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Volumn 143, Issue 1, 1998, Pages 253-266

Cre-loxP-mediated inactivation of the α6A integrin splice variant in vivo: Evidence for a specific functional role of α6A in lymphocyte migration but not in heart development

Author keywords

Integrin; Knockout; Laminin receptor; Lymphocyte; Migration

Indexed keywords

INTEGRIN;

EID: 0032487578     PISSN: 00219525     EISSN: None     Source Type: Journal    
DOI: 10.1083/jcb.143.1.253     Document Type: Article
Times cited : (48)

References (73)
  • 1
    • 0025203926 scopus 로고
    • A human integrin β1 subunit with a unique cytoplasmic domain generated by alternative mRNA processing
    • Altruda, F., P. Cervella, G. Tarone, C. Botta, F. Balzac, G. Stefanuto, and L. Silengo. 1990. A human integrin β1 subunit with a unique cytoplasmic domain generated by alternative mRNA processing. Gene. 5:261-266.
    • (1990) Gene. , vol.5 , pp. 261-266
    • Altruda, F.1    Cervella, P.2    Tarone, G.3    Botta, C.4    Balzac, F.5    Stefanuto, G.6    Silengo, L.7
  • 3
    • 0029671074 scopus 로고    scopus 로고
    • Integrin αvβ3 mediates chemotactic and haptotactic motility in human melanoma cells through different signaling pathways
    • Aznavoorian, S., M.L. Stracke, J. Parsons, J. McClanahan, and L.A. Liotta. 1996. Integrin αvβ3 mediates chemotactic and haptotactic motility in human melanoma cells through different signaling pathways. J. Biol. Chem. 271: 3247-3254.
    • (1996) J. Biol. Chem. , vol.271 , pp. 3247-3254
    • Aznavoorian, S.1    Stracke, M.L.2    Parsons, J.3    McClanahan, J.4    Liotta, L.A.5
  • 4
    • 0030579185 scopus 로고    scopus 로고
    • Differentiation of embryonal stem cells into keratinocytes: Comparison of wild-type and β1 integrin-deficient cells
    • Bagutti, C., A.M. Wobus, R. Fässler, and F.M. Watt. 1996. Differentiation of embryonal stem cells into keratinocytes: comparison of wild-type and β1 integrin-deficient cells. Dev. Biol. 179:184-196.
    • (1996) Dev. Biol. , vol.179 , pp. 184-196
    • Bagutti, C.1    Wobus, A.M.2    Fässler, R.3    Watt, F.M.4
  • 5
    • 0030753712 scopus 로고    scopus 로고
    • Laminin-5 and modulation of keratin cytoskeleton arrangement in FG pancreatic carcinoma cells: Involvement of IFAP300 and evidence that laminin-5/cell interactions correlate with a dephosphorylation of α6A integrin
    • Baker, S.E., O. Skalli, R.D. Goldman, and J.C.R. Jones. 1997. Laminin-5 and modulation of keratin cytoskeleton arrangement in FG pancreatic carcinoma cells: involvement of IFAP300 and evidence that laminin-5/cell interactions correlate with a dephosphorylation of α6A integrin. Cell Motil. Cytoskel. 37:271-286.
    • (1997) Cell Motil. Cytoskel. , vol.37 , pp. 271-286
    • Baker, S.E.1    Skalli, O.2    Goldman, R.D.3    Jones, J.C.R.4
  • 6
    • 0032521681 scopus 로고    scopus 로고
    • Knockout and knockin of the β1 exon D define distinct roles for integrin splice variants in heart function and embryonic development
    • Baudoin, C., M.J. Goumans, C. Mummery, and A. Sonnenberg. 1998. Knockout and knockin of the β1 exon D define distinct roles for integrin splice variants in heart function and embryonic development. Genes Dev. 12:1202-1216.
    • (1998) Genes Dev. , vol.12 , pp. 1202-1216
    • Baudoin, C.1    Goumans, M.J.2    Mummery, C.3    Sonnenberg, A.4
  • 7
    • 0025707939 scopus 로고
    • Human platelets and megakaryocytes contain alternately spliced glycoprotein IIb mRNAs
    • Bray, P.F., C.S. Leung, and M.A. Shuman. 1990. Human platelets and megakaryocytes contain alternately spliced glycoprotein IIb mRNAs. J. Biol. Chem. 265:9587-9590.
    • (1990) J. Biol. Chem. , vol.265 , pp. 9587-9590
    • Bray, P.F.1    Leung, C.S.2    Shuman, M.A.3
  • 8
    • 0029149543 scopus 로고
    • Differential distribution of two cytoplasmic variants of the α6β1 integrin laminin receptor in the ventral plasma membrane of embryonic fibroblasts
    • Cattelino, A., R. Longhi, and I. de Curtis. 1995. Differential distribution of two cytoplasmic variants of the α6β1 integrin laminin receptor in the ventral plasma membrane of embryonic fibroblasts. J. Cell Sci. 108:3067-3078.
    • (1995) J. Cell Sci. , vol.108 , pp. 3067-3078
    • Cattelino, A.1    Longhi, R.2    De Curtis, I.3
  • 9
    • 0026596337 scopus 로고
    • Distinct cellular functions mediated by different VLA integrin α subunit cytoplasmic domains
    • Chan, B.M., P.D. Kassner, J.A. Schiro, H.R. Byers, T.S. Kupper, and M.E. Hemler. 1992. Distinct cellular functions mediated by different VLA integrin α subunit cytoplasmic domains. Cell. 68:1051-1060.
    • (1992) Cell , vol.68 , pp. 1051-1060
    • Chan, B.M.1    Kassner, P.D.2    Schiro, J.A.3    Byers, H.R.4    Kupper, T.S.5    Hemler, M.E.6
  • 10
    • 0027321020 scopus 로고
    • Expression of merosin in the thymus and its interaction with thymocytes
    • Chang, A.C., S. Wadsworth, and J.E. Coligan. 1993. Expression of merosin in the thymus and its interaction with thymocytes. J. Immunol. 151:1789-1801.
    • (1993) J. Immunol. , vol.151 , pp. 1789-1801
    • Chang, A.C.1    Wadsworth, S.2    Coligan, J.E.3
  • 11
    • 0028983544 scopus 로고
    • α3β1 and α6β1 integrins mediate laminin/merosin binding and function as costimulatory molecules for human thymocyte proliferation
    • Chang, A.C., D.R. Salomon, S. Wadsworth, M.J.P. Hong, C.F. Mojcik, S. Otto, E.M. Shevach, and J.E. Coligan. 1995. α3β1 and α6β1 integrins mediate laminin/merosin binding and function as costimulatory molecules for human thymocyte proliferation. J. Immunol. 154:500-510.
    • (1995) J. Immunol. , vol.154 , pp. 500-510
    • Chang, A.C.1    Salomon, D.R.2    Wadsworth, S.3    Hong, M.J.P.4    Mojcik, C.F.5    Otto, S.6    Shevach, E.M.7    Coligan, J.E.8
  • 12
    • 0027662223 scopus 로고
    • Extracellular matrix gene expression by human bone marrow fibroblasts
    • Chichester, C.O., M. Fernandez, and J.J. Minguell. 1993. Extracellular matrix gene expression by human bone marrow fibroblasts. Cell Adhes. Commun. 1:93-99.
    • (1993) Cell Adhes. Commun. , vol.1 , pp. 93-99
    • Chichester, C.O.1    Fernandez, M.2    Minguell, J.J.3
  • 13
    • 0028987936 scopus 로고
    • Integrins and signal transduction pathways: The road taken
    • Clark, E.A., and J.S. Brugge. 1995. Integrins and signal transduction pathways: the road taken. Science. 268:233-239.
    • (1995) Science , vol.268 , pp. 233-239
    • Clark, E.A.1    Brugge, J.S.2
  • 14
    • 0028339023 scopus 로고
    • A novel structural variant of the human β4 integrin cDNA
    • Clarke, A.S., M.M. Lotz, and A.M. Mercurio. 1994. A novel structural variant of the human β4 integrin cDNA. Cell Adhes. Commun. 2:1-6.
    • (1994) Cell Adhes. Commun. , vol.2 , pp. 1-6
    • Clarke, A.S.1    Lotz, M.M.2    Mercurio, A.M.3
  • 15
    • 0028984447 scopus 로고
    • Gradient of integrin α6A distribution in the myocardium during early heart development
    • Collo, G., S.Z. Domanico, G. Klier, and V. Quaranta. 1995. Gradient of integrin α6A distribution in the myocardium during early heart development. Cell Adhes. Commun. 3:101-113.
    • (1995) Cell Adhes. Commun. , vol.3 , pp. 101-113
    • Collo, G.1    Domanico, S.Z.2    Klier, G.3    Quaranta, V.4
  • 16
    • 0026061509 scopus 로고
    • The major laminin receptor of mouse embryonic stem cells is a novel isoform of the α6β1 integrin
    • Cooper, H.M., R.N. Tamura, and V. Quaranta. 1991. The major laminin receptor of mouse embryonic stem cells is a novel isoform of the α6β1 integrin. J. Cell Biol. 115:843-850.
    • (1991) J. Cell Biol. , vol.115 , pp. 843-850
    • Cooper, H.M.1    Tamura, R.N.2    Quaranta, V.3
  • 17
    • 0001882760 scopus 로고    scopus 로고
    • Laminin isoforms and their integrin receptors
    • M.A. Horton, editor, CRC Press, Boca Raton, FL
    • Delwel, G.O., and A. Sonnenberg. 1996. Laminin isoforms and their integrin receptors. In Adhesion Receptors as Therapeutic Targets. M.A. Horton, editor, CRC Press, Boca Raton, FL. 9-36.
    • (1996) Adhesion Receptors as Therapeutic Targets , pp. 9-36
    • Delwel, G.O.1    Sonnenberg, A.2
  • 18
    • 0027371830 scopus 로고
    • Expression and function of the cytoplasmic variants of the integrin α6 subunit in transfected K562 cells. Activation-dependent adhesion and interaction with isoforms of laminin
    • Delwel, G.O., F. Hogervorst, I. Kuikman, M. Paulsson, R. Timpl, and A. Sonnenberg. 1993. Expression and function of the cytoplasmic variants of the integrin α6 subunit in transfected K562 cells. Activation-dependent adhesion and interaction with isoforms of laminin. J. Biol. Chem. 268:25865-25875.
    • (1993) J. Biol. Chem. , vol.268 , pp. 25865-25875
    • Delwel, G.O.1    Hogervorst, F.2    Kuikman, I.3    Paulsson, M.4    Timpl, R.5    Sonnenberg, A.6
  • 19
    • 0029161166 scopus 로고
    • An alternative spliced exon in the extracellular domain of the human α6 integrin subunit. Functional analysis of the α6 integrin variants
    • Delwel, G.O., I. Kuikman, and A. Sonnenberg. 1995. An alternative spliced exon in the extracellular domain of the human α6 integrin subunit. Functional analysis of the α6 integrin variants. Cell Adhes. Commun. 3:143-161.
    • (1995) Cell Adhes. Commun. , vol.3 , pp. 143-161
    • Delwel, G.O.1    Kuikman, I.2    Sonnenberg, A.3
  • 21
    • 0030730986 scopus 로고    scopus 로고
    • Integrin α6Aβ1 induces CD81-dependent cell motility without engaging the extracellular matrix migration substrate
    • Domanico, S.Z., A.J. Pelletier, W.L. Havran, and V. Quaranta. 1997. Integrin α6Aβ1 induces CD81-dependent cell motility without engaging the extracellular matrix migration substrate. Mol. Biol. Cell. 8:2253-2265.
    • (1997) Mol. Biol. Cell. , vol.8 , pp. 2253-2265
    • Domanico, S.Z.1    Pelletier, A.J.2    Havran, W.L.3    Quaranta, V.4
  • 22
    • 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
  • 23
    • 0023907048 scopus 로고
    • Identification of atrial natriuretic factor within ventricular tissue in hamsters and humans with congestive heart failure
    • Edwards, B.S., D.M. Ackermann, M.E. Lee, G.S. Reeder, L.E. Wold, and J.C. Burnett. 1988. Identification of atrial natriuretic factor within ventricular tissue in hamsters and humans with congestive heart failure. J. Clin. Invest. 81: 82-86.
    • (1988) J. Clin. Invest. , vol.81 , pp. 82-86
    • Edwards, B.S.1    Ackermann, D.M.2    Lee, M.E.3    Reeder, G.S.4    Wold, L.E.5    Burnett, J.C.6
  • 24
    • 0030664296 scopus 로고    scopus 로고
    • Parsing the heart: Genetic modules for organ assembly
    • Fishman, M.C., and E.N. Olson. 1997. Parsing the heart: genetic modules for organ assembly. Cell. 91:153-156.
    • (1997) Cell , vol.91 , pp. 153-156
    • Fishman, M.C.1    Olson, E.N.2
  • 25
    • 0028670553 scopus 로고
    • Quantitative measurement of α6β1 and α6β4 integrin internalization under cross-linking conditions: A possible role for α6 cytoplasmic domains
    • Gaietta, G., T.E.K. Redelmeier, M.R. Jackson, R.N. Tamura, and V. Quaranta. 1994. Quantitative measurement of α6β1 and α6β4 integrin internalization under cross-linking conditions: a possible role for α6 cytoplasmic domains. J. Cell Sci. 107:3339-3349.
    • (1994) J. Cell Sci. , vol.107 , pp. 3339-3349
    • Gaietta, G.1    Redelmeier, T.E.K.2    Jackson, M.R.3    Tamura, R.N.4    Quaranta, V.5
  • 27
    • 0026649765 scopus 로고
    • Identification and distribution of the costimulatory receptor CD28 in the mouse
    • Gross, J.A., E. Callas, and J.P. Allison. 1992. Identification and distribution of the costimulatory receptor CD28 in the mouse. J. Immunol. 149:380-388.
    • (1992) J. Immunol. , vol.149 , pp. 380-388
    • Gross, J.A.1    Callas, E.2    Allison, J.P.3
  • 28
    • 0030028984 scopus 로고    scopus 로고
    • Keratinocyte growth factor is required for hair development but not for wound healing
    • Guo, L., L. Degenstein, and E. Fuchs. 1996. Keratinocyte growth factor is required for hair development but not for wound healing. Genes Dev. 10:165-175.
    • (1996) Genes Dev. , vol.10 , pp. 165-175
    • Guo, L.1    Degenstein, L.2    Fuchs, E.3
  • 29
    • 0002637629 scopus 로고
    • 2+
    • I. Leigh and F. Watt, editors. Cambridge University Press, Cambridge, UK
    • 2+. In Keratinocyte Methods. I. Leigh and F. Watt, editors. Cambridge University Press, Cambridge, UK. 21-23.
    • (1994) Keratinocyte Methods , pp. 21-23
    • Hennings, H.1
  • 31
    • 0025117579 scopus 로고
    • Cloning and sequence analysis of β4 cDNA: An integrin subunit that contains a unique 118 kd cytoplasmic domain
    • Hogervorst, F., I. Kuikman, A.E.G.K. von dem Borne, and A. Sonnenberg. 1990. Cloning and sequence analysis of β4 cDNA: an integrin subunit that contains a unique 118 kd cytoplasmic domain. EMBO (Eur. Mol. Biol. Organ.) J. 9:765-770.
    • (1990) EMBO (Eur. Mol. Biol. Organ.) J. , vol.9 , pp. 765-770
    • Hogervorst, F.1    Kuikman, I.2    Von Dem Borne, A.E.G.K.3    Sonnenberg, A.4
  • 32
    • 0025908468 scopus 로고
    • Molecular cloning of the human α6 integrin subunit. Alternative splicing of α6 mRNA and chromosomal localization of the α6 and β4 genes
    • Hogervorst, F., I. Kuikman, A.G. van Kessel, and A. Sonnenberg. 1991. Molecular cloning of the human α6 integrin subunit. Alternative splicing of α6 mRNA and chromosomal localization of the α6 and β4 genes. Eur. J. Biochem. 199:425-433.
    • (1991) Eur. J. Biochem. , vol.199 , pp. 425-433
    • Hogervorst, F.1    Kuikman, I.2    Van Kessel, A.G.3    Sonnenberg, A.4
  • 33
    • 0027301230 scopus 로고
    • The role of phosphorylation in activation of the α6Aβ1 laminin receptor
    • Hogervorst, F., I. Kuikman, E. Noteboom, and A. Sonnenberg. 1993a. The role of phosphorylation in activation of the α6Aβ1 laminin receptor. J. Biol. Chem. 268:18427-18430.
    • (1993) J. Biol. Chem. , vol.268 , pp. 18427-18430
    • Hogervorst, F.1    Kuikman, I.2    Noteboom, E.3    Sonnenberg, A.4
  • 35
    • 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
  • 37
    • 0022626419 scopus 로고
    • Tumor antigen on benign adenomas and on murine lung carcinomas quantitated by a two-site monoclonal antibody assay
    • Kennel, S.J., L.J. Foote, and K.M. Flynn. 1986. Tumor antigen on benign adenomas and on murine lung carcinomas quantitated by a two-site monoclonal antibody assay. Cancer Res. 46:707-712.
    • (1986) Cancer Res. , vol.46 , pp. 707-712
    • Kennel, S.J.1    Foote, L.J.2    Flynn, K.M.3
  • 39
    • 0025802949 scopus 로고
    • Lymphocyte traffic is modified in vivo by anti-laminin antibody
    • Kupiec-Weglinski, J.W., and M. De Sousa. 1991. Lymphocyte traffic is modified in vivo by anti-laminin antibody. Immunology. 72:312-313.
    • (1991) Immunology , vol.72 , pp. 312-313
    • Kupiec-Weglinski, J.W.1    De Sousa, M.2
  • 40
    • 0026334607 scopus 로고
    • Surface relocation of α6β4 integrins and assembly of hemidesmosomes in an in vitro model of wound healing
    • Kurpakus, M.A., V. Quaranta, and J.C.R. Jones. 1991. Surface relocation of α6β4 integrins and assembly of hemidesmosomes in an in vitro model of wound healing. J. Cell Biol. 115:1737-1750.
    • (1991) J. Cell Biol. , vol.115 , pp. 1737-1750
    • Kurpakus, M.A.1    Quaranta, V.2    Jones, J.C.R.3
  • 41
    • 0026739356 scopus 로고
    • An alternative form of the integrin β1 subunit with a variant cytoplasmic domain
    • Languino, L.R., and E. Ruoslahti. 1992. An alternative form of the integrin β1 subunit with a 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
  • 45
    • 0030000184 scopus 로고    scopus 로고
    • Expressions of very late antigen-6 and vitronectin receptor, and their interactions to laminin and vitronectin during tonsillar B-cell activation
    • Ohguro, S., and H. Tsubota. 1996. Expressions of very late antigen-6 and vitronectin receptor, and their interactions to laminin and vitronectin during tonsillar B-cell activation. Auris Nasus Larynx. 23:111-120.
    • (1996) Auris Nasus Larynx , vol.23 , pp. 111-120
    • Ohguro, S.1    Tsubota, H.2
  • 46
    • 0031026454 scopus 로고    scopus 로고
    • Costimulation of T cell activation by integrin-associated protein (CD47) is an adhesion-dependent, CD28-independent signaling pathway
    • Reinhold, M.I., F.P. Lindberg, G.J. Kersh, P.M. Allen, and E.J. Brown. 1997. Costimulation of T cell activation by integrin-associated protein (CD47) is an adhesion-dependent, CD28-independent signaling pathway. J. Exp. Med. 185:1-11.
    • (1997) J. Exp. Med. , vol.185 , pp. 1-11
    • Reinhold, M.I.1    Lindberg, F.P.2    Kersh, G.J.3    Allen, P.M.4    Brown, E.J.5
  • 47
    • 0028979458 scopus 로고
    • α6 integrins participate in pro-T cell homing to the thymus
    • Ruiz, P., M.V. Wiles, and B.A. Imhof. 1995. α6 integrins participate in pro-T cell homing to the thymus. Eur. J. Immunol. 25:2034-2041.
    • (1995) Eur. J. Immunol. , vol.25 , pp. 2034-2041
    • Ruiz, P.1    Wiles, M.V.2    Imhof, B.A.3
  • 48
    • 0028984244 scopus 로고
    • Integrin receptor α6β1 is localized at specific sites of cell-to-cell contact in rat seminiferous epithelium
    • Salanova, M., M. Stefanini, I. de Curtis, and F. Palombi. 1995. Integrin receptor α6β1 is localized at specific sites of cell-to-cell contact in rat seminiferous epithelium. Biol. Reprod. 52:79-87.
    • (1995) Biol. Reprod. , vol.52 , pp. 79-87
    • Salanova, M.1    Stefanini, M.2    De Curtis, I.3    Palombi, F.4
  • 49
    • 0029664439 scopus 로고    scopus 로고
    • Integrin α subunit ratios, cytoplasmic domains, and growth factor synergy regulate muscle proliferation and differentiation
    • Sastry, S., M. Lakonishok, D.A. Thomas, J. Muschler, and A.F. Horwitz. 1996. Integrin α 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.1    Lakonishok, M.2    Thomas, D.A.3    Muschler, J.4    Horwitz, A.F.5
  • 50
    • 0024041732 scopus 로고
    • Site-specific DNA recombination in mammalian cells by the Cre recombinase of bacteriophage P1
    • Sauer, B., and N. Henderson. 1988. Site-specific DNA recombination in mammalian cells by the Cre recombinase of bacteriophage P1. Proc. Natl. Acad. Sci. USA. 85:5166-5170.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 5166-5170
    • Sauer, B.1    Henderson, N.2
  • 51
    • 0027332373 scopus 로고
    • Regulation of α6β1 integrin laminin receptor function by the cytoplasmic domain of the α6 subunit
    • Shaw, L.M., and A.M. Mercurio. 1993. Regulation of α6β1 integrin laminin receptor function by the cytoplasmic domain of the α6 subunit. J. Cell Biol. 123:1017-1025.
    • (1993) J. Cell Biol. , vol.123 , pp. 1017-1025
    • Shaw, L.M.1    Mercurio, A.M.2
  • 52
    • 0028356999 scopus 로고
    • Regulation of cellular interactions with laminin by integrin cytoplasmic domains: The A and B structural variants of the α6β1 integrin differentially modulate the adhesive strength, morphology and migration of macrophages
    • Shaw, L.M., and A.M. Mercurio. 1994. Regulation of cellular interactions with laminin by integrin cytoplasmic domains: the A and B structural variants of the α6β1 integrin differentially modulate the adhesive strength, morphology and migration of macrophages. Mol. Biol. Cell. 5:679-690.
    • (1994) Mol. Biol. Cell. , vol.5 , pp. 679-690
    • Shaw, L.M.1    Mercurio, A.M.2
  • 53
    • 0027258613 scopus 로고
    • Inside-out integrin signaling in macrophages. Analysis of the role of the α6Aβ1 and α6B1 integrin variants in laminin adhesion by cDNA expression in an α6 integrin-deficient macrophage cell line
    • Shaw, L.M., M.M. Lotz, and A.M. Mercurio. 1993. Inside-out integrin signaling in macrophages. Analysis of the role of the α6Aβ1 and α6B1 integrin variants in laminin adhesion by cDNA expression in an α6 integrin-deficient macrophage cell line. J. Biol. Chem. 268:11401-11408.
    • (1993) J. Biol. Chem. , vol.268 , pp. 11401-11408
    • Shaw, L.M.1    Lotz, M.M.2    Mercurio, A.M.3
  • 54
    • 0028970786 scopus 로고
    • The α6Aβ1 and α6Bβ1 integrin variants signal differences in the tyrosine phosphorylation of paxillin and other proteins
    • Shaw, L.M., C.E. Turner, and A.M. Mercurio. 1995. The α6Aβ1 and α6Bβ1 integrin variants signal differences in the tyrosine phosphorylation of paxillin and other proteins. J. Biol. Chem. 270:23648-23652.
    • (1995) J. Biol. Chem. , vol.270 , pp. 23648-23652
    • Shaw, L.M.1    Turner, C.E.2    Mercurio, A.M.3
  • 55
    • 0025307161 scopus 로고    scopus 로고
    • Costimulation of proliferative responses of resting CD4+ T cells by the interaction of VLA-4 and VLA-5 with fibronectin or VLA-6 with laminin
    • Shimizu, Y., G.A. van Seventer, K.J. Horgan, and S. Shaw. 1999a. Costimulation of proliferative responses of resting CD4+ T cells by the interaction of VLA-4 and VLA-5 with fibronectin or VLA-6 with laminin. J. Immunol. 145:59-67.
    • (1999) J. Immunol. , vol.145 , pp. 59-67
    • Shimizu, Y.1    Van Seventer, G.A.2    Horgan, K.J.3    Shaw, S.4
  • 56
    • 0025363922 scopus 로고
    • Regulated expression and binding of three VLA (β1) integrin receptors on T cells
    • Shimizu, Y., G.A. van Seventer, K.J. Horgan, and S. Shaw. 1990b. Regulated expression and binding of three VLA (β1) integrin receptors on T cells. Nature. 345:250-253.
    • (1990) Nature , vol.345 , pp. 250-253
    • Shimizu, Y.1    Van Seventer, G.A.2    Horgan, K.J.3    Shaw, S.4
  • 57
    • 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. Bielser, 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    Bielser, D.A.4    Kaufman, S.J.5
  • 58
    • 0023664709 scopus 로고
    • A complex of platelet glycoproteins Ic and IIa identified by a rat monoclonal antibody
    • Sonnenberg, A., H. Janssen, F. Hogervorst, J. Calafat, and J. Hilgers. 1987. A complex of platelet glycoproteins Ic and IIa identified by a rat monoclonal antibody. J. Biol. Chem. 262:10376-10383.
    • (1987) J. Biol. Chem. , vol.262 , pp. 10376-10383
    • Sonnenberg, A.1    Janssen, H.2    Hogervorst, F.3    Calafat, J.4    Hilgers, J.5
  • 59
    • 0027982876 scopus 로고
    • Traffic signals for lymphocyte recirculation and leukocyte emigration: The multistep paradigm
    • Springer, T.A. 1994. Traffic signals for lymphocyte recirculation and leukocyte emigration: the multistep paradigm. Cell. 76:301-314.
    • (1994) Cell , vol.76 , pp. 301-314
    • Springer, T.A.1
  • 60
    • 0025020280 scopus 로고
    • Amino acid sequence of a novel integrin β4 subunit and primary expression of the mRNA in epithelial cells
    • Suzuki, S., and Y. Naitoh. 1990. Amino acid sequence of a novel integrin β4 subunit and primary expression of the mRNA in epithelial cells. EMBO (Eur. Mol. Biol. Organ.) J. 9:757-763.
    • (1990) EMBO (Eur. Mol. Biol. Organ.) J. , vol.9 , pp. 757-763
    • Suzuki, S.1    Naitoh, Y.2
  • 61
    • 0025940742 scopus 로고
    • Molecular cloning and expression of the cDNA for α3 subunit of human α3β1 (VLA-3), an integrin receptor for fibronectin, laminin, and collagen
    • Takada, Y., E. Murphy, P. Pil, C. Chen, M.H. Ginsberg, and M.E. Hemler. 1991. Molecular cloning and expression of the cDNA for α3 subunit of human α3β1 (VLA-3), an integrin receptor for fibronectin, laminin, and collagen. J. Cell Biol. 115:257-266.
    • (1991) J. Cell Biol. , vol.115 , pp. 257-266
    • Takada, Y.1    Murphy, E.2    Pil, P.3    Chen, C.4    Ginsberg, M.H.5    Hemler, M.E.6
  • 64
    • 0028828282 scopus 로고
    • Expression patterns of laminin receptor splice variants α6Aβ1 and α6Bβ1 suggest different roles in mouse development
    • Thorsteinsdóttir, S., B.A.J. Roelen, E. Freund, A.C. Gaspar, A. Sonnenberg, and C.L. Mummery. 1995. Expression patterns of laminin receptor splice variants α6Aβ1 and α6Bβ1 suggest different roles in mouse development. Dev. Dyn. 204:240-258.
    • (1995) Dev. Dyn. , vol.204 , pp. 240-258
    • Thorsteinsdóttir, S.1    Roelen, B.A.J.2    Freund, E.3    Gaspar, A.C.4    Sonnenberg, A.5    Mummery, C.L.6
  • 65
    • 0029814512 scopus 로고    scopus 로고
    • Dot-like focal contacts in adherent eosinophils, their redistribution into peripheral belts, and correlated effects on cell migration and protected zone formation
    • Tourkin, A., M. Bonner, E. Mantrova, E.C. LeRoy, and S. Hoffman. 1996. Dot-like focal contacts in adherent eosinophils, their redistribution into peripheral belts, and correlated effects on cell migration and protected zone formation. J. Cell Sci. 109:2169-2177.
    • (1996) J. Cell Sci. , vol.109 , pp. 2169-2177
    • Tourkin, A.1    Bonner, M.2    Mantrova, E.3    LeRoy, E.C.4    Hoffman, S.5
  • 66
    • 0028984183 scopus 로고
    • A novel β1 integrin isoform produced by alternative splicing: Unique expression in cardiac and skeletal muscles
    • van der Flier, A., I. Kuikman, C. Baudoin, R. van der Neut, and A. Sonnenberg. 1995. A novel β1 integrin isoform produced by alternative splicing: unique expression in cardiac and skeletal muscles. FEBS Lett. 369:340-344.
    • (1995) FEBS Lett. , vol.369 , pp. 340-344
    • Van Der Flier, A.1    Kuikman, I.2    Baudoin, C.3    Van Der Neut, R.4    Sonnenberg, A.5
  • 69
    • 0031587965 scopus 로고    scopus 로고
    • The unique cytoplasmic domain of the human integrin variant β4E is produced by partial retention of intronic sequences
    • van Leusden, M,R., I. Kuikman, and A. Sonnenberg. 1997. The unique cytoplasmic domain of the human integrin variant β4E is produced by partial retention of intronic sequences. Biochem. Biophys. Res. Commun. 235:826-830.
    • (1997) Biochem. Biophys. Res. Commun. , vol.235 , pp. 826-830
    • Van Leusden, M.R.1    Kuikman, I.2    Sonnenberg, A.3
  • 70
    • 0029969536 scopus 로고    scopus 로고
    • VLA-β1 integrin subunit-specific monoclonal antibodies MB1.1 and MB1.2: Binding to epitopes is not dependent on thymocyte development or regulated by phorbolester and divalent cations
    • von Ballestrem, C.G., S. Uniyal, J.I. McCormick, T. Chau, B. Singh, and B.M.C. Chan. 1996. VLA-β1 integrin subunit-specific monoclonal antibodies MB1.1 and MB1.2: binding to epitopes is not dependent on thymocyte development or regulated by phorbolester and divalent cations. Hybridoma. 15:125-132.
    • (1996) Hybridoma , vol.15 , pp. 125-132
    • Von Ballestrem, C.G.1    Uniyal, S.2    McCormick, J.I.3    Chau, T.4    Singh, B.5    Chan, B.M.C.6
  • 71
    • 0030451425 scopus 로고    scopus 로고
    • Laminins promote the locomotion of skeletal myoblasts via the α7 integrin receptor
    • Yao, C.C., B.L. Liober, A.E. Sutherland, D.L. Mendrick, and R.H. Kramer. 1996. Laminins promote the locomotion of skeletal myoblasts via the α7 integrin receptor. J. Cell Sci. 109:3139-3150.
    • (1996) J. Cell Sci. , vol.109 , pp. 3139-3150
    • Yao, C.C.1    Liober, B.L.2    Sutherland, A.E.3    Mendrick, D.L.4    Kramer, R.H.5
  • 72
    • 0028978745 scopus 로고
    • Novel isoform of β1 integrin expressed in skeletal and cardiac muscles
    • Zhidkova, N.I., A.M. Belkin, and R. Mayne. 1995. Novel isoform of β1 integrin expressed in skeletal and cardiac muscles. Biochem. Biophys. Res. Commun. 214:279-285.
    • (1995) Biochem. Biophys. Res. Commun. , vol.214 , pp. 279-285
    • Zhidkova, N.I.1    Belkin, A.M.2    Mayne, R.3
  • 73
    • 0027454265 scopus 로고
    • Alternative extracellular and cytoplasmic domains of the integrin α7 subunit are differentially expressed during development
    • Ziober, B.L., M.P. Vu, N. Waleb, J. Crawford, C.S. Lin, and R.H. Kramer. 1993. Alternative extracellular and cytoplasmic domains of the integrin α7 subunit are differentially expressed during development. J. Biol. Chem. 268:26773-26783.
    • (1993) J. Biol. Chem. , vol.268 , pp. 26773-26783
    • Ziober, B.L.1    Vu, M.P.2    Waleb, N.3    Crawford, J.4    Lin, C.S.5    Kramer, R.H.6


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