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Volumn 100, Issue 7, 1997, Pages 1870-1881

Integrins (α7β1) in muscle function and survival disrupted expression in merosin-deficient congenital muscular dystrophy

Author keywords

Apoptosis; Basement membrane; Dystrophin glycoprotein complex; Extracellular matrix; Laminin receptor

Indexed keywords

DYSTROPHIN; INTEGRIN; LAMININ; LAMININ RECEPTOR; PROTEOGLYCAN; UTROPHIN; BETA1 INTEGRIN; CYTOSKELETON PROTEIN; INTEGRIN ALPHA7BETA1; MEMBRANE PROTEIN;

EID: 0030610576     PISSN: 00219738     EISSN: None     Source Type: Journal    
DOI: 10.1172/JCI119716     Document Type: Article
Times cited : (186)

References (79)
  • 1
    • 0022357453 scopus 로고
    • The extracellular matrix of skeletal muscle
    • Mayne, R., and R.D. Sanderson. 1985. The extracellular matrix of skeletal muscle. Collagen. Relat. Res 5:444-468.
    • (1985) Collagen. Relat. Res , vol.5 , pp. 444-468
    • Mayne, R.1    Sanderson, R.D.2
  • 2
    • 0028914964 scopus 로고
    • Three muscular dystrophies: Loss of cytoskeleton-extracellular matrix linkage
    • Campbell, K.P. 1995. Three muscular dystrophies: loss of cytoskeleton-extracellular matrix linkage. Cell. 80:675-679.
    • (1995) Cell , vol.80 , pp. 675-679
    • Campbell, K.P.1
  • 4
    • 0030465319 scopus 로고    scopus 로고
    • Merosin/laminin-2 and muscular dystrophy
    • Wewer, U.M., and E. Engvall. 1996. Merosin/laminin-2 and muscular dystrophy. Neuromuscul. Disord. 6:409-118.
    • (1996) Neuromuscul. Disord. , vol.6 , pp. 409-1118
    • Wewer, U.M.1    Engvall, E.2
  • 9
    • 0023970247 scopus 로고
    • Merosin, a protein specific for basement membranes of Schwann cells, striated muscle, and trophoblast, is expressed late in nerve and muscle development
    • Leivo, I., and E. Engvall. 1988. Merosin, a protein specific for basement membranes of Schwann cells, striated muscle, and trophoblast, is expressed late in nerve and muscle development. Proc. Natl. Acad. Sci. USA. 85:1544-1548.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 1544-1548
    • Leivo, I.1    Engvall, E.2
  • 12
    • 0028098737 scopus 로고
    • Abnormal expression of laminin suggests disturbance of sarcolemma-extracellular matrix interaction in Japanese patients with autosomal recessive muscular dystrophy deficient in adhalin
    • Higuchi, I., H. Yamada, H. Fukunaga, H. Iwaki, R. Okubo, M. Nakagawa, M. Osame, S.L. Roberds, T. Shimizu, K.P. Campbell, and K. Matsumura. 1994. Abnormal expression of laminin suggests disturbance of sarcolemma-extracellular matrix interaction in Japanese patients with autosomal recessive muscular dystrophy deficient in adhalin. J. Clin. Invest. 94:601-606.
    • (1994) J. Clin. Invest. , vol.94 , pp. 601-606
    • Higuchi, I.1    Yamada, H.2    Fukunaga, H.3    Iwaki, H.4    Okubo, R.5    Nakagawa, M.6    Osame, M.7    Roberds, S.L.8    Shimizu, T.9    Campbell, K.P.10    Matsumura, K.11
  • 13
    • 0029396750 scopus 로고
    • Laminin β2 chain and adhalin deficiency in the skeletal muscle of Walker-Warburg syndrome (cerebro-ocular dysplasia-muscular dystrophy)
    • Wewer, U.M., M.E. Durkin, X. Zhang, H. Laursen, N.H. Nielsen, J. Towfighi, E. Engvall, and R. Albrechtsen. 1995. Laminin β2 chain and adhalin deficiency in the skeletal muscle of Walker-Warburg syndrome (cerebro-ocular dysplasia-muscular dystrophy). Neurology. 45:2099-2101.
    • (1995) Neurology , vol.45 , pp. 2099-2101
    • Wewer, U.M.1    Durkin, M.E.2    Zhang, X.3    Laursen, H.4    Nielsen, N.H.5    Towfighi, J.6    Engvall, E.7    Albrechtsen, R.8
  • 15
    • 0028318185 scopus 로고
    • Deficiency of merosin in dystrophic dy mice and genetic linkage of laminin M chain gene to dy locus
    • Sunada, Y., S.M. Bernier, C.A. Kozak, Y. Yamada, and K.P. Campbell. 1994. Deficiency of merosin in dystrophic dy mice and genetic linkage of laminin M chain gene to dy locus. J. Biol. Chem. 269:13729-13732.
    • (1994) J. Biol. Chem. , vol.269 , pp. 13729-13732
    • Sunada, Y.1    Bernier, S.M.2    Kozak, C.A.3    Yamada, Y.4    Campbell, K.P.5
  • 16
    • 0028334735 scopus 로고
    • Defective muscle basement membrane and lack of M-laminin in the dystrophic dy/dy mouse
    • Xu, H., P. Christmas, X.-R. Wu, U.M. Wewer, and E. Engvall. 1994. Defective muscle basement membrane and lack of M-laminin in the dystrophic dy/dy mouse. Proc. Natl. Acad. Sci. USA. 91:5572-5576.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 5572-5576
    • Xu, H.1    Christmas, P.2    Wu, X.-R.3    Wewer, U.M.4    Engvall, E.5
  • 17
    • 0028135436 scopus 로고
    • Murine muscular dystrophy caused by a mutation in the laminin α2 (Lama2) gene
    • Xu, H., X.-R. Wu, U.M. Wewer, and E. Engvall. 1994. Murine muscular dystrophy caused by a mutation in the laminin α2 (Lama2) gene. Nat. Genet. 8: 297-302.
    • (1994) Nat. Genet. , vol.8 , pp. 297-302
    • Xu, H.1    Wu, X.-R.2    Wewer, U.M.3    Engvall, E.4
  • 19
    • 0029992191 scopus 로고    scopus 로고
    • Disruption of muscle basal lamina in congenital muscular dystrophy with merosin deficiency
    • Minetti, C., M. Bado, G. Morreale, M. Pedemonte, and G. Cordone. 1996. Disruption of muscle basal lamina in congenital muscular dystrophy with merosin deficiency. Neurology. 46:1354-1358.
    • (1996) Neurology , vol.46 , pp. 1354-1358
    • Minetti, C.1    Bado, M.2    Morreale, G.3    Pedemonte, M.4    Cordone, G.5
  • 21
    • 0030982138 scopus 로고    scopus 로고
    • Electron microscopic examination of basal lamina in Fukuyama congenital muscular dystrophy
    • Ishii, H., Y.K. Hayashi, I. Nonaka, and K. Arahata. 1997. Electron microscopic examination of basal lamina in Fukuyama congenital muscular dystrophy. Neuromusc. Disord. 7:191-197.
    • (1997) Neuromusc. Disord. , vol.7 , pp. 191-197
    • Ishii, H.1    Hayashi, Y.K.2    Nonaka, I.3    Arahata, K.4
  • 22
    • 0029794008 scopus 로고    scopus 로고
    • Merosin and laminin in myogenesis: Specific requirement for merosin in myotube stability and survival
    • Vachon, P.H., F. Loechel, H. Xu, U.M. Wewer, and E. Engvall. 1996. Merosin and laminin in myogenesis: specific requirement for merosin in myotube stability and survival. J. Cell Biol. 134:1483-1497.
    • (1996) J. Cell Biol. , vol.134 , pp. 1483-1497
    • Vachon, P.H.1    Loechel, F.2    Xu, H.3    Wewer, U.M.4    Engvall, E.5
  • 23
    • 0027275643 scopus 로고
    • A role for the dystrophin-glycoprotein complex as a transmembrane linker between laminin and actin
    • Ervasti, J.M., and K.P. Campbell 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
  • 24
    • 0030968026 scopus 로고    scopus 로고
    • Laminin-induced clustering of dystroglycan on embryonic muscle cells: Comparison with agrin-induced clustering
    • Cohen, M.W., C. Jacobson, P.D. Yurchenco, G.E. Morris, and S. Carbonetto. 1997. Laminin-induced clustering of dystroglycan on embryonic muscle cells: comparison with agrin-induced clustering. J. Cell Biol. 136:1047-1058.
    • (1997) J. Cell Biol. , vol.136 , pp. 1047-1058
    • Cohen, M.W.1    Jacobson, C.2    Yurchenco, P.D.3    Morris, G.E.4    Carbonetto, S.5
  • 25
    • 0026770377 scopus 로고
    • Integrins: Versatility, modulation and signaling in cell adhesion
    • Hynes, R.O. 1992. Integrins: versatility, modulation and signaling in cell adhesion. Cell. 69:11-25.
    • (1992) Cell , vol.69 , pp. 11-25
    • Hynes, R.O.1
  • 26
    • 0029775681 scopus 로고    scopus 로고
    • RGD and other recognition sequences for integrins
    • Ruoslahti, E. 1996. RGD and other recognition sequences for integrins. Ann. Rev. Cell Dev. Biol. 12:697-715.
    • (1996) Ann. Rev. Cell Dev. Biol. , vol.12 , pp. 697-715
    • Ruoslahti, E.1
  • 27
    • 0029973887 scopus 로고    scopus 로고
    • Integrin-dependent signal transduclion
    • Lafrenie, R.M., and K.M. Yamada. 1996. Integrin-dependent signal transduclion. J. Cell. Biochem. 61:543-553.
    • (1996) J. Cell. Biochem. , vol.61 , pp. 543-553
    • Lafrenie, R.M.1    Yamada, K.M.2
  • 28
    • 0028335948 scopus 로고
    • Anchorage dependence, integrins, and apoptosis
    • Ruoslahti, E., and J.C. Reed. 1944. Anchorage dependence, integrins, and apoptosis. Cell. 77:477-478.
    • (1944) Cell , vol.77 , pp. 477-478
    • Ruoslahti, E.1    Reed, J.C.2
  • 30
    • 0023649186 scopus 로고
    • Occupation of the extracellular matrix receptor, integrin, is a central point for myogenic differentiation
    • Menko, A.S., and D. Boettinger. 1987. Occupation of the extracellular matrix receptor, integrin, is a central point for myogenic differentiation. Cell. 51:51-57.
    • (1987) Cell , vol.51 , pp. 51-57
    • Menko, A.S.1    Boettinger, D.2
  • 31
    • 0025153883 scopus 로고
    • A role for integrin in the formation of sarcomeric cytoarchitecture
    • Volk, T., L.I. Fessler, and J.H. Fessler. 1990. A role for integrin in the formation of sarcomeric cytoarchitecture. Cell. 63:525-536.
    • (1990) Cell , vol.63 , pp. 525-536
    • Volk, T.1    Fessler, L.I.2    Fessler, J.H.3
  • 32
    • 0027433289 scopus 로고
    • α7β1 integrin is a component of the myotendinous junction on skeletal muscle
    • Bao, Z.Z., M. Lakonishok, S. Kaufman, and A.F. Horwitz. 1993. α7β1 integrin is a component of the myotendinous junction on skeletal muscle. J. Cell Sci. 106:579-590.
    • (1993) J. Cell Sci. , vol.106 , pp. 579-590
    • Bao, Z.Z.1    Lakonishok, M.2    Kaufman, S.3    Horwitz, A.F.4
  • 33
    • 0028890992 scopus 로고
    • 3 integrin subunits are associated with myofibrils during myofibrillogenesis
    • 3 integrin subunits are associated with myofibrils during myofibrillogenesis. J. Cell Sci. 108:975-983.
    • (1995) J. Cell Sci. , vol.108 , pp. 975-983
    • McDonald, K.A.1    Lakonishok, M.2    Horwitz, A.F.3
  • 34
    • 0028990430 scopus 로고
    • pat-3 heterodimers, a family of essential integrin receptors in C. elegans
    • pat-3 heterodimers, a family of essential integrin receptors in C. elegans. J. Cell Biol. 129:1127-1141.
    • (1995) J. Cell Biol. , vol.129 , pp. 1127-1141
    • Gettner, S.N.1    Kenyon, C.2    Reichardt, L.F.3
  • 35
    • 0029664439 scopus 로고    scopus 로고
    • Integrin a subunit ratios, cytoplasmic domains, and growth factor synergy regulate muscle proliferation and differentiation
    • Sastry, S.K., M. Lakonishok, D.A. Thomas, J. Muschler, and A.F. Horwitz. 1996. Integrin a subunit ratios, cytoplasmic domains, and growth factor synergy regulate muscle proliferation and differentiation. J. Cell Biol. 133:169-184.
    • (1996) J. Cell Biol. , vol.133 , pp. 169-184
    • Sastry, S.K.1    Lakonishok, M.2    Thomas, D.A.3    Muschler, J.4    Horwitz, A.F.5
  • 36
    • 0027409341 scopus 로고
    • In vitro and in vivo expression of α7 integrin and desmin define the primary and secondary myogenic lineages
    • George-Weinstein, M., R.F. Foster, J.V. Gerhart, and S.J. Kaufman. 1993. In vitro and in vivo expression of α7 integrin and desmin define the primary and secondary myogenic lineages. Dev. Biol. 156:209-229.
    • (1993) Dev. Biol. , vol.156 , pp. 209-229
    • George-Weinstein, M.1    Foster, R.F.2    Gerhart, J.V.3    Kaufman, S.J.4
  • 38
    • 0030451425 scopus 로고    scopus 로고
    • Laminins promote the locomotion of skeletal myoblasts via the alpha 7 integrin receptor
    • Yao, C.-C., B.L. Ziober, A.E. Sutherland, D.L. Mendrick, and R.H. Kramer. 1996. Laminins promote the locomotion of skeletal myoblasts via the alpha 7 integrin receptor. J. Cell Sci. 109:3139-3150.
    • (1996) J. Cell Sci. , vol.109 , pp. 3139-3150
    • Yao, C.-C.1    Ziober, B.L.2    Sutherland, A.E.3    Mendrick, D.L.4    Kramer, R.H.5
  • 39
    • 0027247797 scopus 로고
    • A new isoform of the laminin receptor α7β1 is developmentally regulated in skeletal muscle
    • Collo, G., L. Starr, and V. Quaranta. 1993. A new isoform of the laminin receptor α7β1 is developmentally regulated in skeletal muscle. J. Biol. Chem. 268:19019-19024.
    • (1993) J. Biol. Chem. , vol.268 , pp. 19019-19024
    • Collo, G.1    Starr, L.2    Quaranta, V.3
  • 40
    • 0027787640 scopus 로고
    • Expression of α7 integrin cytoplasmic domains during skeletal muscle development: Alternate forms, conformational change, and homologies with serine/ threonine kinases and tyrosine phosphatases
    • Song, W.K., W. Wang, H. Sato, D.A. Biesler, and S.J. Kaufman. 1993. Expression of α7 integrin cytoplasmic domains during skeletal muscle development: alternate forms, conformational change, and homologies with serine/ threonine kinases and tyrosine phosphatases. J. Cell Sci. 106:1139-1152.
    • (1993) J. Cell Sci. , vol.106 , pp. 1139-1152
    • Song, W.K.1    Wang, W.2    Sato, H.3    Biesler, D.A.4    Kaufman, S.J.5
  • 41
    • 0029671374 scopus 로고    scopus 로고
    • β1D integrin displaces the β1A isoform in striated muscles: Localization at junctional structures and signaling potential in nonmuscle cells
    • Belkin, A.M., N.I. Zhidkova, F. Balzac, F. Altruda, D. Tomatis, A. Maier, G. Tarone, V.E. Koteliansky, and K. Burridge. 1996. β1D integrin displaces the β1A isoform in striated muscles: localization at junctional structures and signaling potential in nonmuscle cells. J. Cell Biol. 132:211-226.
    • (1996) J. Cell Biol. , vol.132 , pp. 211-226
    • Belkin, A.M.1    Zhidkova, N.I.2    Balzac, F.3    Altruda, F.4    Tomatis, D.5    Maier, A.6    Tarone, G.7    Koteliansky, V.E.8    Burridge, K.9
  • 42
    • 0029988437 scopus 로고    scopus 로고
    • Synaptic integrins in developing, adult, and mutant muscle: Selective association of α1, α7A, and α7B integrins with the neuromuscular junction
    • Martin, P.T., S.J. Kaufman, R.H. Kramer, and J.R. Sanes. 1996. Synaptic integrins in developing, adult, and mutant muscle: selective association of α1, α7A, and α7B integrins with the neuromuscular junction. Dev. Biol. 174: 125-139.
    • (1996) Dev. Biol. , vol.174 , pp. 125-139
    • Martin, P.T.1    Kaufman, S.J.2    Kramer, R.H.3    Sanes, J.R.4
  • 43
    • 0029124239 scopus 로고
    • Expression of laminin subunits in human fetal skeletal muscle
    • Sewry, C.A., M. Chevallay, and F.M.S. Tomé, 1995. Expression of laminin subunits in human fetal skeletal muscle. Histochem. J. 27:497-504.
    • (1995) Histochem. J. , vol.27 , pp. 497-504
    • Sewry, C.A.1    Chevallay, M.2    Tomé, F.M.S.3
  • 44
    • 0029582766 scopus 로고
    • Expression of laminin isoforms in mouse myogenic cells in vitro and in vivo
    • Schuler, F., and L. Sorokin. 1995, Expression of laminin isoforms in mouse myogenic cells in vitro and in vivo. J. Cell Sci. 108:3795-3805.
    • (1995) J. Cell Sci. , vol.108 , pp. 3795-3805
    • Schuler, F.1    Sorokin, L.2
  • 48
    • 0026739356 scopus 로고
    • An alternative form of the integrin beta1 subunit with variant cytoplasmic domain
    • Languino, L.R., and E. Ruoslahti. 1992. An alternative form of the integrin beta1 subunit with variant cytoplasmic domain. J. Biol Chem. 267:7116-7120.
    • (1992) J. Biol Chem. , vol.267 , pp. 7116-7120
    • Languino, L.R.1    Ruoslahti, E.2
  • 50
    • 0027377154 scopus 로고
    • Human dystroglycan: Skeletal muscle cDNA, genomic structure, origin of tissue specific isoforms and chromosomal localization
    • Ibraghimov-Beskrovnaya, O. A. Milatovich, T. Ozcelik, B. Yang, K. Koepnick, U. Francke, and K.P. Campbell. 1993. Human dystroglycan: skeletal muscle cDNA, genomic structure, origin of tissue specific isoforms and chromosomal localization. Hum. Mol. Genet. 2:1651-1657.
    • (1993) Hum. Mol. Genet. , vol.2 , pp. 1651-1657
    • Ibraghimov-Beskrovnaya1    Milatovich, O.A.2    Ozcelik, T.3    Yang, B.4    Koepnick, K.5    Francke, U.6    Campbell, K.P.7
  • 53
    • 0025753667 scopus 로고
    • Molecular cloning of the cDNa encoding human laminin A chain
    • Haaparanta, T., J. Uitto, E. Ruoslahti, and E. Engvall. 1991. Molecular cloning of the cDNA encoding human laminin A chain. Matrix. 11:151 160.
    • (1991) Matrix. , vol.11 , pp. 151160
    • Haaparanta, T.1    Uitto, J.2    Ruoslahti, E.3    Engvall, E.4
  • 54
    • 0029032660 scopus 로고
    • Structure-function analysis of Bcl-2 protein. Identification of conserved domains important for homodimerization with Bcl-2 and heterodimerization with Bax
    • Hanada, M., C. Aime-Sempe, T. Sato, and J.C. Reed. 1995. Structure-function analysis of Bcl-2 protein. Identification of conserved domains important for homodimerization with Bcl-2 and heterodimerization with Bax. J. Biol. Chem. 270:11962-11969.
    • (1995) J. Biol. Chem. , vol.270 , pp. 11962-11969
    • Hanada, M.1    Aime-Sempe, C.2    Sato, T.3    Reed, J.C.4
  • 55
    • 0025214421 scopus 로고
    • Elevated levels of the α5β1 fibronectin receptor suppress the transformed phenotype of Chinese hamster ovary cells
    • Giancotti, F.G., and E. Ruoslahti. 1990. Elevated levels of the α5β1 fibronectin receptor suppress the transformed phenotype of Chinese hamster ovary cells. Cell. 60:849-859.
    • (1990) Cell , vol.60 , pp. 849-859
    • Giancotti, F.G.1    Ruoslahti, E.2
  • 56
    • 0028983407 scopus 로고
    • The α5β1 integrin supports survival of cells on fibronectin and up-regulates Bcl-2 expression
    • Zhang, Z., K. Vuori, J.C. Reed, and E. Ruoslahti. 1995. The α5β1 integrin supports survival of cells on fibronectin and up-regulates Bcl-2 expression. Proc. Natl. Acad. Sci. USA. 92:6161-6165.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 6161-6165
    • Zhang, Z.1    Vuori, K.2    Reed, J.C.3    Ruoslahti, E.4
  • 57
    • 0020443976 scopus 로고
    • Synthesis of type IV collagen and laminin in cultures of skeletal muscle cells and their assembly on the surface of myotubes
    • Kühl, U., R. Timpl, and K. von der Mark. 1982. Synthesis of type IV collagen and laminin in cultures of skeletal muscle cells and their assembly on the surface of myotubes. Dev. Biol. 93:344-354.
    • (1982) Dev. Biol. , vol.93 , pp. 344-354
    • Kühl, U.1    Timpl, R.2    Von Der Mark, K.3
  • 58
  • 59
    • 0028927484 scopus 로고
    • Suppression of ICE and apoptosis in mammary epithelial cells by extracellular matrix
    • Boudreau, N., C.J. Sympson, Z. Werb, and M.J. Bissell. 1995. Suppression of ICE and apoptosis in mammary epithelial cells by extracellular matrix. Science (Wash. DC). 267:891-893.
    • (1995) Science (Wash. DC) , vol.267 , pp. 891-893
    • Boudreau, N.1    Sympson, C.J.2    Werb, Z.3    Bissell, M.J.4
  • 61
    • 0030458602 scopus 로고    scopus 로고
    • A role for Jun-N-terminal kinase in anoikis; suppression by Bcl-2 and crmA
    • Frisch, S.M., K. Vuori, D. Kelaita, and S. Sicks. 1996. A role for Jun-N-terminal kinase in anoikis; suppression by Bcl-2 and crmA. J. Cell Biol. 135: 1377-1382.
    • (1996) J. Cell Biol. , vol.135 , pp. 1377-1382
    • Frisch, S.M.1    Vuori, K.2    Kelaita, D.3    Sicks, S.4
  • 62
    • 0030584079 scopus 로고    scopus 로고
    • Apoptosis meets signal transduction: Elimination of a BAD influence
    • Gajewski, T.F., and C.B. Thompson. 1996. Apoptosis meets signal transduction: elimination of a BAD influence. Cell. 87:589-592.
    • (1996) Cell , vol.87 , pp. 589-592
    • Gajewski, T.F.1    Thompson, C.B.2
  • 63
    • 0029666420 scopus 로고    scopus 로고
    • β4 integrin is required for hemidesmosome formation, cell adhesion and cell survival
    • Dowling, J., Q.-C. Yu, and E. Fuchs. 1996. β4 integrin is required for hemidesmosome formation, cell adhesion and cell survival. J. Cell Biol. 134: 559-572.
    • (1996) J. Cell Biol. , vol.134 , pp. 559-572
    • Dowling, J.1    Yu, Q.-C.2    Fuchs, E.3
  • 66
    • 0028817970 scopus 로고
    • Visualization of dystrophic muscle fibers in mdx mouse by vital staining with Evans blue: Evidence of apoptosis in dystrophin-deficient muscle
    • Matsuda, R., A. Nishikawa, and H. Tanaka. 1995. Visualization of dystrophic muscle fibers in mdx mouse by vital staining with Evans blue: evidence of apoptosis in dystrophin-deficient muscle. J. Biochem. 118:959-964.
    • (1995) J. Biochem. , vol.118 , pp. 959-964
    • Matsuda, R.1    Nishikawa, A.2    Tanaka, H.3
  • 69
    • 0028863558 scopus 로고
    • Control of integrin expression by extracellular matrix
    • Delcommenne, M., and C.H. Streuli. 1995. Control of integrin expression by extracellular matrix. J. Biol. Chem. 270:26794-26801.
    • (1995) J. Biol. Chem. , vol.270 , pp. 26794-26801
    • Delcommenne, M.1    Streuli, C.H.2
  • 70
    • 0028978225 scopus 로고
    • α3Aβ1 integrin localizes to focal contacts in response to diverse extracellular matrix proteins
    • DiPersio, C.M., S. Shah, and R.O. Hynes. 1995. α3Aβ1 integrin localizes to focal contacts in response to diverse extracellular matrix proteins. J. Cell Sci. 108:2321-2336.
    • (1995) J. Cell Sci. , vol.108 , pp. 2321-2336
    • Dipersio, C.M.1    Shah, S.2    Hynes, R.O.3
  • 72
    • 0029959355 scopus 로고    scopus 로고
    • Intracellular signals direct integrin localization to sites of function in embryonic muscles
    • Martin-Bermudo, M.D., and N.H. Brown. 1996. Intracellular signals direct integrin localization to sites of function in embryonic muscles. J. Cell Biol. 134:217-226.
    • (1996) J. Cell Biol. , vol.134 , pp. 217-226
    • Martin-Bermudo, M.D.1    Brown, N.H.2
  • 73
    • 0029976571 scopus 로고    scopus 로고
    • Structural organization of the human and mouse laminin β2 chain genes, and alternative splicing at the 5′ end of the human transcript
    • Durkin, M.E., M. Gautam, F. Loechel, J.R. Sanes, J.P. Merlie, R. Albrechtsen, and U.M. Wewer. 1996. Structural organization of the human and mouse laminin β2 chain genes, and alternative splicing at the 5′ end of the human transcript. J. Biol. Chem. 271:13407-13416.
    • (1996) J. Biol. Chem. , vol.271 , pp. 13407-13416
    • Durkin, M.E.1    Gautam, M.2    Loechel, F.3    Sanes, J.R.4    Merlie, J.P.5    Albrechtsen, R.6    Wewer, U.M.7
  • 74
    • 0029122801 scopus 로고
    • A synaptic localization domain in the synaptic cleft protein laminin β2 (s-laminin)
    • Martin, P.T., A.J. Ettinger, and J.R. Sanes. 1995. A synaptic localization domain in the synaptic cleft protein laminin β2 (s-laminin). Science (Wash. DC). 269:413-416.
    • (1995) Science (Wash. DC) , vol.269 , pp. 413-416
    • Martin, P.T.1    Ettinger, A.J.2    Sanes, J.R.3
  • 76
    • 0030919488 scopus 로고    scopus 로고
    • The laminin a chains: Expression, developmental transitions, and chromosomal locations of α1-5. identification of heterotrimeric laminins 8-11, and cloning of a novel α3 isoform
    • Miner, J.H., B.L. Patton, S.I. Lentz, D.J. Gilbert, W.D. Snider, N.A. Jenkins, N.G. Copeland, and J.S. Sanes. 1997. The laminin a chains: expression, developmental transitions, and chromosomal locations of α1-5. identification of heterotrimeric laminins 8-11, and 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.S.8
  • 77
    • 0030589587 scopus 로고    scopus 로고
    • Targeted mutations in cell adhesion genes: What have we learned from them?
    • Hynes, R.O. 1996. Targeted mutations in cell adhesion genes: what have we learned from them? Dev. Biol. 180:402-412.
    • (1996) Dev. Biol. , vol.180 , pp. 402-412
    • Hynes, R.O.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.