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Volumn 69, Issue 2-3, 2001, Pages 121-134

Dystroglycan binding to laminin α1LG4 module influences epithelial morphogenesis of salivary gland and lung in vitro

Author keywords

Dystroglycan; Laminin; Lung morphogenesis; Organ culture; Salivary gland morphogenesis

Indexed keywords

BLOCKING ANTIBODY; CYTOSKELETON PROTEIN; DYSTROGLYCAN; LAMININ; LAMININ 1; LAMININ RECEPTOR; MEMBRANE PROTEIN; MESSENGER RNA; MONOCLONAL ANTIBODY;

EID: 0035755874     PISSN: 03014681     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-0436.2001.690206.x     Document Type: Article
Times cited : (70)

References (71)
  • 1
    • 0033605915 scopus 로고    scopus 로고
    • Analysis of heparin, α-dystroglycan and sulfatide binding to the G domain of the laminin α1 chain by site-directed mutagenesis
    • Andac, Z., Sasaki, T., Mann, K., Brancaccio, A., Deutzmann, R. and Timpl, R. (1999) Analysis of heparin, α-dystroglycan and sulfatide binding to the G domain of the laminin α1 chain by site-directed mutagenesis. J Mol Biol 287:253-264.
    • (1999) J Mol Biol , vol.287 , pp. 253-264
    • Andac, Z.1    Sasaki, T.2    Mann, K.3    Brancaccio, A.4    Deutzmann, R.5    Timpl, R.6
  • 2
    • 0030589664 scopus 로고    scopus 로고
    • The extracellular matrix in epithelial biology: Shared molecules and common themes in distant phyla
    • Ashkenas, J., Muschler, J. and Bissell, M.J. (1996) The extracellular matrix in epithelial biology: shared molecules and common themes in distant phyla. Dev Biol 180:433-444.
    • (1996) Dev Biol , vol.180 , pp. 433-444
    • Ashkenas, J.1    Muschler, J.2    Bissell, M.J.3
  • 3
    • 0025233920 scopus 로고
    • Antibody to integrin α6 subunit specifically inhibits cell-binding to laminin fragment 8
    • Aumailley, M., Timpl, R. and Sonnenberg, A. (1990) Antibody to integrin α6 subunit specifically inhibits cell-binding to laminin fragment 8. Exp Cell Res 188:55-60.
    • (1990) Exp Cell Res , vol.188 , pp. 55-60
    • Aumailley, M.1    Timpl, R.2    Sonnenberg, A.3
  • 4
    • 0033950910 scopus 로고    scopus 로고
    • Altered synthesis of laminin 1 and absence of basement membrane component deposition in β1 integrin-deficient embryoid bodies
    • Aumailley, M., Pesh, M., Tungall, L., Gaill, F. and Fässler, R. (2000) Altered synthesis of laminin 1 and absence of basement membrane component deposition in β1 integrin-deficient embryoid bodies. J Cell Sci 113:259-268.
    • (2000) J Cell Sci , vol.113 , pp. 259-268
    • Aumailley, M.1    Pesh, M.2    Tungall, L.3    Gaill, F.4    Fässler, R.5
  • 5
    • 0031440110 scopus 로고    scopus 로고
    • Genetic analysis of β1 integrin function: Confirmed, new and revised roles for a crucial family of cell adhesion molecules
    • Brakebusch, C., Hirsch, E., Potocnick, A. and Fässler, R. (1997) Genetic analysis of β1 integrin function: confirmed, new and revised roles for a crucial family of cell adhesion molecules. J Cell Sci 110:2895-2904.
    • (1997) J Cell Sci , vol.110 , pp. 2895-2904
    • Brakebusch, C.1    Hirsch, E.2    Potocnick, A.3    Fässler, R.4
  • 6
    • 0029063024 scopus 로고
    • Electron microscopic evidence for a mucin-like region in chick muscle α-dystroglycan
    • Brancaccio, A., Schultess, T., Gesemann, M. and Engel, J. (1995) Electron microscopic evidence for a mucin-like region in chick muscle α-dystroglycan. FEBS Lett 368:139-142.
    • (1995) FEBS Lett , vol.368 , pp. 139-142
    • Brancaccio, A.1    Schultess, T.2    Gesemann, M.3    Engel, J.4
  • 7
    • 0033032081 scopus 로고    scopus 로고
    • Dystrophic phenotype induced in vitro by antibody blockade of muscle α-dystroglycan-laminin interaction
    • Brown, S.C., Fassati, A., Popplewell, L., Page, A.M., Henry, M.D., Campbell, K.P. and Dickson, G. (1999) Dystrophic phenotype induced in vitro by antibody blockade of muscle α-dystroglycan-laminin interaction. J Cell Sci 112:209-216.
    • (1999) J Cell Sci , vol.112 , pp. 209-216
    • Brown, S.C.1    Fassati, A.2    Popplewell, L.3    Page, A.M.4    Henry, M.D.5    Campbell, K.P.6    Dickson, G.7
  • 8
    • 0029965530 scopus 로고    scopus 로고
    • Identification of receptors binding fibronectin and laminin on fetal rat lung cells
    • Caniggia, I., Liu, J., Han, R., Wang, J., Tanswell, A.K., Laurie, G. and Post, M. (1996) Identification of receptors binding fibronectin and laminin on fetal rat lung cells. Am J Physiol 270:L459-L468.
    • (1996) Am J Physiol , vol.270
    • Caniggia, I.1    Liu, J.2    Han, R.3    Wang, J.4    Tanswell, A.K.5    Laurie, G.6    Post, M.7
  • 9
    • 0033519279 scopus 로고    scopus 로고
    • Laminin polymerization induces a receptor-cytoskeleton network
    • Colognato, H., Winkelmann, D.A. and Yurchenco, P. (1999) Laminin polymerization induces a receptor-cytoskeleton network. J Cell Biol 145:619-631.
    • (1999) J Cell Biol , vol.145 , pp. 619-631
    • Colognato, H.1    Winkelmann, D.A.2    Yurchenco, P.3
  • 10
    • 0034075654 scopus 로고    scopus 로고
    • Form and function: The laminin family of heterotrimers
    • Colognato, H. and Yurchenco, P. (2000) Form and function: the laminin family of heterotrimers. Dev Dyn 218:213-234.
    • (2000) Dev Dyn , vol.218 , pp. 213-234
    • Colognato, H.1    Yurchenco, P.2
  • 11
    • 0030960916 scopus 로고    scopus 로고
    • Laminin E8 alveolarization site: Heparin sensitivity, cell surface receptors, and role in cell spreading
    • Chen, L., Shick, V., Matter, M.L., Laurie, S.M., Ogle, R.C. and Laurie, G.W. (1997) Laminin E8 alveolarization site: heparin sensitivity, cell surface receptors, and role in cell spreading. Am J Physiol 272:L494-L503.
    • (1997) Am J Physiol , vol.272
    • Chen, L.1    Shick, V.2    Matter, M.L.3    Laurie, S.M.4    Ogle, R.C.5    Laurie, G.W.6
  • 12
    • 0031851579 scopus 로고    scopus 로고
    • Role of laminin-1, collagen IV, an autocrine factor(s) in regulated secretion by lacrimal acinar cells
    • Chen, L., Glass, J.D., Walton, S.C. and Laurie, G.W. (1998) Role of laminin-1, collagen IV, an autocrine factor(s) in regulated secretion by lacrimal acinar cells. Am J Physiol 275:C278-C284.
    • (1998) Am J Physiol , vol.275
    • Chen, L.1    Glass, J.D.2    Walton, S.C.3    Laurie, G.W.4
  • 14
    • 0032587606 scopus 로고    scopus 로고
    • Synergistic activities of α3 and α6 integrins are required during apical ectodermal ridge formation and organogenesis in the mouse
    • DeArcangelis, A., Mark, M., Kreidberg, J., Sorokin, L. and Georges-Labouesse, E. (1999) Synergistic activities of α3 and α6 integrins are required during apical ectodermal ridge formation and organogenesis in the mouse. Development 126:3957-3968.
    • (1999) Development , vol.126 , pp. 3957-3968
    • DeArcangelis, A.1    Mark, M.2    Kreidberg, J.3    Sorokin, L.4    Georges-Labouesse, E.5
  • 16
    • 0030610163 scopus 로고    scopus 로고
    • α3β1 integrin is required for normal development of epidermal basement membranes
    • DiPersio, C.M., Hodivala, D.K., Jaenisch, R., Kreidberg, J.A. and Hynes, R.O. (1997) α3β1 integrin is required for normal development of epidermal basement membranes. J Cell Biol 137:729-742.
    • (1997) J Cell Biol , vol.137 , pp. 729-742
    • DiPersio, C.M.1    Hodivala, D.K.2    Jaenisch, R.3    Kreidberg, J.A.4    Hynes, R.O.5
  • 17
    • 0030041083 scopus 로고    scopus 로고
    • Extracellular matrix biology in the lung
    • Dunsmore, S.E. and Rannels, D.E. (1996) Extracellular matrix biology in the lung. Am J Physiol 270:L3-L27.
    • (1996) Am J Physiol , vol.270
    • Dunsmore, S.E.1    Rannels, D.E.2
  • 21
    • 0033543647 scopus 로고    scopus 로고
    • Biochemical characterization of the epithelial dystroglycan complex
    • Durbeej, M. and Campbell, K.P. (1999) Biochemical characterization of the epithelial dystroglycan complex. J Biol Chem 274:26609-26616.
    • (1999) J Biol Chem , vol.274 , pp. 26609-26616
    • Durbeej, M.1    Campbell, K.P.2
  • 25
    • 0025815479 scopus 로고
    • Membrane organization of the dystrophin-glycoprotein complex
    • Ervasti, J.M. and Campbell, K.P. (1991) Membrane organization of the dystrophin-glycoprotein complex. Cell 66:1121-1131.
    • (1991) Cell , vol.66 , pp. 1121-1131
    • Ervasti, J.M.1    Campbell, K.P.2
  • 26
    • 0027275643 scopus 로고
    • A role for the dystrophin-glycoprotein complex as a transmembrane linker between laminin and actin
    • Ervasti, J.M. and Campbell, K.P. (1993) A role for the dystrophin-glycoprotein complex as a transmembrane linker between laminin and actin. J Cell Biol 122:809-823.
    • (1993) J Cell Biol , vol.122 , pp. 809-823
    • Ervasti, J.M.1    Campbell, K.P.2
  • 27
    • 0032715703 scopus 로고    scopus 로고
    • Restricted distribution of laminin α1 chain in normal adult mouse tissues
    • Falk, M., Ferletta, M., Forsberg, E. and Ekblom, P. (1999) Restricted distribution of laminin α1 chain in normal adult mouse tissues. Matrix Biol 18:557-568.
    • (1999) Matrix Biol , vol.18 , pp. 557-568
    • Falk, M.1    Ferletta, M.2    Forsberg, E.3    Ekblom, P.4
  • 28
    • 0032921536 scopus 로고    scopus 로고
    • Identification of laminin-10/11 as a strong cell adhesive complex for a normal and a malignant human epithelial cell line
    • Ferletta, M. and Ekblom, P. (1999) Identification of laminin-10/11 as a strong cell adhesive complex for a normal and a malignant human epithelial cell line. J Cell Sci 112:1-10.
    • (1999) J Cell Sci , vol.112 , pp. 1-10
    • Ferletta, M.1    Ekblom, P.2
  • 29
    • 0031657163 scopus 로고    scopus 로고
    • Laminin 2 attachment selects myofibroblasts from fetal mouse lung
    • Flores-Delgado, G., Bringas, P. and Warburton, D. (1998) Laminin 2 attachment selects myofibroblasts from fetal mouse lung. Am J Physiol 275:L622-L630.
    • (1998) Am J Physiol , vol.275
    • Flores-Delgado, G.1    Bringas, P.2    Warburton, D.3
  • 30
    • 0029143930 scopus 로고
    • Cloning and complete primary structure of the mouse laminin α3 chain
    • Galliano, M.F., Aberdam, D., Aguzzi, A., Ortonne, J.P. and Meneguzzi, G. (1995) Cloning and complete primary structure of the mouse laminin α3 chain. J Biol Chem 270:21820-21825.
    • (1995) J Biol Chem , vol.270 , pp. 21820-21825
    • Galliano, M.F.1    Aberdam, D.2    Aguzzi, A.3    Ortonne, J.P.4    Meneguzzi, G.5
  • 31
    • 0040784424 scopus 로고    scopus 로고
    • N-cadherin, a cell adhesion molecule involved in establishment of embryonic left-right assymetry
    • García-Castro, M.I., Vielmetter, E. and Bronner-Fraser, M. (2000) N-cadherin, a cell adhesion molecule involved in establishment of embryonic left-right assymetry. Science 288:1047-1051.
    • (2000) Science , vol.288 , pp. 1047-1051
    • García-Castro, M.I.1    Vielmetter, E.2    Bronner-Fraser, M.3
  • 32
    • 0027321171 scopus 로고
    • Laminin-binding protein 120 from brain is closely related to the dystrophin-associated glycoprotein, dystroglycan, and binds with high affinity to the major heparin binding domain of laminin
    • Gee, S.H., Blacker, R.W., Douville, P.J., Provost, P.R., Yurchenco, P.D. and Carbonetto, S. (1993) Laminin-binding protein 120 from brain is closely related to the dystrophin-associated glycoprotein, dystroglycan, and binds with high affinity to the major heparin binding domain of laminin. J Biol Chem 268:14972-14980.
    • (1993) J Biol Chem , vol.268 , pp. 14972-14980
    • Gee, S.H.1    Blacker, R.W.2    Douville, P.J.3    Provost, P.R.4    Yurchenco, P.D.5    Carbonetto, S.6
  • 33
    • 0029908558 scopus 로고    scopus 로고
    • Absence of the α6 integrin leads to epidermolysis bullosa and neonatal death in mice
    • Georges-Labouesse, E., Messadeq, N., Yehi, G., Cadalbert, L., Dierich, A. and LeMeur, M. (1996) Absence of the α6 integrin leads to epidermolysis bullosa and neonatal death in mice. Nat Genet 13:370-373.
    • (1996) Nat Genet , vol.13 , pp. 370-373
    • Georges-Labouesse, E.1    Messadeq, N.2    Yehi, G.3    Cadalbert, L.4    Dierich, A.5    Lemeur, M.6
  • 34
    • 0033560842 scopus 로고    scopus 로고
    • Characterization of bone marrow laminins and identification of α5-containing laminins as adhesive proteins for multipotent hematopoietic FDCP-Mix cells
    • Gu, Y., Sorokin, L., Durbeej, M., Hjalt, T., Jönsson, J. and Ekblom, M. (1999) Characterization of bone marrow laminins and identification of α5-containing laminins as adhesive proteins for multipotent hematopoietic FDCP-Mix cells. Blood 93:2533-2542.
    • (1999) Blood , vol.93 , pp. 2533-2542
    • Gu, Y.1    Sorokin, L.2    Durbeej, M.3    Hjalt, T.4    Jönsson, J.5    Ekblom, M.6
  • 35
    • 0032445403 scopus 로고    scopus 로고
    • A role for dystroglycan in basement membrane assembly
    • Henry, M.D. and Campbell, K.P. (1998) A role for dystroglycan in basement membrane assembly. Cell 95:859-870.
    • (1998) Cell , vol.95 , pp. 859-870
    • Henry, M.D.1    Campbell, K.P.2
  • 37
    • 0033231551 scopus 로고    scopus 로고
    • The crystal structure of a laminin G-like module reveals the molecular basis of α-dystroglycan binding to laminins, perlecan, and agrin
    • Hohenester, E., Tisi, D., Talts, J.F. and Timpl, R. (1999) The crystal structure of a laminin G-like module reveals the molecular basis of α-dystroglycan binding to laminins, perlecan, and agrin. Mol Cell 4:783-792.
    • (1999) Mol Cell , vol.4 , pp. 783-792
    • Hohenester, E.1    Tisi, D.2    Talts, J.F.3    Timpl, R.4
  • 39
    • 0035260033 scopus 로고    scopus 로고
    • Regulation of laminin-1-induced pancreatic β-cell differentiation by α6 integrin and α-dystroglycan
    • Jiang, F.X., Georges-Labouesse, E. and Harrison, L.C. (2001) Regulation of laminin-1-induced pancreatic β-cell differentiation by α6 integrin and α-dystroglycan. Mol Med 7:107-114.
    • (2001) Mol Med , vol.7 , pp. 107-114
    • Jiang, F.X.1    Georges-Labouesse, E.2    Harrison, L.C.3
  • 40
    • 0028960136 scopus 로고
    • Antibodies against domain E3 of laminin-1 and integrin α6 subunit perturb branching epithelial morphogenesis of the embryonic submandibular gland, but by different modes
    • Kadoya, Y., Kadoya, K., Durbeej, M., Holmvall, K., Sorokin, L. and Ekblom, P. (1995) Antibodies against domain E3 of laminin-1 and integrin α6 subunit perturb branching epithelial morphogenesis of the embryonic submandibular gland, but by different modes. J Cell Biol 129:521-534.
    • (1995) J Cell Biol , vol.129 , pp. 521-534
    • Kadoya, Y.1    Kadoya, K.2    Durbeej, M.3    Holmvall, K.4    Sorokin, L.5    Ekblom, P.6
  • 41
    • 0031596408 scopus 로고    scopus 로고
    • Laminin α1 chain G domain peptide, RKRLQVQLSIRT, inhibits epithelial branching morphogenesis of cultured embryonic mouse submandibular gland
    • Kadoya, Y., Nomizu, M., Sorokin, L.M., Yamashina, S. and Yamada, Y. (1998) Laminin α1 chain G domain peptide, RKRLQVQLSIRT, inhibits epithelial branching morphogenesis of cultured embryonic mouse submandibular gland. Dev Dyn 212:394-402.
    • (1998) Dev Dyn , vol.212 , pp. 394-402
    • Kadoya, Y.1    Nomizu, M.2    Sorokin, L.M.3    Yamashina, S.4    Yamada, Y.5
  • 42
    • 0034025635 scopus 로고    scopus 로고
    • Integrin binding specificity of laminin-10/11: Laminin-10/11 are recognized by α3β1, α6β1 and α6β4 integrins
    • Kikkawa, Y., Sanzen, N., Fujiwara, H., Sonnenberg, A. and Sekiguchi, K. (2000) Integrin binding specificity of laminin-10/11: laminin-10/11 are recognized by α3β1, α6β1 and α6β4 integrins. J Cell Sci 113:869-876.
    • (2000) J Cell Sci , vol.113 , pp. 869-876
    • Kikkawa, Y.1    Sanzen, N.2    Fujiwara, H.3    Sonnenberg, A.4    Sekiguchi, K.5
  • 43
    • 0023709019 scopus 로고
    • Role of laminin A chain for the development of epithelial cell polarity
    • Klein, G., Langegger, M., Timpl, R. and Ekblom, P. (1988) Role of laminin A chain for the development of epithelial cell polarity. Cell 55:331-341.
    • (1988) Cell , vol.55 , pp. 331-341
    • Klein, G.1    Langegger, M.2    Timpl, R.3    Ekblom, P.4
  • 44
    • 0025222775 scopus 로고
    • Differential expression of laminin A and B chains during development of embryonic mouse organs
    • Klein, G., Ekblom, M., Fecker, L., Timpl, R. and Ekblom, P. (1990) Differential expression of laminin A and B chains during development of embryonic mouse organs. Development 110:823-837.
    • (1990) Development , vol.110 , pp. 823-837
    • Klein, G.1    Ekblom, M.2    Fecker, L.3    Timpl, R.4    Ekblom, P.5
  • 46
    • 0028302929 scopus 로고
    • A novel laminin E8 cell adhesion site required for lung alveolar formation in vitro
    • Matter, M. and Laurie, G.W. (1994) A novel laminin E8 cell adhesion site required for lung alveolar formation in vitro. J Cell Biol 124:1083-1090.
    • (1994) J Cell Biol , vol.124 , pp. 1083-1090
    • Matter, M.1    Laurie, G.W.2
  • 47
    • 0030919488 scopus 로고    scopus 로고
    • The laminin α chains: Expression, developmental transitions, and chromosomal locations of α1-5, identification of heterotrimeric laminins 8-11, cloning of a novel α3 isoform
    • Miner, J.H., Patton, B.L., Lentz, S.I., Gilbert, D.J., Snider, W.D., Jenkins, N.A., Copeland, N.G. and Sanes, J.R. (1997) The laminin α chains: expression, developmental transitions, and chromosomal locations of α1-5, identification of heterotrimeric laminins 8-11, cloning of a novel α3 isoform. J Cell Biol 137:685-701.
    • (1997) J Cell Biol , vol.137 , pp. 685-701
    • Miner, J.H.1    Patton, B.L.2    Lentz, S.I.3    Gilbert, D.J.4    Snider, W.D.5    Jenkins, N.A.6    Copeland, N.G.7    Sanes, J.R.8
  • 48
    • 0032109493 scopus 로고    scopus 로고
    • A correlation between epithelial proliferation rates, basement membrane component localization patterns, and morphogenetic potential in the embryonic mouse lung
    • Mollard, R. and Dziadek, M. (1998) A correlation between epithelial proliferation rates, basement membrane component localization patterns, and morphogenetic potential in the embryonic mouse lung. Am J Respir Cell Mol Biol 1:71-82.
    • (1998) Am J Respir Cell Mol Biol , vol.1 , pp. 71-82
    • Mollard, R.1    Dziadek, M.2
  • 49
    • 0032586951 scopus 로고    scopus 로고
    • Division of labor among the α6β4 integrin, β1 integrins, and an E3 laminin receptor to signal morphogenesis and β-casein expression in mammary epithelial cells
    • Muschler, J., Lochter, A., Roskelley, C.D., Yurchenco, P. and Bissell, M. (1999) Division of labor among the α6β4 integrin, β1 integrins, and an E3 laminin receptor to signal morphogenesis and β-casein expression in mammary epithelial cells. Mol Biol Cell 10:2817-2828.
    • (1999) Mol Biol Cell , vol.10 , pp. 2817-2828
    • Muschler, J.1    Lochter, A.2    Roskelley, C.D.3    Yurchenco, P.4    Bissell, M.5
  • 50
    • 0029100640 scopus 로고
    • Identification of cell binding sites in the laminin α1 chain carboxyterminal globular domains by systematic screening of synthetic peptides
    • Nomizu, M., Kim, W.H., Yamamura, K., Utani, A., Son, S., Otaka, A., Roller, P.P., Kleinman, H.K. and Yamada, Y. (1995) Identification of cell binding sites in the laminin α1 chain carboxyterminal globular domains by systematic screening of synthetic peptides. J Biol Chem 270:20583-20590.
    • (1995) J Biol Chem , vol.270 , pp. 20583-20590
    • Nomizu, M.1    Kim, W.H.2    Yamamura, K.3    Utani, A.4    Son, S.5    Otaka, A.6    Roller, P.P.7    Kleinman, H.K.8    Yamada, Y.9
  • 51
    • 0026328022 scopus 로고
    • Dystrophin-associated proteins are greatly reduced in skeletal muscle from mdx mice
    • Ohlendieck, K. and Campbell, K.P. (1991) Dystrophin-associated proteins are greatly reduced in skeletal muscle from mdx mice. J Cell Biol 115:1685-1694.
    • (1991) J Cell Biol , vol.115 , pp. 1685-1694
    • Ohlendieck, K.1    Campbell, K.P.2
  • 52
    • 0034537124 scopus 로고    scopus 로고
    • Expression patterns of laminin α1 and α5 in human lung during development
    • Pierce, R.A., Griffin, G., Miner, J.H. and Senior, R.M. (2000) Expression patterns of laminin α1 and α5 in human lung during development. Am J Resp Cell Mol Biol 23:742-747.
    • (2000) Am J Resp Cell Mol Biol , vol.23 , pp. 742-747
    • Pierce, R.A.1    Griffin, G.2    Miner, J.H.3    Senior, R.M.4
  • 53
    • 0028007259 scopus 로고
    • A novel laminin-binding form of syndecan-1 (cell surface proteoglycans) produced by syndecan-1 cDNA transfected NIH-3T3 cells
    • Salmivirta, M., Mali, M., Heino, J., Hermonen, J. and Jalkanen, M. (1994) A novel laminin-binding form of syndecan-1 (cell surface proteoglycans) produced by syndecan-1 cDNA transfected NIH-3T3 cells. Exp Cell Res 215:180-188.
    • (1994) Exp Cell Res , vol.215 , pp. 180-188
    • Salmivirta, M.1    Mali, M.2    Heino, J.3    Hermonen, J.4    Jalkanen, M.5
  • 54
    • 0031846576 scopus 로고    scopus 로고
    • Deficiency of β1 integrins in teratoma interferes with basement membrane assembly and laminin-1 expression
    • Sasaki, T., Forsberg, E., Bloch, W., Addics, K., Fässler, R. and Timpl, R. (1998) Deficiency of β1 integrins in teratoma interferes with basement membrane assembly and laminin-1 expression. Exp Cell Res 238:70-81.
    • (1998) Exp Cell Res , vol.238 , pp. 70-81
    • Sasaki, T.1    Forsberg, E.2    Bloch, W.3    Addics, K.4    Fässler, R.5    Timpl, R.6
  • 55
    • 0025870487 scopus 로고
    • Identification of laminin domains involved in branching morphogenesis: Effects of anti-laminin monoclonal antibodies on mouse embryonic lung development
    • Schuger, L., Skubitz, A.P.M., O'Shea, S., Chang, J.F. and Varani, J. (1991) 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) Dev Biol , vol.146 , pp. 531-541
    • Schuger, L.1    Skubitz, A.P.M.2    O'Shea, S.3    Chang, J.F.4    Varani, J.5
  • 56
    • 0029060386 scopus 로고
    • Two separate domains of laminin promote lung organogenesis by different mechanisms of action
    • Schuger, L., Skubitz, A.P.M., De Las Morenas, A. and Gilbridge, K. (1995) Two separate domains of laminin promote lung organogenesis by different mechanisms of action. Dev Biol 169:520-532.
    • (1995) Dev Biol , vol.169 , pp. 520-532
    • Schuger, L.1    Skubitz, A.P.M.2    De Las Morenas, A.3    Gilbridge, K.4
  • 57
    • 0030612005 scopus 로고    scopus 로고
    • Laminin β1 chain synthesis in the mouse developing lung: Requirement for epithelial-mesenchymal contact and possible role in bronchial smooth muscle development
    • Schuger, L., Skubitz, A.P.M., Zhang, J., Sorokin, L. and He, L. (1997) Laminin β1 chain synthesis in the mouse developing lung: requirement for epithelial-mesenchymal contact and possible role in bronchial smooth muscle development. J Cell Biol 139:553-562.
    • (1997) J Cell Biol , vol.139 , pp. 553-562
    • Schuger, L.1    Skubitz, A.P.M.2    Zhang, J.3    Sorokin, L.4    He, L.5
  • 58
    • 0031909937 scopus 로고    scopus 로고
    • Laminin fragment E4 inhibition studies: Basement membrane assembly and embryonic lung epithelial cell polarization requires laminin polymerization
    • Schuger, L., Yurchenco, P., Realn, N.K. and Yang, Y. (1998) Laminin fragment E4 inhibition studies: basement membrane assembly and embryonic lung epithelial cell polarization requires laminin polymerization. Int J Dev Biol 42:217-220.
    • (1998) Int J Dev Biol , vol.42 , pp. 217-220
    • Schuger, L.1    Yurchenco, P.2    Realn, N.K.3    Yang, Y.4
  • 59
    • 0033597343 scopus 로고    scopus 로고
    • Adhesion of cultured bovine aortic endothelial cells to laminin-1 mediated by dystroglycan
    • Shimizu, H., Hosokawa, H., Ninomiya, H., Miner, J.H. and Masaki, T. (1999) Adhesion of cultured bovine aortic endothelial cells to laminin-1 mediated by dystroglycan. J Biol Chem 274:11995-12000.
    • (1999) J Biol Chem , vol.274 , pp. 11995-12000
    • Shimizu, H.1    Hosokawa, H.2    Ninomiya, H.3    Miner, J.H.4    Masaki, T.5
  • 60
    • 0023932372 scopus 로고
    • Localization of three distinct heparin-binding domains of laminin by monoclonal antibodies
    • Skubitz, A.P.N., McCarthy, J.B., Charonis, A.S. and Furcht, L.T. (1988) Localization of three distinct heparin-binding domains of laminin by monoclonal antibodies. J Biol Chem 263:4861-4868.
    • (1988) J Biol Chem , vol.263 , pp. 4861-4868
    • Skubitz, A.P.N.1    McCarthy, J.B.2    Charonis, A.S.3    Furcht, L.T.4
  • 61
    • 0026631140 scopus 로고
    • Monoclonal antibodies against laminin A chain fragment E3 and their effects on binding to cells and proteoglycan and on kidney development
    • Sorokin, L.M., Conzelmann, S., Ekblom, P., Battaglia, C., Aumailley, M. and Timpl, R. (1992) Monoclonal antibodies against laminin A chain fragment E3 and their effects on binding to cells and proteoglycan and on kidney development. Exp Cell Res 201:137-144.
    • (1992) Exp Cell Res , vol.201 , pp. 137-144
    • Sorokin, L.M.1    Conzelmann, S.2    Ekblom, P.3    Battaglia, C.4    Aumailley, M.5    Timpl, R.6
  • 62
    • 0031572281 scopus 로고    scopus 로고
    • Developmental regulation of the laminin α5 chain suggests a role in epithelial and endothelial maturation
    • Sorokin, L.M., Pausch, F., Frieser, M., Kroger, S., Ohage, E. and Deutzmann, R. (1997) Developmental regulation of the laminin α5 chain suggests a role in epithelial and endothelial maturation. Dev Biol 198:285-300.
    • (1997) Dev Biol , vol.198 , pp. 285-300
    • Sorokin, L.M.1    Pausch, F.2    Frieser, M.3    Kroger, S.4    Ohage, E.5    Deutzmann, R.6
  • 64
    • 0032847081 scopus 로고    scopus 로고
    • Mutation of a basic sequence in the laminin α2LG3 module leads to a lack of proteolytic processing and has different effects on β1 integrin-mediated cell adhesion and α-dystroglycan binding
    • Talts, J.F. and Timpl, R. (1999) Mutation of a basic sequence in the laminin α2LG3 module leads to a lack of proteolytic processing and has different effects on β1 integrin-mediated cell adhesion and α-dystroglycan binding. FEBS Lett 458:319-323.
    • (1999) FEBS Lett , vol.458 , pp. 319-323
    • Talts, J.F.1    Timpl, R.2
  • 65
    • 0031033854 scopus 로고    scopus 로고
    • Characterization of monoclonal antibodies against tenascin-C: No apparent effect on kidney development in vitro
    • Talts, J.F., Eng, H., Zhang, H.Y., Faissner, A. and Ekblom, P. (1997) Characterization of monoclonal antibodies against tenascin-C: no apparent effect on kidney development in vitro. Int J Dev Biol 41:39-48.
    • (1997) Int J Dev Biol , vol.41 , pp. 39-48
    • Talts, J.F.1    Eng, H.2    Zhang, H.Y.3    Faissner, A.4    Ekblom, P.5
  • 66
    • 0033557707 scopus 로고    scopus 로고
    • Binding of the G domains of laminin α and α2 chains and perlecan to heparin, sulfatides, α-dystroglycan and several extracellular matrix proteins
    • Talts, J.F., Andac, Z., Göhring, W., Brancaccio, A. and Timpl, R. (1999) Binding of the G domains of laminin α and α2 chains and perlecan to heparin, sulfatides, α-dystroglycan and several extracellular matrix proteins. EMBO J 18:863-870.
    • (1999) EMBO J , vol.18 , pp. 863-870
    • Talts, J.F.1    Andac, Z.2    Göhring, W.3    Brancaccio, A.4    Timpl, R.5
  • 68
    • 0034600063 scopus 로고    scopus 로고
    • Structure of the C-terminal laminin G-like domain pair of the laminin α2 chain harboring binding sites for α-dystroglycan and heparin
    • Tisi, D., Talts, J.F., Timpl, R. and Hohenester, E. (2000) Structure of the C-terminal laminin G-like domain pair of the laminin α2 chain harboring binding sites for α-dystroglycan and heparin. EMBO J 19:1432-1440.
    • (2000) EMBO J , vol.19 , pp. 1432-1440
    • Tisi, D.1    Talts, J.F.2    Timpl, R.3    Hohenester, E.4


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