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Volumn 136, Issue 5, 1997, Pages 1151-1163

Latent transforming growth factor-β binding protein domains involved in activation and transglutaminase-dependent cross-linking of latent transforming growth factor-β

Author keywords

[No Author keywords available]

Indexed keywords

ANTIBODY; ANTISERUM; BINDING PROTEIN; CELL SURFACE RECEPTOR; ENZYME INHIBITOR; GLUTATHIONE TRANSFERASE; HYBRID PROTEIN; PLASMINOGEN ACTIVATOR INHIBITOR 1; PROTEIN GLUTAMINE GAMMA GLUTAMYLTRANSFERASE; TRANSFORMING GROWTH FACTOR BETA;

EID: 0030974902     PISSN: 00219525     EISSN: None     Source Type: Journal    
DOI: 10.1083/jcb.136.5.1151     Document Type: Article
Times cited : (354)

References (66)
  • 1
    • 0028328817 scopus 로고
    • An assay for transforming growth factor-β using cells transfected with a plasminogen activator inhibilor-1 promoter luciferase construct
    • Abe, M., J.G. Harpel, C.N. Metz, I. Nunes, D.J. Loskutoff, and D.B. Rifkin. 1994. An assay for transforming growth factor-β using cells transfected with a plasminogen activator inhibilor-1 promoter luciferase construct. Anal. Biochem. 216:276-284.
    • (1994) Anal. Biochem. , vol.216 , pp. 276-284
    • Abe, M.1    Harpel, J.G.2    Metz, C.N.3    Nunes, I.4    Loskutoff, D.J.5    Rifkin, D.B.6
  • 2
    • 0021564388 scopus 로고
    • The cell biology of macrophage activation
    • Adams, D., and T.A. Hamilton. 1984. The cell biology of macrophage activation. Annu. Rev. Itnmunol 2:283-338.
    • (1984) Annu. Rev. Itnmunol , vol.2 , pp. 283-338
    • Adams, D.1    Hamilton, T.A.2
  • 3
    • 0025823541 scopus 로고
    • Cross-linking of laminin-nidogen complexes by tissue transglutaminase
    • Aeschlimann, D., and M. Paulsson. 1991. Cross-linking of laminin-nidogen complexes by tissue transglutaminase. J. Biol. Chem. 266:15308-15317.
    • (1991) J. Biol. Chem. , vol.266 , pp. 15308-15317
    • Aeschlimann, D.1    Paulsson, M.2
  • 4
    • 0026612802 scopus 로고
    • Identification of gln726 in nidogen as the amine accepior in transglutaminase-catalyzed cross-linking of laminin-nidogen complexes
    • Aeschlimann, D., M. Paulsson, and K. Mann. 1992. Identification of gln726 in nidogen as the amine accepior in transglutaminase-catalyzed cross-linking of laminin-nidogen complexes. J. Biol. Chem. 267:11316-11321.
    • (1992) J. Biol. Chem. , vol.267 , pp. 11316-11321
    • Aeschlimann, D.1    Paulsson, M.2    Mann, K.3
  • 5
    • 0028177037 scopus 로고
    • Transforming growth factor-β activation in irradiated murine mammary gland
    • Barcellos-Hoff, M.H., R. Derynck, M.L. Tsang, and J.A. Weatherbee. 1994. Transforming growth factor-β activation in irradiated murine mammary gland. J. Clin. Invest. 93:892-899.
    • (1994) J. Clin. Invest. , vol.93 , pp. 892-899
    • Barcellos-Hoff, M.H.1    Derynck, R.2    Tsang, M.L.3    Weatherbee, J.A.4
  • 6
    • 0027375114 scopus 로고
    • Transglutaminases catalyze cross-linking of plasminogen to fibronectin and human endothelial cells
    • Bendixen, E., B. Wolfgang, and P.C. Harpel. 1993. Transglutaminases catalyze cross-linking of plasminogen to fibronectin and human endothelial cells. J. Biol. Chem. 268:21962-21967.
    • (1993) J. Biol. Chem. , vol.268 , pp. 21962-21967
    • Bendixen, E.1    Wolfgang, B.2    Harpel, P.C.3
  • 7
    • 0025005006 scopus 로고
    • Expression, purification, and characterization of human factor XIII in Saccharomyces cerevisiae
    • Bishop, P.D., D.C Teller, R.A. Smith, G.W. Lasser, T. Gilbert, and R.L. Scale. 1990. Expression, purification, and characterization of human factor XIII in Saccharomyces cerevisiae. Biochemistry. 29:1861-1869.
    • (1990) Biochemistry. , vol.29 , pp. 1861-1869
    • Bishop, P.D.1    Teller, D.C.2    Smith, R.A.3    Lasser, G.W.4    Gilbert, T.5    Scale, R.L.6
  • 8
    • 0026052923 scopus 로고
    • Lipoprotein(a) is a substrate for factor XIIIa and tissue transglutaminase
    • Borth, W., V.T. Chang, P. Bishop, and P.C. Harpel. 1991. Lipoprotein(a) is a substrate for factor XIIIa and tissue transglutaminase. J. Biol. Chem. 266:18149-18153.
    • (1991) J. Biol. Chem. , vol.266 , pp. 18149-18153
    • Borth, W.1    Chang, V.T.2    Bishop, P.3    Harpel, P.C.4
  • 9
    • 0024994691 scopus 로고
    • Physicochemical activation of recombinant latent transforming growth factor-beta's 1.2.3
    • Brown, P., L. Wakefield, A. Levinson, and M. Sporn. 1990. Physicochemical activation of recombinant latent transforming growth factor-beta's 1.2.3. Growth Factors. 3:35-43.
    • (1990) Growth Factors. , vol.3 , pp. 35-43
    • Brown, P.1    Wakefield, L.2    Levinson, A.3    Sporn, M.4
  • 11
    • 0021322350 scopus 로고
    • The inhibition of glucose-stimulated insulin secretion by primary amines
    • Bungay, P.J., J.M. Potter, and M. Griffin. 1984. The inhibition of glucose-stimulated insulin secretion by primary amines. Biochem. J. 219:819-827.
    • (1984) Biochem. J. , vol.219 , pp. 819-827
    • Bungay, P.J.1    Potter, J.M.2    Griffin, M.3
  • 12
    • 0028302076 scopus 로고
    • Characterization and autoregulation of latent transforming growth factor β(TGF-β) complexes in osteoblast-like cell lines
    • Dallas, S., S. Park-Snyder, K. Miyazono, D. Twardzik, G.R. Mundy, and L.F. Bonewald. 1994. Characterization and autoregulation of latent transforming growth factor β(TGF-β) complexes in osteoblast-like cell lines. J. Biol. Chem. 269:6815-6822.
    • (1994) J. Biol. Chem. , vol.269 , pp. 6815-6822
    • Dallas, S.1    Park-Snyder, S.2    Miyazono, K.3    Twardzik, D.4    Mundy, G.R.5    Bonewald, L.F.6
  • 13
    • 0028885716 scopus 로고
    • Dual role for the latent transforming growth factor-β binding protein in storage of latent TGF-β in the extracellular matrix and as a structural matrix protein
    • Dallas, S.L., K. Miyazono, T.M. Skerry, G.R. Mundy, and L.F. Bonewald. 1995. Dual role for the latent transforming growth factor-β binding protein in storage of latent TGF-β in the extracellular matrix and as a structural matrix protein. J. Cell Biol. 131:539-549.
    • (1995) J. Cell Biol. , vol.131 , pp. 539-549
    • Dallas, S.L.1    Miyazono, K.2    Skerry, T.M.3    Mundy, G.R.4    Bonewald, L.F.5
  • 14
    • 0027122245 scopus 로고
    • Crystal structure of transforming growth factor-β2: An unusual fold for the superfamily
    • Daopin, S., K.A. Piez, Y. Ogawa, and D.R. Davies. 1992. Crystal structure of transforming growth factor-β2: an unusual fold for the superfamily. Science (Wash. DC). 257:369-373.
    • (1992) Science (Wash. DC). , vol.257 , pp. 369-373
    • Daopin, S.1    Piez, K.A.2    Ogawa, Y.3    Davies, D.R.4
  • 15
    • 0024553650 scopus 로고
    • Monoclonal antibodies recognizing transforming growth factor-beta. Bioactivity neutralization and transforming growth factor beta2 affinity purification
    • Dasch, J.R., D.R. Pace, W. Waegell, D. Inenaga, and L. Ellingsworth. 1989. Monoclonal antibodies recognizing transforming growth factor-beta. Bioactivity neutralization and transforming growth factor beta2 affinity purification. J. Immunol. 142:1536-1541.
    • (1989) J. Immunol , vol.142 , pp. 1536-1541
    • Dasch, J.R.1    Pace, D.R.2    Waegell, W.3    Inenaga, D.4    Ellingsworth, L.5
  • 16
    • 0026059613 scopus 로고
    • Cellular activation of latent transforming growth factor β requires binding to the cation-independent mannose 6-phosphate/insulin-like growth factor type II receptor
    • Dennis, P.A., and D.B. Rifkin. 1991. Cellular activation of latent transforming growth factor β requires binding to the cation-independent mannose 6-phosphate/insulin-like growth factor type II receptor. Proc. Natl. Acad. Sci. USA. 88:580-584.
    • (1991) Proc. Natl. Acad. Sci. USA. , vol.88 , pp. 580-584
    • Dennis, P.A.1    Rifkin, D.B.2
  • 18
    • 0026768120 scopus 로고
    • Basic fibroblast growth factor-induced activation of latent transforming growth factor beta in endothelial cells: Regulation of plasminogen activator activity
    • Flaumcnhaft, R., M. Abe, P. Mignatti, and D.B. Rifkin. 1992. Basic fibroblast growth factor-induced activation of latent transforming growth factor beta in endothelial cells: regulation of plasminogen activator activity. J. Cell Biol. 118:901-909.
    • (1992) J. Cell Biol. , vol.118 , pp. 901-909
    • Flaumcnhaft, R.1    Abe, M.2    Mignatti, P.3    Rifkin, D.B.4
  • 19
    • 0027476156 scopus 로고
    • Role of the latent TGF-β binding protein in the activation of latent TGF-β by co-cultures of endothelial and smooth muscle cells
    • Flaumcnhaft, R., M. Abe, Y. Sato, K. Miyazono, J. Harpel, C. Heldin, and D.B. Rifkin. 1993. Role of the latent TGF-β binding protein in the activation of latent TGF-β by co-cultures of endothelial and smooth muscle cells. J. Cell Biol. 120:995-1002.
    • (1993) J. Cell Biol. , vol.120 , pp. 995-1002
    • Flaumcnhaft, R.1    Abe, M.2    Sato, Y.3    Miyazono, K.4    Harpel, J.5    Heldin, C.6    Rifkin, D.B.7
  • 20
  • 21
    • 0023732890 scopus 로고
    • Molecular events in the processing of recombinant type I pre-pro-transforming growth factor beta to the mature polypeptide
    • Gentry, L.E., M.N. Lioubin, A.F. Purchio, and H. Marquardt. 1988. Molecular events in the processing of recombinant type I pre-pro-transforming growth factor beta to the mature polypeptide. Mol. Cell. Biol. 8:4162-4168.
    • (1988) Mol. Cell. Biol. , vol.8 , pp. 4162-4168
    • Gentry, L.E.1    Lioubin, M.N.2    Purchio, A.F.3    Marquardt, H.4
  • 22
    • 0028857166 scopus 로고
    • Bovine latent transforming growth factor-β1-binding protein 2: Molecular cloning, identification of tissue isoforms. and immunolocalization to elastin-associated microfibrils
    • Gibson, M.A., G. Hatzinikolas, E.C. Davis, E. Baker, G.R. Sutherland, and R. Mecham. 1995. Bovine latent transforming growth factor-β1-binding protein 2: molecular cloning, identification of tissue isoforms. and immunolocalization to elastin-associated microfibrils. Mol. Cell. Biol. 15:6932-6942.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 6932-6942
    • Gibson, M.A.1    Hatzinikolas, G.2    Davis, E.C.3    Baker, E.4    Sutherland, G.R.5    Mecham, R.6
  • 23
    • 0029860747 scopus 로고    scopus 로고
    • Identification and characterization of an eight-cysteine repeat of the latent transforming growth factor-β binding protein-1 that mediates bonding to the latent transforming growth factor-β
    • 22a. Gleizes, P.-E., R.C. Beauis, R. Mazzieri, B. Shen, and D.B Rifkin. 1996. Identification and characterization of an eight-cysteine repeat of the latent transforming growth factor-β binding protein-1 that mediates bonding to the latent transforming growth factor-β. J. Biol. Chem. 271:29891-29896.
    • (1996) J. Biol. Chem. , vol.271 , pp. 29891-29896
    • Gleizes, P.-E.1    Beauis, R.C.2    Mazzieri, R.3    Shen, B.4    Rifkin, D.B.5
  • 24
    • 0029029807 scopus 로고
    • Release and activation of platelet latent TGF-β in blood clots during dissolution with plasmin
    • Grainger, D.J., L. Wakefield, H.W. Bethell, R.W. Farndale, and J.C. Metcalfc. 1995. Release and activation of platelet latent TGF-β in blood clots during dissolution with plasmin. Nat. Med. 1:932-937.
    • (1995) Nat. Med. , vol.1 , pp. 932-937
    • Grainger, D.J.1    Wakefield, L.2    Bethell, H.W.3    Farndale, R.W.4    Metcalfc, J.C.5
  • 26
    • 0029147474 scopus 로고
    • Substrate requirements for transglutaminases
    • Grootjans, J.J., T.A. Groenen, and W.W. de Jong. 1995. Substrate requirements for transglutaminases. J. Biol. Chem. 270:22855-22858.
    • (1995) J. Biol. Chem. , vol.270 , pp. 22855-22858
    • Grootjans, J.J.1    Groenen, T.A.2    De Jong, W.W.3
  • 27
    • 0003448569 scopus 로고
    • Cold Spring Harbor Laboratory Press. Cold Spring Harbor, NY.
    • Harlow, E., and D. Lane. 1988. Antibodies: A Laboratory Manual. Cold Spring Harbor Laboratory Press. Cold Spring Harbor, NY. 678-679.
    • (1988) Antibodies: a Laboratory Manual , pp. 678-679
    • Harlow, E.1    Lane, D.2
  • 28
    • 0027017351 scopus 로고
    • Control of transforming growth factor-β activity: Latency vs. activation
    • Harpel, J.G., C.N. Metz, S. Kojima, and D.B. Rifkin. 1993. Control of transforming growth factor-β activity: latency vs. activation. Prog. Growth Factor Res. 4:321-335.
    • (1993) Prog. Growth Factor Res. , vol.4 , pp. 321-335
    • Harpel, J.G.1    Metz, C.N.2    Kojima, S.3    Rifkin, D.B.4
  • 30
    • 0028925277 scopus 로고
    • Cysteine-to-arginine point mutation in a "hybrid" eight-cysteine domain of FBN1: Consequences for fibrillin aggregation and microfibril assembly
    • Kielty, C.M., T. Rantamaki, A.H. Child, C.A. Shuttleworth, and L. Peltonen. 1995. Cysteine-to-arginine point mutation in a "hybrid" eight-cysteine domain of FBN1: consequences for fibrillin aggregation and microfibril assembly. J. Cell Sci. 108:1317-1323.
    • (1995) J. Cell Sci. , vol.108 , pp. 1317-1323
    • Kielty, C.M.1    Rantamaki, T.2    Child, A.H.3    Shuttleworth, C.A.4    Peltonen, L.5
  • 31
    • 0027298030 scopus 로고
    • Mechanism of retinoid-induced activation of latent transforming growth factor-β in bovine endothelial cells
    • Kojima, S., and D.B. Rifkin. 1993. Mechanism of retinoid-induced activation of latent transforming growth factor-β in bovine endothelial cells. J. Cell. Physiol. 155:323-332.
    • (1993) J. Cell. Physiol. , vol.155 , pp. 323-332
    • Kojima, S.1    Rifkin, D.B.2
  • 32
    • 0027419881 scopus 로고
    • Requirement for trans-glutaminase in the activation of latent transforming growth factor-β in bovine endothelial cells
    • Kojima, S., N. Kiyomitsu, and D.B. Rifkin. 1993. Requirement for trans-glutaminase in the activation of latent transforming growth factor-β in bovine endothelial cells. J. Cell Biol. 121:439-148.
    • (1993) J. Cell Biol. , vol.121 , pp. 439-1148
    • Kojima, S.1    Kiyomitsu, N.2    Rifkin, D.B.3
  • 33
    • 0024592869 scopus 로고
    • Interactions of recombinant and platelet transforming growth factor-β1 precursor with the insulin-like growth factor II/mannose 6-phosphate receptor
    • Kovacina, K.S., G. Steele-Perkins, A.F. Purchio, M. Lioubin, K. Miyazono, C. Heldin, and R. Roth. 1989. Interactions of recombinant and platelet transforming growth factor-β1 precursor with the insulin-like growth factor II/mannose 6-phosphate receptor. Biochem. Biophys. Res. Commun. 160:393-403.
    • (1989) Biochem. Biophys. Res. Commun. , vol.160 , pp. 393-403
    • Kovacina, K.S.1    Steele-Perkins, G.2    Purchio, A.F.3    Lioubin, M.4    Miyazono, K.5    Heldin, C.6    Roth, R.7
  • 35
    • 0025098903 scopus 로고
    • Transforming growth factor-β and the regulation of cell proliferation
    • Lyons, R.M., and H.L. Moses. 1990. Transforming growth factor-β and the regulation of cell proliferation. Eur. J. Biochem. 187:467-473.
    • (1990) Eur. J. Biochem. , vol.187 , pp. 467-473
    • Lyons, R.M.1    Moses, H.L.2
  • 36
    • 0023916551 scopus 로고
    • Proteolytic activation of latent transforming growth factor-β from fibroblast-conditioned medium
    • Lyons, R.M., J. Keski-Oja, and H.L. Moses. 1988. Proteolytic activation of latent transforming growth factor-β from fibroblast-conditioned medium. J. Cell Biol. 106:1659-1665.
    • (1988) J. Cell Biol. , vol.106 , pp. 1659-1665
    • Lyons, R.M.1    Keski-Oja, J.2    Moses, H.L.3
  • 37
    • 0025215307 scopus 로고
    • Mechanism of activation of latent recombinant transforming growth factor β1 by plasmin
    • Lyons, R.M., L.E. Gentry, A.F. Purchio, and H.L. Moses. 1990. Mechanism of activation of latent recombinant transforming growth factor β1 by plasmin. J. Cell Biol. 110:1361-1367.
    • (1990) J. Cell Biol. , vol.110 , pp. 1361-1367
    • Lyons, R.M.1    Gentry, L.E.2    Purchio, A.F.3    Moses, H.L.4
  • 38
    • 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. 1994. Transglutaminase-mediated processing of fibronectin by endothelial cell monolayers. Biochemistry. 33:2538-2545.
    • (1994) Biochemistry. , vol.33 , pp. 2538-2545
    • Martinez, J.1    Chalupowicz, D.G.2    Roush, R.K.3    Sheth, A.4    Barsigian, C.5
  • 39
    • 0025222517 scopus 로고
    • The transforming growth factor-β family
    • Massague, J. 1990. The transforming growth factor-β family. Annu. Rev. Cell Biol. 6:597-641.
    • (1990) Annu. Rev. Cell Biol. , vol.6 , pp. 597-641
    • Massague, J.1
  • 40
    • 0018822124 scopus 로고
    • Radioiodination of proteins by the use of the chloramine-T method
    • McConahey, P.J., and F.J. Dixon. 1980. Radioiodination of proteins by the use of the chloramine-T method. Methods Enzymol. 70:210-213.
    • (1980) Methods Enzymol. , vol.70 , pp. 210-213
    • McConahey, P.J.1    Dixon, F.J.2
  • 41
    • 0023940794 scopus 로고
    • Latent high molecular weight complex of transforming growth factor β1
    • Miyazono, K., U. Hellman, C. Wernstedt, and C. Heldin. 1988. Latent high molecular weight complex of transforming growth factor β1. J. Biol. Chem. 263:6407-6415.
    • (1988) J. Biol. Chem. , vol.263 , pp. 6407-6415
    • Miyazono, K.1    Hellman, U.2    Wernstedt, C.3    Heldin, C.4
  • 42
    • 0025765844 scopus 로고
    • A role of the latent TGF-β1 hinding protein in the assembly and secretion of TGF-β1 EMBO 1
    • Miyazono, K., A. Olofsson, P. Colosetti, and C. Heldin. 1991. A role of the latent TGF-β1 hinding protein in the assembly and secretion of TGF-β1 EMBO 1 Eur. Mol. Biol. Organ.) J. 10:1091-1101.
    • (1991) Eur. Mol. Biol. Organ. J. , vol.10 , pp. 1091-1101
    • Miyazono, K.1    Olofsson, A.2    Colosetti, P.3    Heldin, C.4
  • 43
    • 0027466618 scopus 로고
    • Transforming growth factor-beta: Latent forms, binding proteins and receptors
    • Miyazono, K., H. Ichijo, and C.H. Heldin. 1993. Transforming growth factor-beta: latent forms, binding proteins and receptors. Growth Factors. 8: 11-22.
    • (1993) Growth Factors. , vol.8 , pp. 11-22
    • Miyazono, K.1    Ichijo, H.2    Heldin, C.H.3
  • 45
    • 0028984569 scopus 로고
    • Characterization of late TGF-β activation by murine peritoneal macrophages
    • Nunes, I., R.L. Shapiro, and D.R. Rifkin. 1995. Characterization of late TGF-β activation by murine peritoneal macrophages. J. Immunol. 155: 1450-1459.
    • (1995) J. Immunol. , vol.155 , pp. 1450-1459
    • Nunes, I.1    Shapiro, R.L.2    Rifkin, D.R.3
  • 46
    • 0024309936 scopus 로고
    • Purification and structural analysis of a latent transforming growth factor-β rat platelets
    • Okada, F., K. Yamaguchi, A. Ichihara, and T. Nakamura. 1989. Purification and structural analysis of a latent transforming growth factor-β rat platelets. J. Biochem. 106:304-310.
    • (1989) J. Biochem. , vol.106 , pp. 304-310
    • Okada, F.1    Yamaguchi, K.2    Ichihara, A.3    Nakamura, T.4
  • 47
    • 0029565595 scopus 로고
    • Efficient association of an amino-terminally extended form of human latent transforming growth factor-β binding protein with the extracellular matrix
    • Olofsson, A., H. Ichijo, A. Moren, P. ten Dijke, K. Miyazono, and C.H. Heldin. 1995. Efficient association of an amino-terminally extended form of human latent transforming growth factor-β binding protein with the extracellular matrix. J. Biol. Chem. 270:31294-31297.
    • (1995) J. Biol. Chem. , vol.270 , pp. 31294-31297
    • Olofsson, A.1    Ichijo, H.2    Moren, A.3    Ten Dijke, P.4    Miyazono, K.5    Heldin, C.H.6
  • 48
    • 0029665565 scopus 로고    scopus 로고
    • Fibrillin mutations in Marfan syndrome and related phenotypes
    • Ramirez, F. 1996. Fibrillin mutations in Marfan syndrome and related phenotypes. Curr. Opin. Genet. Dev. 6:309-315.
    • (1996) Curr. Opin. Genet. Dev. , vol.6 , pp. 309-315
    • Ramirez, F.1
  • 50
    • 0030058699 scopus 로고    scopus 로고
    • Association of the small latent transforming growth factor-β with an eight cysteine repeat of its binding protein LTBP-1
    • Saharinen, J., J. Taipale, and J. Keski-Oja. 1996. Association of the small latent transforming growth factor-β with an eight cysteine repeat of its binding protein LTBP-1. EMBO (Eur. Moi. Biol. Organ.) J. 15:245-253.
    • (1996) EMBO (Eur. Moi. Biol. Organ.) J. , vol.15 , pp. 245-253
    • Saharinen, J.1    Taipale, J.2    Keski-Oja, J.3
  • 51
    • 0026315446 scopus 로고
    • Purification and partial characertization of fibrillin, a cysteine-rich structural component of connective tissue microfibrils
    • Sakai, L.Y., D.R. Keene, R.W. Glanville, and H.P. Bachinger. 1991. Purification and partial characertization of fibrillin, a cysteine-rich structural component of connective tissue microfibrils. J. Biol. Chem. 266:14763-14770.
    • (1991) J. Biol. Chem. , vol.266 , pp. 14763-14770
    • Sakai, L.Y.1    Keene, D.R.2    Glanville, R.W.3    Bachinger, H.P.4
  • 52
    • 0025974048 scopus 로고
    • Vitronectin in the substratum of endothelial cells is cross-linked and phosphorylated
    • Sane, D.C., T.L. Moser, and C.S. Greenberg. 1991. Vitronectin in the substratum of endothelial cells is cross-linked and phosphorylated. Biochem. Biophys. Res. Commun. 174:465-469.
    • (1991) Biochem. Biophys. Res. Commun. , vol.174 , pp. 465-469
    • Sane, D.C.1    Moser, T.L.2    Greenberg, C.S.3
  • 53
    • 0024077722 scopus 로고
    • Autocrine activities of basic finroblast growth factor: Regulation of endothelial cell movement, plasminogen activator synthesis, and DNA synthesis. J
    • Sato, Y., and D.B. Rifkin, 1988. Autocrine activities of basic finroblast growth factor: regulation of endothelial cell movement, plasminogen activator synthesis, and DNA synthesis. J. Cell Biol. 107:1199-1205.
    • (1988) Cell Biol. , vol.107 , pp. 1199-1205
    • Sato, Y.1    Rifkin, D.B.2
  • 54
    • 0024382711 scopus 로고
    • Inhibition of endothelial cell movement by pericytes and smooth muscle cells: Activation of a latent transforming growth factor-β1-like molecule by plasmin during co-culture. J
    • Sato, Y., and D. Rifkin. 1989. Inhibition of endothelial cell movement by pericytes and smooth muscle cells: activation of a latent transforming growth factor-β1-like molecule by plasmin during co-culture. J. Cell Biol. 109:309-315.
    • (1989) Cell Biol. , vol.109 , pp. 309-315
    • Sato, Y.1    Rifkin, D.2
  • 55
    • 0025310993 scopus 로고
    • Characterization of the activation of latent TGF-β by co-cultures of endothelial cells and pericytes or smooth muscle cells: A self-regulating system
    • Sato, Y., R. Tsuboi, R. Lyons, H. Moses, and D.B. Rifkin. 1990. Characterization of the activation of latent TGF-β by co-cultures of endothelial cells and pericytes or smooth muscle cells: a self-regulating system. J. Cell Biol. 111:757-763.
    • (1990) J. Cell Biol. , vol.111 , pp. 757-763
    • Sato, Y.1    Tsuboi, R.2    Lyons, R.3    Moses, H.4    Rifkin, D.B.5
  • 56
    • 0027427964 scopus 로고
    • The mechanism for the activation of latent TGF-β during co-culture of endothelial cells and smooth muscle cells cell-type specific targeting of latent TGF-β to smooth muscle cells
    • Sato, Y., F. Okada, M. Abe, T. Seguchi, M. Kuwano, S. Sato, A. Furuya, N. Hanai, and T. Tamaoki. 1993. The mechanism for the activation of latent TGF-β during co-culture of endothelial cells and smooth muscle cells cell-type specific targeting of latent TGF-β to smooth muscle cells. J. Cell Biol. 123:1249-1254.
    • (1993) J. Cell Biol. , vol.123 , pp. 1249-1254
    • Sato, Y.1    Okada, F.2    Abe, M.3    Seguchi, T.4    Kuwano, M.5    Sato, S.6    Furuya, A.7    Hanai, N.8    Tamaoki, T.9
  • 57
    • 0027967771 scopus 로고
    • Thrombospondin binds and activates the small and large forms of latent transforming growth factor-β in a chemically defined system
    • Schultz-Cherry, S., S. Ribeiro, L. Gentry, and J.E. Murphy-Ullrich. 1994. Thrombospondin binds and activates the small and large forms of latent transforming growth factor-β in a chemically defined system. J. Biol. Chem. 269:26775-26782.
    • (1994) J. Biol. Chem. , vol.269 , pp. 26775-26782
    • Schultz-Cherry, S.1    Ribeiro, S.2    Gentry, L.3    Murphy-Ullrich, J.E.4
  • 58
    • 0023806075 scopus 로고
    • Single-step purification of polypeptides expressed in Escherichia coli as fusions with glutathione S-transferase
    • Smith, D.B., and K.S. Johnson. 1988. Single-step purification of polypeptides expressed in Escherichia coli as fusions with glutathione S-transferase. Gene. 67:31-40.
    • (1988) Gene. , vol.67 , pp. 31-40
    • Smith, D.B.1    Johnson, K.S.2
  • 59
    • 0026445528 scopus 로고
    • Transforming growth factor-β: Recent progress and new challenges
    • Sporn, M.B., and A.B. Robert. 1992. Transforming growth factor-β: recent progress and new challenges. J. Cell Biol. 119:1017-1021.
    • (1992) J. Cell Biol. , vol.119 , pp. 1017-1021
    • Sporn, M.B.1    Robert, A.B.2
  • 60
    • 0026447801 scopus 로고
    • Release of transforming growth factor-β1 from the pericellular matrix of cultured fibroblasts and fibrosarcoma cells by plasmin and thrombin
    • Taipale, J., K. Koli, and J. Keski-Oja. 1992. Release of transforming growth factor-β1 from the pericellular matrix of cultured fibroblasts and fibrosarcoma cells by plasmin and thrombin. J. Biol. Chem. 267:25378-25384.
    • (1992) J. Biol. Chem. , vol.267 , pp. 25378-25384
    • Taipale, J.1    Koli, K.2    Keski-Oja, J.3
  • 61
    • 0027976521 scopus 로고
    • Latent transforming growth factor-β1 associates to fibroblast extracellular matrix via latent TGF-β binding protein
    • Taipale, J., K. Miyazono, C.H. Heldin, and J. Keski-Oja. 1994. Latent transforming growth factor-β1 associates to fibroblast extracellular matrix via latent TGF-β binding protein. J. Cell Biol. 124:171-181.
    • (1994) J. Cell Biol. , vol.124 , pp. 171-181
    • Taipale, J.1    Miyazono, K.2    Heldin, C.H.3    Keski-Oja, J.4
  • 62
    • 0028956737 scopus 로고
    • Human mast cell chymasc and leukocyte elastase release latent transforming growth factor-β1 from the extracellular matrix of cultured human epithelial and endothelial cells
    • Taipale, J., J. Lohi, J. Saarinen, P.T. Kovanen, and J. Keski-Oja. 1995. Human mast cell chymasc and leukocyte elastase release latent transforming growth factor-β1 from the extracellular matrix of cultured human epithelial and endothelial cells. J. Biol. Chem. 270:4689-4696.
    • (1995) J. Biol. Chem. , vol.270 , pp. 4689-4696
    • Taipale, J.1    Lohi, J.2    Saarinen, J.3    Kovanen, P.T.4    Keski-Oja, J.5
  • 63
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • Towbin, H., T. Staehelin, and J. Gordon. 1979. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc. Natl Acad. Sci. USA. 76:4350-4354.
    • (1979) Proc. Natl Acad. Sci. USA. , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 64
    • 0025885719 scopus 로고
    • Localization of cellular transglutaminase on the extracellular matrix after wounding: Characteristics of the matrix bound enzyme
    • Upchurch, H.F., E. Conway, M.K. Patterson, and M.D. Maxwell. 1991. Localization of cellular transglutaminase on the extracellular matrix after wounding: characteristics of the matrix bound enzyme. J. Cell. Physiol. 149:375-382.
    • (1991) J. Cell. Physiol. , vol.149 , pp. 375-382
    • Upchurch, H.F.1    Conway, E.2    Patterson, M.K.3    Maxwell, M.D.4
  • 66
    • 0028267099 scopus 로고
    • Structure and expression of fibrillin-2, a novel microfibrillar component preferentially located in elastic matrices
    • Zhang, H., S.D. Apfelroth, E. Hu, E.C. Davis, C. Sanguineti, J. Bonadio, R.P. Mecham, and F. Ramirez. 1994. Structure and expression of fibrillin-2, a novel microfibrillar component preferentially located in elastic matrices. J. Cell Biol. 124:855-863.
    • (1994) J. Cell Biol. , vol.124 , pp. 855-863
    • Zhang, H.1    Apfelroth, S.D.2    Hu, E.3    Davis, E.C.4    Sanguineti, C.5    Bonadio, J.6    Mecham, R.P.7    Ramirez, F.8


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