithelial cells
    • edited by R. G. Crystal and J. B. West. New York: Raven
    • Rennard, S. I., J. D. Beckmann, and R. A. Robbins. Biology of airway epithelial cells. In: The Lung, edited by R. G. Crystal and J. B. West. New York: Raven, 1991, p. 157-167.
    • (1991) The Lung , pp. 157-167
    • Rennard, S.I.1    Beckmann, J.D.2    Robbins, R.A.3
  • 341
    • 0021071294 scopus 로고
    • Response of the lower respiratory tract to injury. Mechanisms of repair of the parenchymal cells of the alveolar wall
    • Rennard, S. I., P. B. Bitterman, and R. G. Crystal. Response of the lower respiratory tract to injury. Mechanisms of repair of the parenchymal cells of the alveolar wall. Chest 84: 735-739, 1983.
    • (1983) Chest , vol.84 , pp. 735-739
    • Rennard, S.I.1    Bitterman, P.B.2    Crystal, R.G.3
  • 343
    • 0026737553 scopus 로고
    • Species diversity of neuronectin and cytotactin expression patterns in the vertebrate central nervous system
    • Retting, W. J., S. Hoffman, S. L. Su, and P. Garin-Chesa. Species diversity of neuronectin and cytotactin expression patterns in the vertebrate central nervous system. Brain Res. 590: 219-228, 1992.
    • (1992) Brain Res. , vol.590 , pp. 219-228
    • Retting, W.J.1    Hoffman, S.2    Su, S.L.3    Garin-Chesa, P.4
  • 344
    • 0027936342 scopus 로고
    • Localization of the gene (LAMA4) to chromosome 6q21 and isolation of a partial cDNA encoding A variant laminin a chain
    • Richards, A. J., L. Al-Imara, N. P. Carter, J. C. Lloyd, M.A. Leversha, and F. M. Pope. Localization of the gene (LAMA4) to chromosome 6q21 and isolation of a partial cDNA encoding a variant laminin A chain. Genomics 22: 227-239, 1994.
    • (1994) Genomics , vol.22 , pp. 227-239
    • Richards, A.J.1    Al-Imara, L.2    Carter, N.P.3    Lloyd, J.C.4    Leversha, M.A.5    Pope, F.M.6
  • 345
    • 0026165309 scopus 로고
    • Attachment characteristics of bovine bronchial epithelial cells to extracellular matrix components
    • Rickard, K. A., S. Shoji, J. R. Spurzem, and S. I. Rennard. Attachment characteristics of bovine bronchial epithelial cells to extracellular matrix components. Am. J. Respir. Cell Mol. Biol. 4: 440-448, 1991.
    • (1991) Am. J. Respir. Cell Mol. Biol. , vol.4 , pp. 440-448
    • Rickard, K.A.1    Shoji, S.2    Spurzem, J.R.3    Rennard, S.I.4
  • 348
    • 0028984957 scopus 로고
    • Cloning, characterization, and development expression of a rat lung alveolar type I cell gene in embryonic endodermal and neural derivatives
    • Rishi, A. K., M. Joyce-Brady, J. Fisher, L. G. Dobbs, J. Floros, J. VanderSpek, J. S. Brody, and M. C. Williams. Cloning, characterization, and development expression of a rat lung alveolar type I cell gene in embryonic endodermal and neural derivatives. Dev. Biol. 167: 294-306, 1995.
    • (1995) Dev. Biol. , vol.167 , pp. 294-306
    • Rishi, A.K.1    Joyce-Brady, M.2    Fisher, J.3    Dobbs, L.G.4    Floros, J.5    VanderSpek, J.6    Brody, J.S.7    Williams, M.C.8
  • 349
    • 0023926486 scopus 로고
    • Transforming growth factor β stimulates the expression of fibronectin and both subunits of the human fibronectin receptor in cultured human lung fibroblasts
    • Roberts, C. J., T. M. Birkenmeier, J. J. McQuillan, S. K. Akiyama, S. J. Yamada, W.-T. Chen, K. M. Yamada, and J. A. McDonald. Transforming growth factor β stimulates the expression of fibronectin and both subunits of the human fibronectin receptor in cultured human lung fibroblasts. J. Biol. Chem. 263: 4586-4592, 1988.
    • (1988) J. Biol. Chem. , vol.263 , pp. 4586-4592
    • Roberts, C.J.1    Birkenmeier, T.M.2    McQuillan, J.J.3    Akiyama, S.K.4    Yamada, S.J.5    Chen, W.-T.6    Yamada, K.M.7    McDonald, J.A.8
  • 351
    • 0026033356 scopus 로고
    • Reagents that inhibit fibronectin matrix assembly of cultured cells also inhibit lung branching morphogenesis in vitro. Implications for lung development, injury, and repair
    • Roman, J., E. C. Crouch, and J. A. McDonald. Reagents that inhibit fibronectin matrix assembly of cultured cells also inhibit lung branching morphogenesis in vitro. Implications for lung development, injury, and repair. Chest 99: 20S-21S, 1991.
    • (1991) Chest , vol.99
    • Roman, J.1    Crouch, E.C.2    McDonald, J.A.3
  • 352
    • 0025727577 scopus 로고
    • Potential role of RGD-binding integrins in mammalian lung branching morphogenesis
    • Roman, J., C. W. Little, and J. A. McDonald. Potential role of RGD-binding integrins in mammalian lung branching morphogenesis. Development 112: 551-558, 1991.
    • (1991) Development , vol.112 , pp. 551-558
    • Roman, J.1    Little, C.W.2    McDonald, J.A.3
  • 353
    • 0026856971 scopus 로고
    • Expression of fibronectin, the integrin α5 and α-smooth muscle actin in heart and lung development
    • Roman, J., and J. A. McDonald. Expression of fibronectin, the integrin α5 and α-smooth muscle actin in heart and lung development. Am. J. Respir. Cell Mol. Biol. 6: 472-480, 1992.
    • (1992) Am. J. Respir. Cell Mol. Biol. , vol.6 , pp. 472-480
    • Roman, J.1    McDonald, J.A.2
  • 354
    • 0028049687 scopus 로고
    • Molecular and cellular processing of lung surfactant
    • Rooney, S. A., S. L. Young, and C. R. Mendelson. Molecular and cellular processing of lung surfactant. FASEB J. 8: 957-967, 1994.
    • (1994) FASEB J. , vol.8 , pp. 957-967
    • Rooney, S.A.1    Young, S.L.2    Mendelson, C.R.3
  • 355
    • 0027422979 scopus 로고
    • Extracellular matrix 4: The elastic fiber
    • Rosenbloom, J., W. R. Abrams, and R. Mecham. Extracellular matrix 4: the elastic fiber. FASEB J. 7: 1208-1218, 1993.
    • (1993) FASEB J. , vol.7 , pp. 1208-1218
    • Rosenbloom, J.1    Abrams, W.R.2    Mecham, R.3
  • 356
    • 0020608392 scopus 로고
    • Light-microscopic immunocytochemical localization of fibronectin in the developing rat lung
    • Rosenkrans, W. A., Jr., J. T. Albright, R. E. Hausman, and D. P. Penney. Light-microscopic immunocytochemical localization of fibronectin in the developing rat lung. Cell Tissue Res. 233: 113-123, 1983.
    • (1983) Cell Tissue Res. , vol.233 , pp. 113-123
    • Rosenkrans Jr., W.A.1    Albright, J.T.2    Hausman, R.E.3    Penney, D.P.4
  • 357
    • 0021037665 scopus 로고
    • Ultrastructural immunocytochemical localization of fibronectin in the developing rat lung
    • Rosenkrans, W. A., Jr., J. T. Albright, R. E. Hausman, and D. P. Penney. Ultrastructural immunocytochemical localization of fibronectin in the developing rat lung. Cell Tissue Res. 234: 165-177, 1983.
    • (1983) Cell Tissue Res. , vol.234 , pp. 165-177
    • Rosenkrans Jr., W.A.1    Albright, J.T.2    Hausman, R.E.3    Penney, D.P.4
  • 358
    • 0024008629 scopus 로고
    • Flow cytometric analysis of cell-surface binding elements for fibronectin on mouse lung cell isolates
    • Rosenkrans, W. A., Jr., D. P. Penney, and J. F. Leary. Flow cytometric analysis of cell-surface binding elements for fibronectin on mouse lung cell isolates. Cell Biol. Int. Reports 12: 337-346, 1988.
    • (1988) Cell Biol. Int. Reports , vol.12 , pp. 337-346
    • Rosenkrans Jr., W.A.1    Penney, D.P.2    Leary, J.F.3
  • 359
    • 0025879967 scopus 로고
    • Kalinin: An epithelium-specific basement membrane adhesion molecule that is a component of anchoring filaments
    • Rousselle, P., G. P. Lunstrum, D. R. Keene, and R. E. Burgeson. Kalinin: an epithelium-specific basement membrane adhesion molecule that is a component of anchoring filaments. J. Cell Biol. 114: 567-576, 1991.
    • (1991) J. Cell Biol. , vol.114 , pp. 567-576
    • Rousselle, P.1    Lunstrum, G.P.2    Keene, D.R.3    Burgeson, R.E.4
  • 360
    • 0023920076 scopus 로고
    • Fibronectin and its receptors
    • Ruoslahti, E. Fibronectin and its receptors. Annu. Rev. Biochem. 57: 375-413, 1988.
    • (1988) Annu. Rev. Biochem. , vol.57 , pp. 375-413
    • Ruoslahti, E.1
  • 362
    • 0024599959 scopus 로고
    • Coordinate induction of fibronectin, fibronectin receptor, tropomyosin, and actin genes in serum-stimulated fibroblasts
    • Ryseck, R.-P., H. MacDonald-Bravo, M. Zerial, and R. Bravo. Coordinate induction of fibronectin, fibronectin receptor, tropomyosin, and actin genes in serum-stimulated fibroblasts. Exp. Cell Res. 180: 537-545, 1989.
    • (1989) Exp. Cell Res. , vol.180 , pp. 537-545
    • Ryseck, R.-P.1    MacDonald-Bravo, H.2    Zerial, M.3    Bravo, R.4
  • 364
    • 0020584332 scopus 로고
    • Granular pneumocytes in primary culture secrete several major components of the extracellular matrix
    • Sage, H., F. M. Farin, G. E. Striker, and A. B. Fisher. Granular pneumocytes in primary culture secrete several major components of the extracellular matrix. Biochemistry 22: 2148-2155, 1983.
    • (1983) Biochemistry , vol.22 , pp. 2148-2155
    • Sage, H.1    Farin, F.M.2    Striker, G.E.3    Fisher, A.B.4
  • 365
    • 0025298544 scopus 로고
    • Type VIII collagen in murine development. Association with capillary formation in vitro
    • Sage, H., and M. L. Iruela-Arispe. Type VIII collagen in murine development. Association with capillary formation in vitro. Ann. NYAcad. Sci. 580: 17-31, 1990.
    • (1990) Ann. NYAcad. Sci. , vol.580 , pp. 17-31
    • Sage, H.1    Iruela-Arispe, M.L.2
  • 366
    • 0019253897 scopus 로고
    • A unique, pepsinsensitive collagen synthesized by aortic endothelial cells in culture
    • Sage, H., P. Pritzl, and P. Bornstein. A unique, pepsinsensitive collagen synthesized by aortic endothelial cells in culture. Biochemistry 19: 5747-5756, 1980.
    • (1980) Biochemistry , vol.19 , pp. 5747-5756
    • Sage, H.1    Pritzl, P.2    Bornstein, P.3
  • 367
    • 0019230915 scopus 로고
    • Isolation and characterization of glycosaminoglycans secreted by human foetal lung type II pneumocytes in culture
    • Sahu, S., K. Tanswell, and W. S. Lynn. Isolation and characterization of glycosaminoglycans secreted by human foetal lung type II pneumocytes in culture. J. Cell Sci. 42: 183-188, 1980.
    • (1980) J. Cell Sci. , vol.42 , pp. 183-188
    • Sahu, S.1    Tanswell, K.2    Lynn, W.S.3
  • 368
    • 0023002893 scopus 로고
    • Fibrillin, a new 350-kD glycoprotein, is a component of extracellular microfibrils
    • Sakai, L. Y., D. R. Keene, and E. Engvall. Fibrillin, a new 350-kD glycoprotein, is a component of extracellular microfibrils. J. Cell Biol. 103: 2499-2509, 1986.
    • (1986) J. Cell Biol. , vol.103 , pp. 2499-2509
    • Sakai, L.Y.1    Keene, D.R.2    Engvall, E.3
  • 369
    • 0023035458 scopus 로고
    • Type VII collagen is a major structural component of anchoring fibrils
    • Sakai, L. Y., D. R. Keene, N. P. Morris, and R. E. Burgeson. Type VII collagen is a major structural component of anchoring fibrils. J. Cell Biol. 103: 1577-1586, 1986.
    • (1986) J. Cell Biol. , vol.103 , pp. 1577-1586
    • Sakai, L.Y.1    Keene, D.R.2    Morris, N.P.3    Burgeson, R.E.4
  • 370
    • 0024261808 scopus 로고
    • Degradative processes of connective tissue proteins with special emphasis on collagenolysis and bone resorption
    • Sakamoto, S., and M. Sakamoto. Degradative processes of connective tissue proteins with special emphasis on collagenolysis and bone resorption. Mol. Aspects Med. 10: 301-428, 1988.
    • (1988) Mol. Aspects Med. , vol.10 , pp. 301-428
    • Sakamoto, S.1    Sakamoto, M.2
  • 371
    • 0024146930 scopus 로고
    • Cell-associated plasminogen activation: Regulation and physiological functions
    • Saksela, O., and D. B. Rifkin. Cell-associated plasminogen activation: regulation and physiological functions. Annu. Rev. Cell Biol. 4: 93-126, 1988.
    • (1988) Annu. Rev. Cell Biol. , vol.4 , pp. 93-126
    • Saksela, O.1    Rifkin, D.B.2
  • 372
    • 0021195598 scopus 로고
    • Lammin interacts with plasminogen and its tissue-type activator
    • Salonen, E. M., A. Zitting, and A. Vaheri. Lammin interacts with plasminogen and its tissue-type activator. FEBS Lett. 172: 29-32, 1984.
    • (1984) FEBS Lett. , vol.172 , pp. 29-32
    • Salonen, E.M.1    Zitting, A.2    Vaheri, A.3
  • 373
    • 0021261922 scopus 로고
    • Differences in basement membrane microdomains of type I and type II pneumocytes in the rat and rabbit lung
    • Sannes, P. L. Differences in basement membrane microdomains of type I and type II pneumocytes in the rat and rabbit lung. J. Histochem. Cytochem. 32: 827-833, 1984.
    • (1984) J. Histochem. Cytochem. , vol.32 , pp. 827-833
    • Sannes, P.L.1
  • 374
    • 0025914107 scopus 로고
    • Structural and functional relationships between type II pneumocytes and components of extracellular matrices
    • Sannes, P. L. Structural and functional relationships between type II pneumocytes and components of extracellular matrices. Exp. Lung Res. 17: 639-659, 1991.
    • (1991) Exp. Lung Res. , vol.17 , pp. 639-659
    • Sannes, P.L.1
  • 375
    • 0027570234 scopus 로고
    • Immunohistochemical localization of chondroitin sulfate, chondroitin sulfate proteoglycan, heparan sulfate proteoglycan, entactin, and laminin in basement membranes of postnatal developing and adult rat lungs
    • Sannes, P. L., K. K. Burch, J. Khosla, K. J. McCarthy, and J. R. Couchman. Immunohistochemical localization of chondroitin sulfate, chondroitin sulfate proteoglycan, heparan sulfate proteoglycan, entactin, and laminin in basement membranes of postnatal developing and adult rat lungs. Am. J. Respir. Cell Mol. Biol. 8: 245-251, 1993.
    • (1993) Am. J. Respir. Cell Mol. Biol. , vol.8 , pp. 245-251
    • Sannes, P.L.1    Burch, K.K.2    Khosla, J.3    McCarthy, K.J.4    Couchman, J.R.5
  • 376
    • 0025963535 scopus 로고
    • Molecular interactions of isolated rat type II pneumocytes with components of extracellular matrices in vitro
    • Sannes, P. L., B. Peters, and K. B. Adler. Molecular interactions of isolated rat type II pneumocytes with components of extracellular matrices in vitro. Chest 99: 70S-71S, 1991.
    • (1991) Chest , vol.99
    • Sannes, P.L.1    Peters, B.2    Adler, K.B.3
  • 377
    • 0023701420 scopus 로고
    • Laminin, a multidomain protein. The A chain has a unique globular domain and homology with the basement membrane proteoglycan and the laminin B chains
    • Sasaki, M., H. K. Kleinman, H. Huber, R. Deutzmann, and Y. Yamada. Laminin, a multidomain protein. The A chain has a unique globular domain and homology with the basement membrane proteoglycan and the laminin B chains. J. Biol. Chem. 263: 16536-16544, 1988.
    • (1988) J. Biol. Chem. , vol.263 , pp. 16536-16544
    • Sasaki, M.1    Kleinman, H.K.2    Huber, H.3    Deutzmann, R.4    Yamada, Y.5
  • 378
    • 0028815977 scopus 로고
    • Structural characterization of two variants of fibulin-1 that differ in nidogen affinity
    • Sasaki, T., G. Kostka, W. Gohring, H. Wiedemann, K. Mann, M. L. Chu, and R. Timpl. Structural characterization of two variants of fibulin-1 that differ in nidogen affinity. J. Mol. Biol. 245: 241-250, 1995.
    • (1995) J. Mol. Biol. , vol.245 , pp. 241-250
    • Sasaki, T.1    Kostka, G.2    Gohring, W.3    Wiedemann, H.4    Mann, K.5    Chu, M.L.6    Timpl, R.7
  • 379
    • 0027679403 scopus 로고
    • Integrin cytoplasmic domains: Mediators of cytoskeletal linkages and extra- and intracellular initiated transmembrane signaling
    • Sastry, S. K., and A. F. Horwitz. Integrin cytoplasmic domains: mediators of cytoskeletal linkages and extra- and intracellular initiated transmembrane signaling. Curr. Opin. Cell Biol. 5: 819-831, 1993.
    • (1993) Curr. Opin. Cell Biol. , vol.5 , pp. 819-831
    • Sastry, S.K.1    Horwitz, A.F.2
  • 381
    • 0025117435 scopus 로고
    • Characterization of the collagen in the hexagonal lattice of Descemet's membrane: Its relation to type VIII collagen
    • Sawada, H., H. Konomi, and K. Hirosawa. Characterization of the collagen in the hexagonal lattice of Descemet's membrane: its relation to type VIII collagen. J. Cell Biol. 110: 219-227, 1990.
    • (1990) J. Cell Biol. , vol.110 , pp. 219-227
    • Sawada, H.1    Konomi, H.2    Hirosawa, K.3
  • 382
    • 0028122650 scopus 로고
    • Focal adhesion kinase and associated proteins
    • Schaller, M. D., and J. T. Parsons. Focal adhesion kinase and associated proteins. Curr. Opin. Cell Biol. 6: 705-710, 1994.
    • (1994) Curr. Opin. Cell Biol. , vol.6 , pp. 705-710
    • Schaller, M.D.1    Parsons, J.T.2
  • 383
    • 0028609382 scopus 로고
    • Integrin-mediated signal transduction linked to Ras pathway by GRB2 binding to focal adhesion kinase
    • Schlaepfer, D. D., S. K. Hanks, T. Hunter, and P. van der Geer. Integrin-mediated signal transduction linked to Ras pathway by GRB2 binding to focal adhesion kinase. Nature Lond. 372: 786-791, 1994.
    • (1994) Nature Lond. , vol.372 , pp. 786-791
    • Schlaepfer, D.D.1    Hanks, S.K.2    Hunter, T.3    Van Der Geer, P.4
  • 384
    • 0025219168 scopus 로고
    • Immunoelectron microscopy of type X collagen: Supramolecular forms with embryonic chick cartilage
    • Schmid, T. M., and T. F. Linsenmayer. Immunoelectron microscopy of type X collagen: supramolecular forms with embryonic chick cartilage. Dev. Biol. 138: 53-62, 1990.
    • (1990) Dev. Biol. , vol.138 , pp. 53-62
    • Schmid, T.M.1    Linsenmayer, T.F.2
  • 385
    • 0027057123 scopus 로고
    • A novel transcriptional enhancer is involved in the prolactin- and extracellular matrix-dependent regulation of β-casein gene expression
    • Schmidhauser, C., G. F. Casperson, C. A. Myers, K. T. Sanzo, S. Bolten, and M. J. Bissell. A novel transcriptional enhancer is involved in the prolactin- and extracellular matrix-dependent regulation of β-casein gene expression. Mol. Biol. Cell 3: 699-709, 1992.
    • (1992) Mol. Biol. Cell , vol.3 , pp. 699-709
    • Schmidhauser, C.1    Casperson, G.F.2    Myers, C.A.3    Sanzo, K.T.4    Bolten, S.5    Bissell, M.J.6
  • 386
    • 0025349558 scopus 로고
    • Extracellular accumulation of small dermatan sulphate proteoglycan II by interference with a secretion-recapture pathway
    • Schmidt, G., H. Hausser, and H. Kresse. Extracellular accumulation of small dermatan sulphate proteoglycan II by interference with a secretion-recapture pathway. Biochem. J. 266: 591-595, 1990.
    • (1990) Biochem. J. , vol.266 , pp. 591-595
    • Schmidt, G.1    Hausser, H.2    Kresse, H.3
  • 387
    • 0027403241 scopus 로고
    • Regulation of cell function by extracellular matrix
    • Schnaper, H. W., and H. K. Eleinman. Regulation of cell function by extracellular matrix. Pediatr. Nephrol. 7: 96-104, 1993.
    • (1993) Pediatr. Nephrol. , vol.7 , pp. 96-104
    • Schnaper, H.W.1    Eleinman, H.K.2
  • 388
    • 0000105857 scopus 로고
    • Alveolar type I cells
    • edited by R. G. Crystal and J. B. West. New York: Raven
    • Schneeberger, E. E. Alveolar type I cells. In: The Lung, edited by R. G. Crystal and J. B. West. New York: Raven, 1991, p. 229-234.
    • (1991) The Lung , pp. 229-234
    • Schneeberger, E.E.1
  • 389
    • 0025685314 scopus 로고
    • Organotypic arrangement of mouse embryonic lung cells on a basement membrane extract: Involvement of laminin
    • Schuger, L., K. S. O'Shea, B. B. Nelson, and J. Varani. Organotypic arrangement of mouse embryonic lung cells on a basement membrane extract: involvement of laminin. Development 110: 1091-1099, 1990.
    • (1990) Development , vol.110 , pp. 1091-1099
    • Schuger, L.1    O'Shea, K.S.2    Nelson, B.B.3    Varani, J.4
  • 390
    • 0025060221 scopus 로고
    • Laminin in lung development: Effects of anti-laminin antibody in murine morphogenesis
    • Schuger, L., S. O'Shea, J. Rheinheimer, and J. Varani. Laminin in lung development: effects of anti-laminin antibody in murine morphogenesis. Dev. Biol. 137: 26-32, 1990.
    • (1990) Dev. Biol. , vol.137 , pp. 26-32
    • Schuger, L.1    O'Shea, S.2    Rheinheimer, J.3    Varani, J.4
  • 391
    • 0025870487 scopus 로고
    • Identification of laminin domains involved in branching morphogenesis: Effects of anti-laminin monoclonal antibodies on mouse embryonic lung development
    • Schuger, L., A. P. Skubitz, K. S. O'Shea, J. F. Chang, and J. Varani. Identification of laminin domains involved in branching morphogenesis: effects of anti-laminin monoclonal antibodies on mouse embryonic lung development. Dev. Biol. 146: 531-541, 1991.
    • (1991) Dev. Biol. , vol.146 , pp. 531-541
    • Schuger, L.1    Skubitz, A.P.2    O'Shea, K.S.3    Chang, J.F.4    Varani, J.5
  • 392
    • 0027076656 scopus 로고
    • Laminin expression in the mouse lung increases with development and stimulates spontaneous organotypic rearrangement of mixed lung cells
    • Schuger, L., J. Varani, P. D. Killen, A. P. Skubitz, and K. Gilbride. Laminin expression in the mouse lung increases with development and stimulates spontaneous organotypic rearrangement of mixed lung cells. Dev. Dynamics 195: 43-54, 1992.
    • (1992) Dev. Dynamics , vol.195 , pp. 43-54
    • Schuger, L.1    Varani, J.2    Killen, P.D.3    Skubitz, A.P.4    Gilbride, K.5
  • 393
    • 0025741871 scopus 로고
    • Multiple integrins share the ability to induce elevation of intracellular pH
    • Schwartz, M. A., D. E. Ingber, M. Lawrence, T.A. Springer, and C. Lechene. Multiple integrins share the ability to induce elevation of intracellular pH. Exp. Cell Res. 195: 533-535, 1991.
    • (1991) Exp. Cell Res. , vol.195 , pp. 533-535
    • Schwartz, M.A.1    Ingber, D.E.2    Lawrence, M.3    Springer, T.A.4    Lechene, C.5
  • 395
    • 0025896188 scopus 로고
    • Identification of the fibronectin sequences required for assembly of a fibrillar matrix
    • Schwarzbauer, J. E. Identification of the fibronectin sequences required for assembly of a fibrillar matrix. J. Cell Biol. 113: 1463-1473, 1991.
    • (1991) J. Cell Biol. , vol.113 , pp. 1463-1473
    • Schwarzbauer, J.E.1
  • 396
    • 0023409308 scopus 로고
    • Multiple sites of alternative splicing of the rat fibronectin gene transcript
    • Schwarzbauer, J. E., R. S. Patel, D. Fonda, and R. O. Hynes. Multiple sites of alternative splicing of the rat fibronectin gene transcript. EMBO J. 6: 2573-2580, 1987.
    • (1987) EMBO J. , vol.6 , pp. 2573-2580
    • Schwarzbauer, J.E.1    Patel, R.S.2    Fonda, D.3    Hynes, R.O.4
  • 397
    • 0028200338 scopus 로고
    • Entactin gene expression in normal and fibrotic rat liver and in rat liver cells
    • Schwoengler, S., K. Neubauer, T. Knittel, A. E. Chung, and G. Ramadori. Entactin gene expression in normal and fibrotic rat liver and in rat liver cells. Lab. Invest. 70: 525-536, 1994.
    • (1994) Lab. Invest. , vol.70 , pp. 525-536
    • Schwoengler, S.1    Neubauer, K.2    Knittel, T.3    Chung, A.E.4    Ramadori, G.5
  • 398
    • 0023697305 scopus 로고
    • Cellular fibronectin is induced by epidermal growth factor, but not by dexamethasone or cyclic AMP in rat liver epithelial cells
    • Seebacher, T., M. Manske, A. R. Kornblihtt, and E. G. Bade. Cellular fibronectin is induced by epidermal growth factor, but not by dexamethasone or cyclic AMP in rat liver epithelial cells. FEBS Lett. 239: 113-116, 1988.
    • (1988) FEBS Lett. , vol.239 , pp. 113-116
    • Seebacher, T.1    Manske, M.2    Kornblihtt, A.R.3    Bade, E.G.4
  • 401
    • 0025378574 scopus 로고
    • Effect of a reconstituted basement membrane on expression of surfactant apoproteins in cultured adult rat alveolar type II cells
    • Shannon, J. M., P. A. Emrie, J. H. Fisher, Y. Kuroki, S. D. Jennings, and R. J. Mason. Effect of a reconstituted basement membrane on expression of surfactant apoproteins in cultured adult rat alveolar type II cells. Am. J. Respir. Cell Mol. Biol. 2: 183-192, 1990.
    • (1990) Am. J. Respir. Cell Mol. Biol. , vol.2 , pp. 183-192
    • Shannon, J.M.1    Emrie, P.A.2    Fisher, J.H.3    Kuroki, Y.4    Jennings, S.D.5    Mason, R.J.6
  • 402
    • 0026721489 scopus 로고
    • Modulation of alveolar type II cell differentiated function in vitro
    • Lung Cell. Mol. Physiol. 6
    • Shannon, J. M., S. D. Jennings, and L. D. Nielsen. Modulation of alveolar type II cell differentiated function in vitro. Am. J. Physiol. 262 (Lung Cell. Mol. Physiol. 6): L427-L436, 1992.
    • (1992) Am. J. Physiol. , vol.262
    • Shannon, J.M.1    Jennings, S.D.2    Nielsen, L.D.3
  • 403
    • 0023652128 scopus 로고
    • Functional differentiation of alveolar type II epithelial cells in vitro: Effects of cell shape, cell-matrix interactions, and cell-cell interactions
    • Shannon, J. M., R. J. Mason, and S. D. Jennings. Functional differentiation of alveolar type II epithelial cells in vitro: effects of cell shape, cell-matrix interactions, and cell-cell interactions. Biochim. Biophys. Acta 931: 143-156, 1987.
    • (1987) Biochim. Biophys. Acta , vol.931 , pp. 143-156
    • Shannon, J.M.1    Mason, R.J.2    Jennings, S.D.3
  • 405
    • 0027515289 scopus 로고
    • Cloning and characterization of a unique elastolytic metalloproteinase produced by human alveolar macrophages
    • Shapiro, S. D., D. K. Kobayashi, and T. Ley. Cloning and characterization of a unique elastolytic metalloproteinase produced by human alveolar macrophages. J. Biol. Chem. 268: 23824-23829, 1993.
    • (1993) J. Biol. Chem. , vol.268 , pp. 23824-23829
    • Shapiro, S.D.1    Kobayashi, D.K.2    Ley, T.3
  • 406
    • 0025828716 scopus 로고
    • FACIT collagens: Diverse molecular bridges in extracellular matrices
    • Shaw, L. M., and B. R. Olsen. FACIT collagens: diverse molecular bridges in extracellular matrices. Trends Biochem. Sci. 16: 191-194, 1991.
    • (1991) Trends Biochem. Sci. , vol.16 , pp. 191-194
    • Shaw, L.M.1    Olsen, B.R.2
  • 407
    • 0027138128 scopus 로고
    • Identification and characterization of novel airway epithelial integrins
    • Sheppard, D. Identification and characterization of novel airway epithelial integrins. Am. Rev. Respir. Dis. 148: S38-S42, 1993.
    • (1993) Am. Rev. Respir. Dis. , vol.148
    • Sheppard, D.1
  • 411
    • 85047677284 scopus 로고
    • Presence of lysosomal enzymes in normal glomerular basement membrane matrix
    • Singh, A. K. Presence of lysosomal enzymes in normal glomerular basement membrane matrix. Histochem. J. 25: 562-568, 1993.
    • (1993) Histochem. J. , vol.25 , pp. 562-568
    • Singh, A.K.1
  • 413
    • 0027444528 scopus 로고
    • Degradation of entactin by matrix metalloproteinases. Susceptibility to matrilysin and identification of cleavage sites
    • Sires, U. I., G. L. Griffin, T. J. Broekelmann, R. P. Mecham, G. Murphy, A. E. Chung, H. G. Welgus, and R. M. Senior. Degradation of entactin by matrix metalloproteinases. Susceptibility to matrilysin and identification of cleavage sites. J. Biol. Chem. 268: 2069-2074, 1993.
    • (1993) J. Biol. Chem. , vol.268 , pp. 2069-2074
    • Sires, U.I.1    Griffin, G.L.2    Broekelmann, T.J.3    Mecham, R.P.4    Murphy, G.5    Chung, A.E.6    Welgus, H.G.7    Senior, R.M.8
  • 414
    • 0024521228 scopus 로고
    • Transferrin stimulates proteoglycan accumulation by fetal lung cells in culture
    • Skinner, S. J. M., C. J. Ashby, and G. C. Liggins. Transferrin stimulates proteoglycan accumulation by fetal lung cells in culture. Exp. Lung Res. 15: 269-283, 1989.
    • (1989) Exp. Lung Res. , vol.15 , pp. 269-283
    • Skinner, S.J.M.1    Ashby, C.J.2    Liggins, G.C.3
  • 415
    • 0023280228 scopus 로고
    • Characterization of proteoglycans synthesized by fetal rat lung type II pneumocytes in vitro and the effects of Cortisol
    • Skinner, S. J. M., M. Post, J. S. Torday, A. D. Stiles, and B. T. Smith. Characterization of proteoglycans synthesized by fetal rat lung type II pneumocytes in vitro and the effects of Cortisol. Exp. Lung Res. 12: 253-264, 1987.
    • (1987) Exp. Lung Res. , vol.12 , pp. 253-264
    • Skinner, S.J.M.1    Post, M.2    Torday, J.S.3    Stiles, A.D.4    Smith, B.T.5
  • 417
    • 0025609382 scopus 로고
    • Definition of a sequence, RYVVLPR, within laminin peptide F-9 that mediates metastatic fibrosarcoma cell adhesion and spreading
    • Skubitz, A. P., J. B. McCarthy, Q. Zhao, X. Y. Yi, and L. T. Furcht. Definition of a sequence, RYVVLPR, within laminin peptide F-9 that mediates metastatic fibrosarcoma cell adhesion and spreading. Cancer Res. 50: 7612-7622, 1990.
    • (1990) Cancer Res. , vol.50 , pp. 7612-7622
    • Skubitz, A.P.1    McCarthy, J.B.2    Zhao, Q.3    Yi, X.Y.4    Furcht, L.T.5
  • 418
    • 0027530551 scopus 로고
    • Regulation of expression of the type I collagen genes
    • Slack, J. L., D. J. Liska, and P. Bornstein. Regulation of expression of the type I collagen genes. Am. J. Med. Genet. 45: 140-151, 1993.
    • (1993) Am. J. Med. Genet. , vol.45 , pp. 140-151
    • Slack, J.L.1    Liska, D.J.2    Bornstein, P.3
  • 419
    • 0021795701 scopus 로고
    • Endocytosis and degradation of chondroitin sulphate by liver endothelial cells
    • Smedsrod, B., L. Kjellen, and H. Perfort. Endocytosis and degradation of chondroitin sulphate by liver endothelial cells. Biochem. J. 229: 63-71, 1985.
    • (1985) Biochem. J. , vol.229 , pp. 63-71
    • Smedsrod, B.1    Kjellen, L.2    Perfort, H.3
  • 420
    • 0023927631 scopus 로고
    • Morphological studies on endocytosis of chondroitin sulphate proteoglycan by rat liver endothelial cells
    • Smedsrod, B., M. Malmgren, J. Ericsson, and T. C. Laurent. Morphological studies on endocytosis of chondroitin sulphate proteoglycan by rat liver endothelial cells. Cells Tissue Res. 253: 39-45, 1988.
    • (1988) Cells Tissue Res. , vol.253 , pp. 39-45
    • Smedsrod, B.1    Malmgren, M.2    Ericsson, J.3    Laurent, T.C.4
  • 422
    • 0027364276 scopus 로고
    • Protein kinase C modulation of fibronectin matrix assembly
    • Somers, C. E., and D. F. Mosher. Protein kinase C modulation of fibronectin matrix assembly J. Biol. Chem. 268: 22277-22280, 1993.
    • (1993) J. Biol. Chem. , vol.268 , pp. 22277-22280
    • Somers, C.E.1    Mosher, D.F.2
  • 424
    • 0017362069 scopus 로고
    • Immunocytoehemical localization of lysozymes in respiratory and other tissues
    • Spicer, S. S., R. Frayser, G. Virella, and B. J. Hall. Immunocytoehemical localization of lysozymes in respiratory and other tissues. Lab. Invest. 36: 282-295, 1977.
    • (1977) Lab. Invest. , vol.36 , pp. 282-295
    • Spicer, S.S.1    Frayser, R.2    Virella, G.3    Hall, B.J.4
  • 425
    • 0026589779 scopus 로고
    • Binding of human plasminogen to basement membrane (type IV) collagen
    • Stack, M. S., T. L. Moser, and S. V. Pizzo. Binding of human plasminogen to basement membrane (type IV) collagen. Biochem. J. 284: 103-108, 1992.
    • (1992) Biochem. J. , vol.284 , pp. 103-108
    • Stack, M.S.1    Moser, T.L.2    Pizzo, S.V.3
  • 426
    • 0017165234 scopus 로고
    • Purification and comparison of elastins from different animal species
    • Starcher, B. C., and M. J. Galione. Purification and comparison of elastins from different animal species. Anal. Biochem. 74: 441-447, 1976.
    • (1976) Anal. Biochem. , vol.74 , pp. 441-447
    • Starcher, B.C.1    Galione, M.J.2
  • 427
    • 0027232776 scopus 로고
    • Laminin cleavage by activated human neutrophils yields proteolytic fragments with selective migratory properties
    • Steadman, R., M. H. Irwin, P. L. St. John, W. D. Blackburn, L. W. Heck, and D. R. Abrahamson. Laminin cleavage by activated human neutrophils yields proteolytic fragments with selective migratory properties. J. Leukocyte Biol. 53: 354-365, 1993.
    • (1993) J. Leukocyte Biol. , vol.53 , pp. 354-365
    • Steadman, R.1    Irwin, M.H.2    St John, P.L.3    Blackburn, W.D.4    Heck, L.W.5    Abrahamson, D.R.6
  • 428
    • 0017811523 scopus 로고
    • Distribution of a major connective tissue protein, fibronectin, in normal human tissues
    • Stenman, S., and A. Vaheri. Distribution of a major connective tissue protein, fibronectin, in normal human tissues. J. Exp. Med. 147: 1054-1064, 1978
    • (1978) J. Exp. Med. , vol.147 , pp. 1054-1064
    • Stenman, S.1    Vaheri, A.2
  • 430
    • 0027333411 scopus 로고
    • Tumor cell interactions with the extracellular matrix during invasion and metastasis
    • Stetler-Stevenson, W. G., S. Aznavoorian, and L. A. Liotta. Tumor cell interactions with the extracellular matrix during invasion and metastasis. Annu. Rev. Cell Biol. 9: 541-573, 1993.
    • (1993) Annu. Rev. Cell Biol. , vol.9 , pp. 541-573
    • Stetler-Stevenson, W.G.1    Aznavoorian, S.2    Liotta, L.A.3
  • 431
    • 0028229692 scopus 로고
    • The role of the extracellular matrix in tumor cell metastasis
    • Stracke, M. L., J. Murata, S. Aznavoorian, and L. A. Liotta. The role of the extracellular matrix in tumor cell metastasis. In Vivo 8: 49-58, 1994.
    • (1994) In Vivo , vol.8 , pp. 49-58
    • Stracke, M.L.1    Murata, J.2    Aznavoorian, S.3    Liotta, L.A.4
  • 432
    • 0027613368 scopus 로고
    • Extracellular matrix and gene expression in mammary epithelium
    • Streuli, C. H. Extracellular matrix and gene expression in mammary epithelium. Semin. Cell Biol. 4: 203-212, 1993.
    • (1993) Semin. Cell Biol. , vol.4 , pp. 203-212
    • Streuli, C.H.1
  • 434
    • 0027303306 scopus 로고
    • The effect of fibronectin on cytoskeleton structure and transepithelial resistance of alveolar type II cells in primary culture
    • Sugahara, K., T. Kiyota, R. A. F. Clark, and R. J. Mason. The effect of fibronectin on cytoskeleton structure and transepithelial resistance of alveolar type II cells in primary culture. Virchows Arch. B Cell Pathol. 64: 115-122, 1993.
    • (1993) Virchows Arch. B Cell Pathol. , vol.64 , pp. 115-122
    • Sugahara, K.1    Kiyota, T.2    Clark, R.A.F.3    Mason, R.J.4
  • 435
    • 0027724684 scopus 로고
    • Reconstruction of alveolus-like structure from alveolar type II epithelial cells in three-dimensional collagen gel matrix culture
    • Sugihara, H., S. Toda, S. Miyabara, C. Fujiyama, and N. Yonemitsu. Reconstruction of alveolus-like structure from alveolar type II epithelial cells in three-dimensional collagen gel matrix culture. Am. J. Pathol. 142: 783-792, 1993.
    • (1993) Am. J. Pathol. , vol.142 , pp. 783-792
    • Sugihara, H.1    Toda, S.2    Miyabara, S.3    Fujiyama, C.4    Yonemitsu, N.5
  • 437
    • 0023019712 scopus 로고
    • Immunoelectron microscopic observations on the localization of fibronectin in normal human lung
    • Takusagawa, K., N. Asoo, T. Sato, H. Nagai, M. Motomiya, and K. Konno. Immunoelectron microscopic observations on the localization of fibronectin in normal human lung. Tohoku J. Exp. Med. 150: 209-223, 1986.
    • (1986) Tohoku J. Exp. Med. , vol.150 , pp. 209-223
    • Takusagawa, K.1    Asoo, N.2    Sato, T.3    Nagai, H.4    Motomiya, M.5    Konno, K.6
  • 438
    • 0020569136 scopus 로고
    • Plasma fibronectin is synthesized and secreted by hepatocytes
    • Tamkun, J. W., and R. O. Hynes. Plasma fibronectin is synthesized and secreted by hepatocytes. J. Biol. Chem. 258: 4641-4647, 1983.
    • (1983) J. Biol. Chem. , vol.258 , pp. 4641-4647
    • Tamkun, J.W.1    Hynes, R.O.2
  • 439
    • 0025769411 scopus 로고
    • Limited division of low-density adult rat type II pneumocytes in serum-free culture
    • Lung Cell. Mol. Physiol. 4
    • Tanswell, A. K., P. J. Byrne, R. N. Han, J. D. Edelson, and V. K. Han. Limited division of low-density adult rat type II pneumocytes in serum-free culture. Am. J. Physiol. 260 (Lung Cell. Mol. Physiol. 4): L395-L402, 1991.
    • (1991) Am. J. Physiol. , vol.260
    • Tanswell, A.K.1    Byrne, P.J.2    Han, R.N.3    Edelson, J.D.4    Han, V.K.5
  • 440
    • 0027279422 scopus 로고
    • Genes coding for basement membrane glycoproteins laminin, nidogen, and collagen IV are differentially expressed in the nervous system and by epithelial, endothelial and mesenchymal cells of the mouse embryo
    • Thomas, T., and M. Dziadek. Genes coding for basement membrane glycoproteins laminin, nidogen, and collagen IV are differentially expressed in the nervous system and by epithelial, endothelial and mesenchymal cells of the mouse embryo. Exp. Cell Res. 208: 54-67, 1993.
    • (1993) Exp. Cell Res. , vol.208 , pp. 54-67
    • Thomas, T.1    Dziadek, M.2
  • 441
    • 0028175622 scopus 로고
    • Expression of collagen alpha I(IV), laminin and nidogen genes in the embryonic mouse lung: Implications for branching morphogenesis
    • Thomas, T., and M. Dziadek. Expression of collagen alpha I(IV), laminin and nidogen genes in the embryonic mouse lung: implications for branching morphogenesis. Mech. Dev. 45: 193-201, 1994.
    • (1994) Mech. Dev. , vol.45 , pp. 193-201
    • Thomas, T.1    Dziadek, M.2
  • 442
    • 0027151901 scopus 로고
    • Proteoglycans of basement membranes
    • Timpl, R. Proteoglycans of basement membranes. Experientia Basel 49: 417-428, 1993.
    • (1993) Experientia Basel , vol.49 , pp. 417-428
    • Timpl, R.1
  • 443
  • 445
    • 0019781637 scopus 로고
    • A network model for the organization of type IV collagen molecules in basement membranes
    • Timpl, R., H. Wiedmann, V. van Delden, H. Furthmayr, and K. Kuhn. A network model for the organization of type IV collagen molecules in basement membranes. Eur. J. Biochem. 120: 203-211, 1981.
    • (1981) Eur. J. Biochem. , vol.120 , pp. 203-211
    • Timpl, R.1    Wiedmann, H.2    Van Delden, V.3    Furthmayr, H.4    Kuhn, K.5
  • 446
    • 0021868083 scopus 로고
    • Ultrastructural distribution of fibronectin in normal and fibrotic human lung
    • Torikata, C., B. Villiger, C. Kuhn, and J. A. McDonald. Ultrastructural distribution of fibronectin in normal and fibrotic human lung. Lab. Invest. 52: 399-408, 1985.
    • (1985) Lab. Invest. , vol.52 , pp. 399-408
    • Torikata, C.1    Villiger, B.2    Kuhn, C.3    McDonald, J.A.4
  • 448
    • 0027832390 scopus 로고
    • Integrins: A review of their structure and mechanisms of ligand binding
    • Tuckwell, D. S., S. A. Weston, and M. J. Humphries. Integrins: a review of their structure and mechanisms of ligand binding. Symp. Soc. Exp. Biol. 47: 107-136, 1993.
    • (1993) Symp. Soc. Exp. Biol. , vol.47 , pp. 107-136
    • Tuckwell, D.S.1    Weston, S.A.2    Humphries, M.J.3
  • 449
    • 0026014727 scopus 로고
    • DNA distribution analysis of type II pneumocytes by laser flow cytometry: Technical considerations
    • Lung Cell. Mol. Physiol. 5
    • Uhal, B. D., and D. E. Rannels. DNA distribution analysis of type II pneumocytes by laser flow cytometry: technical considerations. Am. J. Physiol. 261 (Lung Cell. Mol. Physiol. 5): L296-L306, 1991.
    • (1991) Am. J. Physiol. , vol.261
    • Uhal, B.D.1    Rannels, D.E.2
  • 450
    • 0019790414 scopus 로고
    • Structural features of alveolar wall basement membrane in the adult rat lung
    • Vaccaro, C. A., and J. S. Brody. Structural features of alveolar wall basement membrane in the adult rat lung. J. Cell Biol. 91: 427-437, 1981.
    • (1981) J. Cell Biol. , vol.91 , pp. 427-437
    • Vaccaro, C.A.1    Brody, J.S.2
  • 451
    • 0025792023 scopus 로고
    • Collagen family of proteins
    • Van der Rest, M., and R. Garrone. Collagen family of proteins. FASEB J. 5: 2814-2823, 1991.
    • (1991) FASEB J. , vol.5 , pp. 2814-2823
    • Van Der Rest, M.1    Garrone, R.2
  • 453
    • 0021259032 scopus 로고
    • Staining of proteoglycans in mouse lung alveoli. II. Characterization of the cuprolinic bluepositive anionic sites
    • Van Kuppevelt, T. H. S. M., F. P. M. Cremers, J. G. W. Domen, and C. M. A. Kuyper. Staining of proteoglycans in mouse lung alveoli. II. Characterization of the cuprolinic bluepositive anionic sites. Histochem. J. 16: 671-686, 1984.
    • (1984) Histochem. J. , vol.16 , pp. 671-686
    • Van Kuppevelt, T.H.S.M.1    Cremers, F.P.M.2    Domen, J.G.W.3    Kuyper, C.M.A.4
  • 454
    • 0021255618 scopus 로고
    • Staining of proteoglycans in mouse lung alveoli. I. Ultrastructural localization of anionic sites
    • Van Kuppevelt, T. H. S. M., F. P. M. Cremers, and C. M. A. Kuyper. Staining of proteoglycans in mouse lung alveoli. I. Ultrastructural localization of anionic sites. Histochem. J. 16: 657-669, 1984.
    • (1984) Histochem. J. , vol.16 , pp. 657-669
    • Van Kuppevelt, T.H.S.M.1    Cremers, F.P.M.2    Kuyper, C.M.A.3
  • 456
    • 0024215608 scopus 로고
    • Specific binding of basic fibroblast growth factor to basement membrane-like structures and to purified heparan sulfate proteoglycans of the EHS tumor
    • Vigny, M., M. P. Ollier-Hartmann, M. Lavigne, N. Fayein, J. C. Jeanny, M. Laurent, and Y. Courtois. Specific binding of basic fibroblast growth factor to basement membrane-like structures and to purified heparan sulfate proteoglycans of the EHS tumor. J. Cell. Physiol. 137: 321-328, 1988.
    • (1988) J. Cell. Physiol. , vol.137 , pp. 321-328
    • Vigny, M.1    Ollier-Hartmann, M.P.2    Lavigne, M.3    Fayein, N.4    Jeanny, J.C.5    Laurent, M.6    Courtois, Y.7
  • 458
    • 0019770337 scopus 로고
    • Extracellular, surface, and intracellular proteoglycans produced by human embryo lung fibroblasts in culture (IMR-90)
    • Vogel, K. G., and D. W. Peterson. Extracellular, surface, and intracellular proteoglycans produced by human embryo lung fibroblasts in culture (IMR-90). J. Biol Chem. 256: 13235-13242, 1981.
    • (1981) J. Biol Chem. , vol.256 , pp. 13235-13242
    • Vogel, K.G.1    Peterson, D.W.2
  • 459
    • 0021715115 scopus 로고
    • Specific inhibition of type I and type II collagen fibrillogenesis by the small proteoglycan of tendon
    • Vogel, K. G., M. Paulsson, and D. Heinegard. Specific inhibition of type I and type II collagen fibrillogenesis by the small proteoglycan of tendon. Biochem. J. 223: 587-597, 1984.
    • (1984) Biochem. J. , vol.223 , pp. 587-597
    • Vogel, K.G.1    Paulsson, M.2    Heinegard, D.3
  • 460
    • 0023355097 scopus 로고
    • The effect of proteoglycans on the morphology of collagen fibrils formed in vitro
    • Vogel, K. G., and J. A. Trotter. The effect of proteoglycans on the morphology of collagen fibrils formed in vitro. Collagen Rel. Res. 7: 105-114, 1987.
    • (1987) Collagen Rel. Res. , vol.7 , pp. 105-114
    • Vogel, K.G.1    Trotter, J.A.2
  • 461
    • 0021164529 scopus 로고
    • Binding and degradation of proteoglycans by cultured arterial smooth muscle cells. I. Endocytosis and intracellular translocation of proteoglycan-gold conjugates
    • Volker, W., A. Schmidt, H. Robenek, and E. Buddecke. Binding and degradation of proteoglycans by cultured arterial smooth muscle cells. I. Endocytosis and intracellular translocation of proteoglycan-gold conjugates. Eur. J. Cell Biol. 34: 110-117, 1984.
    • (1984) Eur. J. Cell Biol. , vol.34 , pp. 110-117
    • Volker, W.1    Schmidt, A.2    Robenek, H.3    Buddecke, E.4
  • 463
  • 464
    • 0027172919 scopus 로고
    • Mechariotransduction across the cell surface and through the cytoskeleton
    • Wang, N., J. P. Butler, and D. E. Ingber. Mechariotransduction across the cell surface and through the cytoskeleton. Science Wash. DC 260: 1124-1127, 1993.
    • (1993) Science Wash. DC , vol.260 , pp. 1124-1127
    • Wang, N.1    Butler, J.P.2    Ingber, D.E.3
  • 466
    • 0026651513 scopus 로고
    • Processing of surfactant protein B proprotein by a cathepsin D-like protease
    • Lung Cell. Mol. Physiol. 7
    • Weaver, T. E., S. Lin, B. Bogucki, and C. Dey. Processing of surfactant protein B proprotein by a cathepsin D-like protease. Am. J. Physiol. 263 (Lung Cell. Mol. Physiol. 7): L95-L103, 1992.
    • (1992) Am. J. Physiol. , vol.263
    • Weaver, T.E.1    Lin, S.2    Bogucki, B.3    Dey, C.4
  • 467
    • 0000352274 scopus 로고
    • Structural organization of the pulmonary interstitium
    • edited by R. G. Crystal and J. B. West. New York: Raven
    • Weibel, E. R., and R. G. Crystal. Structural organization of the pulmonary interstitium. In: The Lung, edited by R. G. Crystal and J. B. West. New York: Raven, 1991, p. 369-380.
    • (1991) The Lung , pp. 369-380
    • Weibel, E.R.1    Crystal, R.G.2
  • 469
    • 0022447670 scopus 로고
    • Isolation of pulmonary alveolar type I cells from adult rats
    • Weller, N. K., and M. J. Karnovsky. Isolation of pulmonary alveolar type I cells from adult rats. Am. J. Pathol. 124: 448-456, 1986.
    • (1986) Am. J. Pathol. , vol.124 , pp. 448-456
    • Weller, N.K.1    Karnovsky, M.J.2
  • 470
    • 0002669303 scopus 로고
    • Proteinases and matrix degradation
    • edited by W. N. Kelley, E. D. Harris, Jr., S. Ruddy, and C. B. Sledge. Philadelphia, PA: Saunders
    • Werb, Z. Proteinases and matrix degradation. In: Textbook of Rheumatology, edited by W. N. Kelley, E. D. Harris, Jr., S. Ruddy, and C. B. Sledge. Philadelphia, PA: Saunders, 1989, p. 300-321.
    • (1989) Textbook of Rheumatology , pp. 300-321
    • Werb, Z.1
  • 472
    • 0026940259 scopus 로고
    • The role of proteoglycans in cell adhesion, migration, and proliferation
    • Wight, T. N., M. G. Kinsella, and E. E. Qwarnstrom. The role of proteoglycans in cell adhesion, migration, and proliferation. Curr. Opin. Cell Biol. 4: 793-801, 1992.
    • (1992) Curr. Opin. Cell Biol. , vol.4 , pp. 793-801
    • Wight, T.N.1    Kinsella, M.G.2    Qwarnstrom, E.E.3
  • 473
    • 0024330327 scopus 로고
    • SV40-transformed human lung fibroblasts secrete a 92-kDa type IV collagenase which is identical to that secreted by normal human macrophages
    • Wilhelm, S. M., I. E. Collier, B. L. Marmer, A. Z. Eisen, G.A. Grant, and G. I. Goldberg. SV40-transformed human lung fibroblasts secrete a 92-kDa type IV collagenase which is identical to that secreted by normal human macrophages. J. Biol. Chem. 264: 17213-17221, 1989.
    • (1989) J. Biol. Chem. , vol.264 , pp. 17213-17221
    • Wilhelm, S.M.1    Collier, I.E.2    Marmer, B.L.3    Eisen, A.Z.4    Grant, G.A.5    Goldberg, G.I.6
  • 474
    • 0025439383 scopus 로고
    • Expression of cell-specific markers for alveolar epithelium in fetal rat lung
    • Williams, M. C., and L. G. Dobbs. Expression of cell-specific markers for alveolar epithelium in fetal rat lung. Am. J. Respir. Cell Mol. Biol. 2: 533-542, 1990.
    • (1990) Am. J. Respir. Cell Mol. Biol. , vol.2 , pp. 533-542
    • Williams, M.C.1    Dobbs, L.G.2
  • 478
    • 0026094282 scopus 로고
    • Potential role of entactin in hemostasis. Specific interaction of entactin with fibrinogen Aα and Bβ chains
    • Wu, C., and A. E. Chung. Potential role of entactin in hemostasis. Specific interaction of entactin with fibrinogen Aα and Bβ chains. J. Biol. Chem. 266: 18802-18807, 1991.
    • (1991) J. Biol. Chem. , vol.266 , pp. 18802-18807
    • Wu, C.1    Chung, A.E.2
  • 479
    • 0023768277 scopus 로고
    • Differentiating human leukemia cells express heparanase that degrades heparan sulfate in subendothelial extracellular matrix
    • Yahalom, J., E. Fibach, R. Bar-Tana, Z. Fuks, and I. Vlodavsky. Differentiating human leukemia cells express heparanase that degrades heparan sulfate in subendothelial extracellular matrix. Leuk. Res. 12: 711-717, 1988.
    • (1988) Leuk. Res. , vol.12 , pp. 711-717
    • Yahalom, J.1    Fibach, E.2    Bar-Tana, R.3    Fuks, Z.4    Vlodavsky, I.5
  • 480
    • 0018438010 scopus 로고
    • Fibroblast cellular and plasma fibronectins are similar but not identical
    • Yamada, K. M., and D. W. Kennedy. Fibroblast cellular and plasma fibronectins are similar but not identical. J. Cell Biol. 80: 492-498, 1979.
    • (1979) J. Cell Biol. , vol.80 , pp. 492-498
    • Yamada, K.M.1    Kennedy, D.W.2
  • 481
    • 0025353729 scopus 로고
    • Negative regulation of transforming growth factor β by the proteoglycan decorin
    • Yamaguchi, Y., D. M. Mann, and E. Ruoslahti. Negative regulation of transforming growth factor β by the proteoglycan decorin. Nature Lond. 346: 281-284, 1990.
    • (1990) Nature Lond. , vol.346 , pp. 281-284
    • Yamaguchi, Y.1    Mann, D.M.2    Ruoslahti, E.3
  • 482
    • 0027267162 scopus 로고
    • Functions of proteoglycans in the extracellular matrix
    • Yanagishita, M. Functions of proteoglycans in the extracellular matrix. Acta Pathol. Jpn. 43: 283-293, 1993.
    • (1993) Acta Pathol. Jpn. , vol.43 , pp. 283-293
    • Yanagishita, M.1
  • 486
    • 0027508012 scopus 로고
    • Imrmmohistochemical detection of hepatocyte growth/scatter factor in human cancerous and inflammatory lesions of various organs
    • Yoshinaga, Y., Y. Matsuno, S. Fujita, T. Nakamura, M. Kikuchi, Y. Shimosato, and S. Hirohashi. Imrmmohistochemical detection of hepatocyte growth/scatter factor in human cancerous and inflammatory lesions of various organs. Jpn. J. Cancer Res. 84: 1150-1158, 1993.
    • (1993) Jpn. J. Cancer Res. , vol.84 , pp. 1150-1158
    • Yoshinaga, Y.1    Matsuno, Y.2    Fujita, S.3    Nakamura, T.4    Kikuchi, M.5    Shimosato, Y.6    Hirohashi, S.7
  • 487
    • 0028329091 scopus 로고
    • Tenascin-C in rat lung: Distribution, ontogeny and role in branching morphogenesis
    • Young, S. L., L.-Y. Chang, and H. P. Erickson. Tenascin-C in rat lung: distribution, ontogeny and role in branching morphogenesis. Dev. Biol. 161: 615-625, 1994.
    • (1994) Dev. Biol. , vol.161 , pp. 615-625
    • Young, S.L.1    Chang, L.-Y.2    Erickson, H.P.3
  • 488
    • 0027313437 scopus 로고
    • Self-assembly and calcium-binding sites in laminin: A three-arm interaction model
    • Yurchenco, P. D., and Y. S. Cheng. Self-assembly and calcium-binding sites in laminin: a three-arm interaction model. J. Biol. Chem. 268: 17286-17299, 1993.
    • (1993) J. Biol. Chem. , vol.268 , pp. 17286-17299
    • Yurchenco, P.D.1    Cheng, Y.S.2
  • 489
    • 0023630089 scopus 로고
    • Self-assembly of a high molecular weight basement membrane heparan sulfate proteoglycan into dimers and oligomers
    • Yurchenco, P. D., Y.-S. Cheng, and G. C. Ruben. Self-assembly of a high molecular weight basement membrane heparan sulfate proteoglycan into dimers and oligomers. J. Biol. Chem. 262: 17668-17676, 1987.
    • (1987) J. Biol. Chem. , vol.262 , pp. 17668-17676
    • Yurchenco, P.D.1    Cheng, Y.-S.2    Ruben, G.C.3
  • 490
    • 0023600043 scopus 로고
    • Basement membrane structure in situ: Evidence for lateral associations in the type IV collagen network
    • Yurchenco, P. D., and G. C. Ruben. Basement membrane structure in situ: evidence for lateral associations in the type IV collagen network. J. Cell Biol. 105: 2559-2568, 1987.
    • (1987) J. Cell Biol. , vol.105 , pp. 2559-2568
    • Yurchenco, P.D.1    Ruben, G.C.2
  • 491
    • 0025363827 scopus 로고
    • Molecular architecture of basement membranes
    • Yurchenco, P. D., and J. G. Schittny. Molecular architecture of basement membranes. FASEB J. 4: 1577-1590, 1990.
    • (1990) FASEB J. , vol.4 , pp. 1577-1590
    • Yurchenco, P.D.1    Schittny, J.G.2
  • 493
    • 0021991889 scopus 로고
    • Basement membrane formation and lung cell differentiation in vitro
    • Zimmermann, B., H. J. Barrach, H. J. Merker, and N. Hinz. Basement membrane formation and lung cell differentiation in vitro. Eur. J. Cell Biol. 36: 66-73, 1985.
    • (1985) Eur. J. Cell Biol. , vol.36 , pp. 66-73
    • Zimmermann, B.1    Barrach, H.J.2    Merker, H.J.3    Hinz, N.4


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