메뉴 건너뛰기




Volumn 138, Issue 5, 2005, Pages 539-552

Regulation of cell adhesion and type VII collagen binding by the β3 chain short arm of laminin-5: Effect of its proteolytic cleavage

Author keywords

Cell adhesion; Cell migration; Laminin 3 chain; Laminin 5; Proteolytic cleavage

Indexed keywords

CELL RECEPTOR; COLLAGEN TYPE 7; EPIDERMAL GROWTH FACTOR; INTEGRIN; KALININ; MUTANT PROTEIN; PROTEINASE; RECOMBINANT PROTEIN;

EID: 30344450039     PISSN: 0021924X     EISSN: None     Source Type: Journal    
DOI: 10.1093/jb/mvi153     Document Type: Article
Times cited : (28)

References (40)
  • 1
    • 0034075654 scopus 로고    scopus 로고
    • Form and function: The laminin family of heterotrimers
    • Colognato, H. and Yurchenco, P.D. (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.D.2
  • 2
    • 0032910126 scopus 로고    scopus 로고
    • Laminins of the dermo-epidermal junction
    • Aumailley, M. and Rousselle, P. (1999) Laminins of the dermo-epidermal junction. Matrix Biol. 18, 19-28
    • (1999) Matrix Biol. , vol.18 , pp. 19-28
    • Aumailley, M.1    Rousselle, P.2
  • 3
    • 0030919488 scopus 로고    scopus 로고
    • The laminin α 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., 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, 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.R.8
  • 4
    • 0034698047 scopus 로고    scopus 로고
    • Structural requirement of carboxyl-terminal globular domains of laminin α3 chain for promotion of rapid cell adhesion and migration by laminin-5
    • Hirosaki, T., Mizushima, H., Tsubota, Y., Moriyama, K., and Miyazaki, K. (2000) Structural requirement of carboxyl-terminal globular domains of laminin α3 chain for promotion of rapid cell adhesion and migration by laminin-5. J. Biol. Chem. 275, 22495-22502
    • (2000) J. Biol. Chem. , vol.275 , pp. 22495-22502
    • Hirosaki, T.1    Mizushima, H.2    Tsubota, Y.3    Moriyama, K.4    Miyazaki, K.5
  • 5
    • 0037441482 scopus 로고    scopus 로고
    • Differential regulation of cellular adhesion and migration by recombinant laminin-5 forms with partial deletion or mutation within the G3 domain of α3 chain
    • Kariya, Y., Tsubota, Y., Hirosaki, T., Mizushima, H., Puzon-McLaughlin, W., Takada, Y., and Miyazaki, K. (2003) Differential regulation of cellular adhesion and migration by recombinant laminin-5 forms with partial deletion or mutation within the G3 domain of α3 chain. J. Cell Biochem. 88, 506-520
    • (2003) J. Cell Biochem. , vol.88 , pp. 506-520
    • Kariya, Y.1    Tsubota, Y.2    Hirosaki, T.3    Mizushima, H.4    Puzon-McLaughlin, W.5    Takada, Y.6    Miyazaki, K.7
  • 6
    • 0026629850 scopus 로고
    • The dermal-epidermal junction of human skin contains a novel laminin variant
    • Marinkovich, M.P., Lunstrum, G.P., Keene, D.R., and Burgeson, R.E. (1992) The dermal-epidermal junction of human skin contains a novel laminin variant. J. Cell Biol. 119, 695-703
    • (1992) J. Cell Biol. , vol.119 , pp. 695-703
    • Marinkovich, M.P.1    Lunstrum, G.P.2    Keene, D.R.3    Burgeson, R.E.4
  • 8
    • 0025887362 scopus 로고
    • Epiligrin, a new cell adhesion ligand for integrin α3β1 in epithelial basement membranes
    • Carter, W.G., Ryan, M.C., and Gahr, P.J. (1991) Epiligrin, a new cell adhesion ligand for integrin α3β1 in epithelial basement membranes. Cell 65, 599-610
    • (1991) Cell , vol.65 , pp. 599-610
    • Carter, W.G.1    Ryan, M.C.2    Gahr, P.J.3
  • 10
    • 0030987772 scopus 로고    scopus 로고
    • Interactions of the amino-terminal noncollagenous (NC1) domain of type VII collagen with extracellular matrix components. A potential role in epidermal-dermal adherence in human skin
    • Chen, M., Marinkovich, M.P., Veis, A., Cai, X., Rao, C.N., O'Toole, E.A., and Woodley, D.T. (1997) Interactions of the amino-terminal noncollagenous (NC1) domain of type VII collagen with extracellular matrix components. A potential role in epidermal-dermal adherence in human skin. J. Biol. Chem. 272, 14516-14522
    • (1997) J. Biol. Chem. , vol.272 , pp. 14516-14522
    • Chen, M.1    Marinkovich, M.P.2    Veis, A.3    Cai, X.4    Rao, C.N.5    O'Toole, E.A.6    Woodley, D.T.7
  • 11
    • 0029864911 scopus 로고    scopus 로고
    • Human amnion contains a novel laminin variant, laminin 7, which like laminin 6, covalently associates with laminin 5 to promote stable epithelial-stromal attachment
    • Champliaud, M.F., Lunstrum, G.P., Rousselle, P., Nishiyama, T., Keene, D.R., and Burgeson, R.E. (1996) Human amnion contains a novel laminin variant, laminin 7, which like laminin 6, covalently associates with laminin 5 to promote stable epithelial-stromal attachment. J. Cell Biol. 132, 1189-1198
    • (1996) J. Cell Biol. , vol.132 , pp. 1189-1198
    • Champliaud, M.F.1    Lunstrum, G.P.2    Rousselle, P.3    Nishiyama, T.4    Keene, D.R.5    Burgeson, R.E.6
  • 12
    • 0032962217 scopus 로고    scopus 로고
    • Mutation analysis and molecular genetics of epidermolysis bullosa
    • Pulkkinen, L. and Uitto, J. (1999) Mutation analysis and molecular genetics of epidermolysis bullosa. Matrix Biol. 18, 29-42
    • (1999) Matrix Biol. , vol.18 , pp. 29-42
    • Pulkkinen, L.1    Uitto, J.2
  • 13
    • 0033553883 scopus 로고    scopus 로고
    • Targeted disruption of the LAMA3 gene in mice reveals abnormalities in survival and late stage differentiation of epithelial cells
    • Ryan, M.C., Lee, K., Miyashita, Y., and Carter, W.G. (1999) Targeted disruption of the LAMA3 gene in mice reveals abnormalities in survival and late stage differentiation of epithelial cells. J. Cell Biol. 145, 1309-1323
    • (1999) J. Cell Biol. , vol.145 , pp. 1309-1323
    • Ryan, M.C.1    Lee, K.2    Miyashita, Y.3    Carter, W.G.4
  • 15
    • 0027938248 scopus 로고
    • Marked stimulation of cell adhesion and motility by ladsin, a laminin-like scatter factor
    • Kikkawa, Y., Umeda, M., and Miyazaki, K. (1994) Marked stimulation of cell adhesion and motility by ladsin, a laminin-like scatter factor. J. Biochem. 116, 862-869
    • (1994) J. Biochem. , vol.116 , pp. 862-869
    • Kikkawa, Y.1    Umeda, M.2    Miyazaki, K.3
  • 16
    • 0028294842 scopus 로고
    • Kalinin is more efficient than laminin in promoting adhesion of primary keratinocytes and some other epithelial cells and has a different requirement for integrin receptors
    • Rousselle, P. and Aumailley, M. (1994) Kalinin is more efficient than laminin in promoting adhesion of primary keratinocytes and some other epithelial cells and has a different requirement for integrin receptors. J. Cell Biol. 125, 205-214
    • (1994) J. Cell Biol. , vol.125 , pp. 205-214
    • Rousselle, P.1    Aumailley, M.2
  • 17
    • 0028085840 scopus 로고
    • Cloning of the LamA3 gene encoding the α3 chain of the adhesive ligand epiligrin. Expression in wound repair
    • Ryan, M.C., Tizard, R., Van Devanter, D.R., Carter, and W.G. (1994) Cloning of the LamA3 gene encoding the α3 chain of the adhesive ligand epiligrin. Expression in wound repair. J. Biol. Chem. 269, 22779-22787
    • (1994) J. Biol. Chem. , vol.269 , pp. 22779-22787
    • Ryan, M.C.1    Tizard, R.2    Van Devanter, D.R.3    Carter, W.G.4
  • 18
    • 0033813105 scopus 로고    scopus 로고
    • Deposition of laminin 5 in epidermal wounds regulates integrin signaling and adhesion
    • Nguyen, B.P., Ryan, M.C., Gil, S.G., and Carter, W.G. (2000) Deposition of laminin 5 in epidermal wounds regulates integrin signaling and adhesion. Curr. Opin. Cell Biol. 12, 554-562
    • (2000) Curr. Opin. Cell Biol. , vol.12 , pp. 554-562
    • Nguyen, B.P.1    Ryan, M.C.2    Gil, S.G.3    Carter, W.G.4
  • 19
    • 0034858098 scopus 로고    scopus 로고
    • Biological and clinical relevance of Laminin-5 in cancer
    • Giannelli, G. and Antonaci, S. (2001) Biological and clinical relevance of Laminin-5 in cancer. Clin. Exp. Metastasis 18, 439-443
    • (2001) Clin. Exp. Metastasis , vol.18 , pp. 439-443
    • Giannelli, G.1    Antonaci, S.2
  • 20
    • 0035892362 scopus 로고    scopus 로고
    • Laminin-5 in the progression of carcinomas
    • Lohi, J. (2001) Laminin-5 in the progression of carcinomas. Int. J. Cancer 94, 763-767
    • (2001) Int. J. Cancer , vol.94 , pp. 763-767
    • Lohi, J.1
  • 21
    • 0026640262 scopus 로고
    • The anchoring filament protein kalinin is synthesized and secreted as a high molecular weight precursor
    • Marinkovich, M.P., Lunstrum, G.P., and Burgeson, R.E. (1992) The anchoring filament protein kalinin is synthesized and secreted as a high molecular weight precursor. J. Biol. Chem. 267, 17900-17906
    • (1992) J. Biol. Chem. , vol.267 , pp. 17900-17906
    • Marinkovich, M.P.1    Lunstrum, G.P.2    Burgeson, R.E.3
  • 24
    • 0034614939 scopus 로고    scopus 로고
    • Role of cell surface metalloprotease MT1-MMP in epithelial cell migration over laminin-5
    • Koshikawa, N., Giannelli, G., Cirulli, V., Miyazaki, K., and Quaranta, V. (2000) Role of cell surface metalloprotease MT1-MMP in epithelial cell migration over laminin-5. J. Cell Biol. 148, 615-624
    • (2000) J. Cell Biol. , vol.148 , pp. 615-624
    • Koshikawa, N.1    Giannelli, G.2    Cirulli, V.3    Miyazaki, K.4    Quaranta, V.5
  • 25
    • 0032489876 scopus 로고    scopus 로고
    • Processing of laminin-5 and its functional consequences: Role of plasmin and tissue-type plasminogen activator
    • Goldfinger, L.E., Stack, M.S., and Jones, J.C. (1998) Processing of laminin-5 and its functional consequences: role of plasmin and tissue-type plasminogen activator. J. Cell Biol. 141, 255-265
    • (1998) J. Cell Biol. , vol.141 , pp. 255-265
    • Goldfinger, L.E.1    Stack, M.S.2    Jones, J.C.3
  • 27
    • 0037147336 scopus 로고    scopus 로고
    • Laminin-6 is activated by proteolytic processing and regulates cellular adhesion and migration differently from laminin-5
    • Hirosaki, T., Tsubota, Y., Kariya, Y., Moriyama, K., Mizushima, H., and Miyazaki, K. (2002) Laminin-6 is activated by proteolytic processing and regulates cellular adhesion and migration differently from laminin-5. J. Biol. Chem. 277, 49287-49295
    • (2002) J. Biol. Chem. , vol.277 , pp. 49287-49295
    • Hirosaki, T.1    Tsubota, Y.2    Kariya, Y.3    Moriyama, K.4    Mizushima, H.5    Miyazaki, K.6
  • 29
    • 9444224381 scopus 로고    scopus 로고
    • Regulation of biological activity of laminin-5 by proteolytic processing of γ2 chain
    • Ogawa, T., Tsubota, Y., Maeda, M., Kariya, Y., and Miyazaki, K. (2004) Regulation of biological activity of laminin-5 by proteolytic processing of γ2 chain. J. Cell Biochem. 92, 701-714
    • (2004) J. Cell Biochem. , vol.92 , pp. 701-714
    • Ogawa, T.1    Tsubota, Y.2    Maeda, M.3    Kariya, Y.4    Miyazaki, K.5
  • 30
    • 17644420066 scopus 로고    scopus 로고
    • Regulation of biological activity and matrix assembly of laminin-5 by COOH-terminal, LG4-5 domain of α3 chain
    • Tsubota, Y., Yasuda, C., Kariya, Y., Ogawa, T., Hirosaki, T., Mizushima, H., and Miyazaki, K. (2005) Regulation of biological activity and matrix assembly of laminin-5 by COOH-terminal, LG4-5 domain of α3 chain. J. Biol. Chem. 280, 14370-14377
    • (2005) J. Biol. Chem. , vol.280 , pp. 14370-14377
    • Tsubota, Y.1    Yasuda, C.2    Kariya, Y.3    Ogawa, T.4    Hirosaki, T.5    Mizushima, H.6    Miyazaki, K.7
  • 31
    • 0035980008 scopus 로고    scopus 로고
    • The LG3 module of laminin-5 harbors a binding site for integrin α3β1 that promotes cell adhesion, spreading, and migration
    • Shang, M., Koshikawa, N., Schenk, S., and Quaranta, V. (2001) The LG3 module of laminin-5 harbors a binding site for integrin α3β1 that promotes cell adhesion, spreading, and migration. J. Biol. Chem. 276, 33045-33053
    • (2001) J. Biol. Chem. , vol.276 , pp. 33045-33053
    • Shang, M.1    Koshikawa, N.2    Schenk, S.3    Quaranta, V.4
  • 32
    • 0035081580 scopus 로고    scopus 로고
    • Sole expression of laminin γ2 chain in invading tumor cells and its association with stromal fibrosis in lung adenocarcinomas
    • Kagesato, Y., Mizushima, H., Koshikawa, N., Kitamura, H., Hayashi, H., Ogawa, N., Tsukuda, M., and Miyazaki, K. (2001) Sole expression of laminin γ2 chain in invading tumor cells and its association with stromal fibrosis in lung adenocarcinomas. Jpn. J. Cancer Res. 92, 184-192
    • (2001) Jpn. J. Cancer Res. , vol.92 , pp. 184-192
    • Kagesato, Y.1    Mizushima, H.2    Koshikawa, N.3    Kitamura, H.4    Hayashi, H.5    Ogawa, N.6    Tsukuda, M.7    Miyazaki, K.8
  • 33
    • 0038713422 scopus 로고    scopus 로고
    • Membrane type-1-matrix metalloproteinase expressed by prostate carcinoma cells cleaves human laminin-5 β3 chain and induces cell migration
    • Udayakumar, T.S., Chen, M.L., Bair, E.L., Von Bredow, D.C., Cress, A.E., Nagle, R.B., and Bowden, G.T. (2003) Membrane type-1-matrix metalloproteinase expressed by prostate carcinoma cells cleaves human laminin-5 β3 chain and induces cell migration. Cancer Res. 63, 2292-2299
    • (2003) Cancer Res. , vol.63 , pp. 2292-2299
    • Udayakumar, T.S.1    Chen, M.L.2    Bair, E.L.3    Von Bredow, D.C.4    Cress, A.E.5    Nagle, R.B.6    Bowden, G.T.7
  • 34
    • 2942735025 scopus 로고    scopus 로고
    • The basement membrane protein laminin-5 acts as a soluble cell motility factor
    • Kariya, Y. and Miyazaki, K. (2004) The basement membrane protein laminin-5 acts as a soluble cell motility factor. Exp. Cell Res. 297, 508-520
    • (2004) Exp. Cell Res. , vol.297 , pp. 508-520
    • Kariya, Y.1    Miyazaki, K.2
  • 35
    • 0032948789 scopus 로고    scopus 로고
    • NC1 domain of type VII collagen binds to the β3 chain of laminin 5 via a unique subdomain within the fibronectin-like repeats
    • Chen, M., Marinkovich, M.P., Jones, J.C., O'Toole, E.A., Li, Y.Y., and Woodley, D.T. (1999) NC1 domain of type VII collagen binds to the β3 chain of laminin 5 via a unique subdomain within the fibronectin-like repeats. J. Invest. Dermatol. 112, 177-183
    • (1999) J. Invest. Dermatol. , vol.112 , pp. 177-183
    • Chen, M.1    Marinkovich, M.P.2    Jones, J.C.3    O'Toole, E.A.4    Li, Y.Y.5    Woodley, D.T.6
  • 39
    • 0027313437 scopus 로고
    • Self-assembly and calcium-binding sites in laminin. A three-arm interaction model
    • Yurchenco, P.D. and Cheng, Y.S. (1993) Self-assembly and calcium-binding sites in laminin. A three-arm interaction model. J. Biol. Chem. 268, 17286-17299
    • (1993) J. Biol. Chem , vol.268 , pp. 17286-17299
    • Yurchenco, P.D.1    Cheng, Y.S.2
  • 40
    • 0028310422 scopus 로고
    • The complete primary structure for a novel laminin chain, the laminin Blk chain
    • Gerecke, D.R., Wagman, D.W., Champliaud, M.F., and Burgeson, R.E. (1994) The complete primary structure for a novel laminin chain, the laminin Blk chain. J. Biol. Chem. 269, 11073-11080
    • (1994) J. Biol. Chem. , vol.269 , pp. 11073-11080
    • Gerecke, D.R.1    Wagman, D.W.2    Champliaud, M.F.3    Burgeson, R.E.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.