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Volumn 7, Issue 5, 2007, Pages 370-380

Tumour microenvironment: Laminin 332 in squamous-cell carcinoma

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA6BETA4 INTEGRIN; ANTINEOPLASTIC AGENT; CELL SURFACE RECEPTOR; COLLAGEN TYPE 7; EPIDERMAL GROWTH FACTOR RECEPTOR; EPIDERMAL GROWTH FACTOR RECEPTOR ANTIBODY; KALININ; LAMININ; LAMININ 111; LAMININ GAMMA2; MEMBRANE PROTEIN; MEMBRANE RECEPTOR; PHOSPHATIDYLINOSITOL 3 KINASE; RAC1 PROTEIN; SYNDECAN 1; UNCLASSIFIED DRUG; VERY LATE ACTIVATION ANTIGEN 3;

EID: 34247474890     PISSN: 1474175X     EISSN: 14741768     Source Type: Journal    
DOI: 10.1038/nrc2089     Document Type: Review
Times cited : (256)

References (105)
  • 1
    • 0028284693 scopus 로고
    • Nonmelanoma skin cancer in the United States: Incidence
    • Miller, D. L. & Weinstock, M. A. Nonmelanoma skin cancer in the United States: incidence. J. Am. Acad. Dermatol. 30, 774-778 (1994).
    • (1994) J. Am. Acad. Dermatol , vol.30 , pp. 774-778
    • Miller, D.L.1    Weinstock, M.A.2
  • 2
    • 0028280454 scopus 로고
    • Metastases from squamous cell carcinoma of the skin in southern Australia
    • Czarnecki, D., Staples, M., Mar, A., Giles, G. & Meehan, C. Metastases from squamous cell carcinoma of the skin in southern Australia. Dermatology 189, 52-54 (1994).
    • (1994) Dermatology , vol.189 , pp. 52-54
    • Czarnecki, D.1    Staples, M.2    Mar, A.3    Giles, G.4    Meehan, C.5
  • 4
    • 0030818252 scopus 로고    scopus 로고
    • Immunodissection of the connective tissue matrix in human skin
    • Keene, D. R., Marinkovich, M. P. & Sakai, L. Y. Immunodissection of the connective tissue matrix in human skin. Microsc. Res. Tech. 38, 394-406 (1997).
    • (1997) Microsc. Res. Tech , vol.38 , pp. 394-406
    • Keene, D.R.1    Marinkovich, M.P.2    Sakai, L.Y.3
  • 6
    • 5044238876 scopus 로고    scopus 로고
    • Integrin signalling during tumour progression
    • Guo, W. & Giancotti, F. G. Integrin signalling during tumour progression. Nature Rev. Mol. Cell Biol. 5, 816-826 (2004).
    • (2004) Nature Rev. Mol. Cell Biol , vol.5 , pp. 816-826
    • Guo, W.1    Giancotti, F.G.2
  • 7
    • 0042371856 scopus 로고    scopus 로고
    • Proteolyzed matrix as a template for the regulation of tumor progression
    • Hornebeck, W. & Maquart, F. X. Proteolyzed matrix as a template for the regulation of tumor progression. Biomed. Pharmacother. 57, 223-230 (2003).
    • (2003) Biomed. Pharmacother , vol.57 , pp. 223-230
    • Hornebeck, W.1    Maquart, F.X.2
  • 8
    • 0037379779 scopus 로고    scopus 로고
    • Clinical, cellular, and molecular aspects of cancer invasion
    • Mareel, M. & Leroy, A. Clinical, cellular, and molecular aspects of cancer invasion. Physiol. Rev. 83, 337-376 (2003).
    • (2003) Physiol. Rev , vol.83 , pp. 337-376
    • Mareel, M.1    Leroy, A.2
  • 9
    • 0022555838 scopus 로고
    • Biochemical interactions of tumor cells with basement membrane
    • Liotta, L. A., Rao, C. N. & Wewer, U. M. Biochemical interactions of tumor cells with basement membrane. Ann. Rev. Biochem. 55, 1037-1057 (1986).
    • (1986) Ann. Rev. Biochem , vol.55 , pp. 1037-1057
    • Liotta, L.A.1    Rao, C.N.2    Wewer, U.M.3
  • 10
    • 0019195010 scopus 로고
    • Metastatic potential correlates with enzymatic degradation of basement membrane collagen
    • Liotta, L. A. et al. Metastatic potential correlates with enzymatic degradation of basement membrane collagen. Nature 284, 67-68 (1980).
    • (1980) Nature , vol.284 , pp. 67-68
    • Liotta, L.A.1
  • 11
    • 1842509188 scopus 로고    scopus 로고
    • Laminin: The crux of basement membrane assembly
    • Sasaki, T., Fassler, R. & Hohenester, E. Laminin: the crux of basement membrane assembly. J. Cell Biol. 164, 959-963 (2004).
    • (2004) J. Cell Biol , vol.164 , pp. 959-963
    • Sasaki, T.1    Fassler, R.2    Hohenester, E.3
  • 12
    • 0030512153 scopus 로고    scopus 로고
    • The functions of laminins: Lessons from in vivo studies
    • Ryan, M. C. et al. The functions of laminins: lessons from in vivo studies. Matrix Biol. 15, 369-381 (1996).
    • (1996) Matrix Biol , vol.15 , pp. 369-381
    • Ryan, M.C.1
  • 13
    • 0027420876 scopus 로고
    • The basement membrane proteins kalinin and nicein are structurally and immunologically identical
    • Marinkovich, M. P. et al. The basement membrane proteins kalinin and nicein are structurally and immunologically identical. Lab. Invest. 69, 295-299 (1993).
    • (1993) Lab. Invest , vol.69 , pp. 295-299
    • Marinkovich, M.P.1
  • 14
    • 0027106641 scopus 로고
    • Kalinin is abnormally expressed in epithelial basement membranes of Herlitz's junctional epidermolysis bullosa patients
    • Meneguzzi, G. et al. Kalinin is abnormally expressed in epithelial basement membranes of Herlitz's junctional epidermolysis bullosa patients. Exp. Dermatol. 1, 221-229 (1992).
    • (1992) Exp. Dermatol , vol.1 , pp. 221-229
    • Meneguzzi, G.1
  • 15
    • 0028568985 scopus 로고
    • A homozygous nonsense mutation in the beta 3 chain gene of laminin 5 (LAMB3) in Herlitz junctional epidermolysis bullosa
    • Pulkkinen, L. et al. A homozygous nonsense mutation in the beta 3 chain gene of laminin 5 (LAMB3) in Herlitz junctional epidermolysis bullosa. Genomics 24, 357-360 (1994).
    • (1994) Genomics , vol.24 , pp. 357-360
    • Pulkkinen, L.1
  • 16
    • 18344413641 scopus 로고
    • Herlitz's junctional epidermolysis bullosa is linked to mutations in the gene (LAMC2) for the gamma 2 subunit of nicein/kalinin (LAMININ-5)
    • Aberdam, D. et al. Herlitz's junctional epidermolysis bullosa is linked to mutations in the gene (LAMC2) for the gamma 2 subunit of nicein/kalinin (LAMININ-5). Nature Genet. 6, 299-304 (1994).
    • (1994) Nature Genet , vol.6 , pp. 299-304
    • Aberdam, D.1
  • 17
    • 0023503414 scopus 로고
    • Laminin and other basement membrane components
    • Martin, G. R. & Timpl, R. Laminin and other basement membrane components. Annu. Rev. Cell Biol. 3, 57-85 (1987).
    • (1987) Annu. Rev. Cell Biol , vol.3 , pp. 57-85
    • Martin, G.R.1    Timpl, R.2
  • 18
    • 0026754516 scopus 로고    scopus 로고
    • Kallunki, P. et al. A truncated laminin chain homologous to the B2 chain: structure, spacial expression, and chromosomal assignment. J. Cell Biol. 119, 679-694 (1992). Identification of laminin 332 as a member of the laminin family.
    • Kallunki, P. et al. A truncated laminin chain homologous to the B2 chain: structure, spacial expression, and chromosomal assignment. J. Cell Biol. 119, 679-694 (1992). Identification of laminin 332 as a member of the laminin family.
  • 19
    • 0030447227 scopus 로고    scopus 로고
    • Differential expression of laminin-5/ladsin subunits in human tissues and cancer cell lines and their induction by tumor promoter and growth factors
    • Mizushima, H. et al. Differential expression of laminin-5/ladsin subunits in human tissues and cancer cell lines and their induction by tumor promoter and growth factors. J. Biochem. (Tokyo) 120, 1196-1202 (1996).
    • (1996) J. Biochem. (Tokyo) , vol.120 , pp. 1196-1202
    • Mizushima, H.1
  • 20
    • 0029144854 scopus 로고    scopus 로고
    • Pyke, C. et al. Laminin-5 is a marker of invading cancer cells in some human carcinomas and is coexpressed with the receptor for urokinase plasminogen activator in budding cancer cells in colon adenocarcinomas. Cancer Res. 55, 4132-4139 (1995). Early extensive survey of laminin 332 in human carcinomas.
    • Pyke, C. et al. Laminin-5 is a marker of invading cancer cells in some human carcinomas and is coexpressed with the receptor for urokinase plasminogen activator in budding cancer cells in colon adenocarcinomas. Cancer Res. 55, 4132-4139 (1995). Early extensive survey of laminin 332 in human carcinomas.
  • 21
    • 0030669932 scopus 로고    scopus 로고
    • Pancreatic carcinomas deposit laminin-5, preferably adhere to laminin-5, and migrate on the newly deposited basement membrane
    • Tani, T. et al. Pancreatic carcinomas deposit laminin-5, preferably adhere to laminin-5, and migrate on the newly deposited basement membrane. Am. J. Pathol. 151, 1289-1302 (1997).
    • (1997) Am. J. Pathol , vol.151 , pp. 1289-1302
    • Tani, T.1
  • 22
    • 0031543797 scopus 로고    scopus 로고
    • Oral squamous cell carcinoma invasion is associated with a laminin-5 matrix re-organization but independent of basement membrane and hemidesmosome formation. Clues from an in vitro invasion model
    • Berndt, A., Hyckel, P., Könneker, A., Katenkamp, D. & Kosmehl, H. Oral squamous cell carcinoma invasion is associated with a laminin-5 matrix re-organization but independent of basement membrane and hemidesmosome formation. Clues from an in vitro invasion model. Invasion Metastasis 17, 251-258 (1997).
    • (1997) Invasion Metastasis , vol.17 , pp. 251-258
    • Berndt, A.1    Hyckel, P.2    Könneker, A.3    Katenkamp, D.4    Kosmehl, H.5
  • 23
    • 0031868639 scopus 로고    scopus 로고
    • Human colonic cancer cells synthesize and adhere to laminin-5. Their adhesion to laminin-5 involves multiple receptors among which is integrin alpha2beta1
    • Orian-Rousseau, V. et al. Human colonic cancer cells synthesize and adhere to laminin-5. Their adhesion to laminin-5 involves multiple receptors among which is integrin alpha2beta1. J. Cell Sci. 111, 1993-2004 (1998).
    • (1998) J. Cell Sci , vol.111 , pp. 1993-2004
    • Orian-Rousseau, V.1
  • 24
    • 0033520765 scopus 로고    scopus 로고
    • Laminin-5 as a marker of invasiveness in cervical lesions
    • Skyldberg, B. et al. Laminin-5 as a marker of invasiveness in cervical lesions. J. Natl Cancer Inst. 91, 1882-1887 (1999).
    • (1999) J. Natl Cancer Inst , vol.91 , pp. 1882-1887
    • Skyldberg, B.1
  • 25
    • 0033137299 scopus 로고    scopus 로고
    • Clinocopathologic significance of laminin-5 ?2 chain expression in squamous cell carcinoma of the tongue: Immunohistochemical analysis of 67 lesions
    • Ono, Y. et al. Clinocopathologic significance of laminin-5 ?2 chain expression in squamous cell carcinoma of the tongue: immunohistochemical analysis of 67 lesions. Cancer 85, 2315-2321 (1999).
    • (1999) Cancer , vol.85 , pp. 2315-2321
    • Ono, Y.1
  • 26
    • 0034069310 scopus 로고    scopus 로고
    • Basement membrane laminin-5 is deposited in colorectal adenomas and carcinomas and serves as a ligand for α3β1 integrin
    • Lohi, J. et al. Basement membrane laminin-5 is deposited in colorectal adenomas and carcinomas and serves as a ligand for α3β1 integrin. APMIS 108, 161-172 (2000).
    • (2000) APMIS , vol.108 , pp. 161-172
    • Lohi, J.1
  • 27
    • 0035064919 scopus 로고    scopus 로고
    • Laminin-5 as a predictor of invasiveness in cancer in situ lesions of the larynx
    • Nordemar, S. et al. Laminin-5 as a predictor of invasiveness in cancer in situ lesions of the larynx. Anticancer Res. 21, 509-512 (2001).
    • (2001) Anticancer Res , vol.21 , pp. 509-512
    • Nordemar, S.1
  • 28
    • 0034800325 scopus 로고    scopus 로고
    • Laminin-5 gamma 2 chain expression correlates with unfavorable prognosis in colon carcinomas
    • Lenander, C. et al. Laminin-5 gamma 2 chain expression correlates with unfavorable prognosis in colon carcinomas. Anal. Cell. Pathol. 22, 201-209 (2001).
    • (2001) Anal. Cell. Pathol , vol.22 , pp. 201-209
    • Lenander, C.1
  • 29
    • 0035120266 scopus 로고    scopus 로고
    • Laminin-5-mediated gene expression in human prostate carcinoma cells
    • Calaluce, R. et al. Laminin-5-mediated gene expression in human prostate carcinoma cells. Mol. Carcinog. 30, 119-129 (2001).
    • (2001) Mol. Carcinog , vol.30 , pp. 119-129
    • Calaluce, R.1
  • 30
    • 0842321844 scopus 로고    scopus 로고
    • Laminin-5 gamma 2: A marker to identify oral mucosal lesions at risk for tumor development?
    • Nordemar, S., Hogmo, A., Lindholm, J., Auer, G. & Munck-Wikland, E. Laminin-5 gamma 2: a marker to identify oral mucosal lesions at risk for tumor development? Anticancer Res. 23, 4985-4989 (2003).
    • (2003) Anticancer Res , vol.23 , pp. 4985-4989
    • Nordemar, S.1    Hogmo, A.2    Lindholm, J.3    Auer, G.4    Munck-Wikland, E.5
  • 31
    • 0141679409 scopus 로고    scopus 로고
    • Laminin-5 chains are expressed differentially in metastatic and nonmetastatic hepatocellular carcinoma
    • Giannelli, G., Fransvea, E., Bergamini, C., Marinosci, F. & Antonaci, S. Laminin-5 chains are expressed differentially in metastatic and nonmetastatic hepatocellular carcinoma. Clin. Cancer Res. 9, 3684-3691 (2003).
    • (2003) Clin. Cancer Res , vol.9 , pp. 3684-3691
    • Giannelli, G.1    Fransvea, E.2    Bergamini, C.3    Marinosci, F.4    Antonaci, S.5
  • 32
    • 0034906939 scopus 로고    scopus 로고
    • Expression of the γ (2) chain of laminin-5 at the invasive front is associated with recurrence and poor prognosis in human esophageal squamous cell carcinoma
    • Yamamoto, H., Itoh, F., Iku, S., Hosokawa, M. & Imai, K. Expression of the γ (2) chain of laminin-5 at the invasive front is associated with recurrence and poor prognosis in human esophageal squamous cell carcinoma. Clin. Cancer Res. 7, 896-900 (2001).
    • (2001) Clin. Cancer Res , vol.7 , pp. 896-900
    • Yamamoto, H.1    Itoh, F.2    Iku, S.3    Hosokawa, M.4    Imai, K.5
  • 33
    • 0036192802 scopus 로고    scopus 로고
    • Laminin-5 gamma 2 chain as an invasivity marker for uni- and multifocal lesions in the lower anogenital tract
    • Nordstrom, B. et al. Laminin-5 gamma 2 chain as an invasivity marker for uni- and multifocal lesions in the lower anogenital tract. Int. J. Gynecol. Cancer 12, 105-109 (2002).
    • (2002) Int. J. Gynecol. Cancer , vol.12 , pp. 105-109
    • Nordstrom, B.1
  • 34
    • 0034858098 scopus 로고    scopus 로고
    • Biological and clinical relevance of Laminin-5 in cancer
    • Giannelli, G. & Antonaci, S. Biological and clinical relevance of Laminin-5 in cancer. Clin. Exp. Metastasis 18, 439-443 (2000).
    • (2000) Clin. Exp. Metastasis , vol.18 , pp. 439-443
    • Giannelli, G.1    Antonaci, S.2
  • 35
    • 0037207873 scopus 로고    scopus 로고
    • Laminin γ2-chain fragment in the circulation: A prognostic indicator of epithelial tumor invasion
    • Katayama, M., Sanzen, N., Funakoshi, A. & Sekiguchi, K. Laminin γ2-chain fragment in the circulation: a prognostic indicator of epithelial tumor invasion. Cancer Res. 63, 222-229 (2003).
    • (2003) Cancer Res , vol.63 , pp. 222-229
    • Katayama, M.1    Sanzen, N.2    Funakoshi, A.3    Sekiguchi, K.4
  • 36
    • 13444260900 scopus 로고    scopus 로고
    • Prognostic implication of laminin-5 gamma 2 chain expression in the invasive front of colorectal cancers, disclosed by area-specific four-point tissue microarrays
    • Shinto, E. et al. Prognostic implication of laminin-5 gamma 2 chain expression in the invasive front of colorectal cancers, disclosed by area-specific four-point tissue microarrays. Lab. Invest. 85, 257-266 (2005).
    • (2005) Lab. Invest , vol.85 , pp. 257-266
    • Shinto, E.1
  • 37
    • 0027202061 scopus 로고
    • Expression and topography of integrins and basement membrane proteins in epidermal carcinomas: Basal but not squamous cell carcinomas display loss of alpha 6 beta 4 and BM-600/nicein
    • Savoia, P., Trusolino, L., Pepino, E. & Marchisio, P. C. Expression and topography of integrins and basement membrane proteins in epidermal carcinomas: basal but not squamous cell carcinomas display loss of alpha 6 beta 4 and BM-600/nicein. J. Invest. Dermatol. 101, 352-358 (1993).
    • (1993) J. Invest. Dermatol , vol.101 , pp. 352-358
    • Savoia, P.1    Trusolino, L.2    Pepino, E.3    Marchisio, P.C.4
  • 38
    • 0031756580 scopus 로고    scopus 로고
    • Down-regulation of laminin-5 in breast carcinoma cells
    • Martin, K. J. et al. Down-regulation of laminin-5 in breast carcinoma cells. Mol. Med. 4, 602-613 (1998).
    • (1998) Mol. Med , vol.4 , pp. 602-613
    • Martin, K.J.1
  • 39
    • 21044438494 scopus 로고    scopus 로고
    • Laminin isoform expression in breast tumors
    • Holler, E. Laminin isoform expression in breast tumors. Breast Cancer Res. 7, 166-167 (2005).
    • (2005) Breast Cancer Res , vol.7 , pp. 166-167
    • Holler, E.1
  • 40
    • 0035103373 scopus 로고    scopus 로고
    • Investigation into the mechanism of the loss of laminin 5 (α3β3γ2) expression in prostate cancer
    • Hao, J. et al. Investigation into the mechanism of the loss of laminin 5 (α3β3γ2) expression in prostate cancer. Am. J. Pathol. 158, 1129-135. (2001).
    • (2001) Am. J. Pathol , vol.158 , pp. 1129-1135
    • Hao, J.1
  • 41
    • 33644522372 scopus 로고    scopus 로고
    • New roles for integrins in squamous-cell carcinoma
    • Janes, S. M. & Watt, F. M. New roles for integrins in squamous-cell carcinoma. Nature Rev. Cancer 3, 175-183 (2006).
    • (2006) Nature Rev. Cancer , vol.3 , pp. 175-183
    • Janes, S.M.1    Watt, F.M.2
  • 42
    • 0038242298 scopus 로고    scopus 로고
    • Laminin-10 is crucial for hair morphogenesis
    • Li, J. et al. Laminin-10 is crucial for hair morphogenesis. EMBO J. 22, 2400-2410 (2003).
    • (2003) EMBO J , vol.22 , pp. 2400-2410
    • Li, J.1
  • 43
    • 0033523759 scopus 로고    scopus 로고
    • Sonic hedgehog opposes epithelial cell cycle arrest
    • Fan, H. & Khavari, P. A. Sonic hedgehog opposes epithelial cell cycle arrest. J. Cell Biol. 147, 71-76 (1999).
    • (1999) J. Cell Biol , vol.147 , pp. 71-76
    • Fan, H.1    Khavari, P.A.2
  • 44
    • 21644481842 scopus 로고    scopus 로고
    • Tumor cell invasion assays
    • Shaw, L. M. Tumor cell invasion assays. Methods Mol. Biol. 294, 97-105 (2005).
    • (2005) Methods Mol. Biol , vol.294 , pp. 97-105
    • Shaw, L.M.1
  • 45
    • 5444241773 scopus 로고    scopus 로고
    • In vivo matrigel migration and angiogenesis assays
    • Malinda, K. M. In vivo matrigel migration and angiogenesis assays. Methods Mol. Med. 78, 329-335 (2003).
    • (2003) Methods Mol. Med , vol.78 , pp. 329-335
    • Malinda, K.M.1
  • 46
    • 2142849935 scopus 로고    scopus 로고
    • The use of Matrigel to facilitate the establishment of human cancer cell lines as xenografts
    • Mullen, P. The use of Matrigel to facilitate the establishment of human cancer cell lines as xenografts. Methods Mol. Med. 88, 287-292 (2004).
    • (2004) Methods Mol. Med , vol.88 , pp. 287-292
    • Mullen, P.1
  • 47
    • 0345381943 scopus 로고    scopus 로고
    • Expression and biological role of laminin-1
    • Ekblom, P., Lonai, P. & Talts, J. F. Expression and biological role of laminin-1. Matrix Biol. 22, 35-47 (2003).
    • (2003) Matrix Biol , vol.22 , pp. 35-47
    • Ekblom, P.1    Lonai, P.2    Talts, J.F.3
  • 48
    • 0025879967 scopus 로고    scopus 로고
    • Rousselle, P., Lunstrum, G. P., Keene, D. R. & Burgeson, R. E. Kalinin: an epithelium-specific basement membrane adhesion molecule that is a component of anchoring filaments. J. Cell Biol. 114, 567-576 (1991). Characterization of the role of laminin 332 in epidermal adhesion.
    • Rousselle, P., Lunstrum, G. P., Keene, D. R. & Burgeson, R. E. Kalinin: an epithelium-specific basement membrane adhesion molecule that is a component of anchoring filaments. J. Cell Biol. 114, 567-576 (1991). Characterization of the role of laminin 332 in epidermal adhesion.
  • 49
    • 0025887362 scopus 로고    scopus 로고
    • Carter, W. G., Ryan, M. C. & Gahr, P. J. Epiligrin, a new cell adhesion ligand for integrin-3-1 in epithelial basement membranes. Cell 65, 559-610 (1991). Characterization of laminin 332 integrin specificity.
    • Carter, W. G., Ryan, M. C. & Gahr, P. J. Epiligrin, a new cell adhesion ligand for integrin-3-1 in epithelial basement membranes. Cell 65, 559-610 (1991). Characterization of laminin 332 integrin specificity.
  • 50
    • 0025679064 scopus 로고
    • Distinct functions for integrins alpha 3 beta 1 in focal adhesions and alpha 6 beta 4/bullous pemphigoid antigen in a new stable anchoring contact (SAC) of keratinocytes: Relation to hemidesmosomes
    • Carter, W. G., Kaur, P., Gil, S. G., Gahr, P. J. & Wayner, E. A. Distinct functions for integrins alpha 3 beta 1 in focal adhesions and alpha 6 beta 4/bullous pemphigoid antigen in a new stable anchoring contact (SAC) of keratinocytes: relation to hemidesmosomes. J. Cell Biol. 111, 3141-3154 (1990).
    • (1990) J. Cell Biol , vol.111 , pp. 3141-3154
    • Carter, W.G.1    Kaur, P.2    Gil, S.G.3    Gahr, P.J.4    Wayner, E.A.5
  • 51
    • 0036488589 scopus 로고    scopus 로고
    • Role of integrins in cell invasion and migration
    • Hood, J. D. & Cheresh, D. A. Role of integrins in cell invasion and migration. Nature Rev. Cancer 2, 91-100 (2002).
    • (2002) Nature Rev. Cancer , vol.2 , pp. 91-100
    • Hood, J.D.1    Cheresh, D.A.2
  • 53
    • 33745947286 scopus 로고    scopus 로고
    • Current insights into the formation and breakdown of hemidesmosomes
    • Litjens, S. H., de Pereda, J. M. & Sonnenberg, A. Current insights into the formation and breakdown of hemidesmosomes. Trends Cell Biol. 16, 376-383 (2006).
    • (2006) Trends Cell Biol , vol.16 , pp. 376-383
    • Litjens, S.H.1    de Pereda, J.M.2    Sonnenberg, A.3
  • 54
    • 0036854284 scopus 로고    scopus 로고
    • Dynamics of the α6β4 Integrin in keratinocytes
    • Geuijen, C. A. & Sonnenberg, A. Dynamics of the α6β4 Integrin in keratinocytes. Mol. Biol. Cell 13, 3845-3858 (2002).
    • (2002) Mol. Biol. Cell , vol.13 , pp. 3845-3858
    • Geuijen, C.A.1    Sonnenberg, A.2
  • 55
    • 0032893454 scopus 로고    scopus 로고
    • Laminin-5 promotes adhesion and migration of epithelial cells: Identification of a migration-related element in the γ2 chain gene (LAMC2) with activity in transgenic mice
    • Salo, S. et al. Laminin-5 promotes adhesion and migration of epithelial cells: identification of a migration-related element in the γ2 chain gene (LAMC2) with activity in transgenic mice. Matrix Biol. 18, 197-210 (1999).
    • (1999) Matrix Biol , vol.18 , pp. 197-210
    • Salo, S.1
  • 56
    • 0030798679 scopus 로고    scopus 로고
    • Giannelli, G., Falk-Marzillier, J., Schiraldi, O., Stetler-Stevenson, W. G. & Quaranta, V. Induction of cell migration by matrix metalloprotease-2 cleavage of laminin-5. Science 277, 225-228 (1997). Shows the association between laminin 332 processing and carcinoma cell migration.
    • Giannelli, G., Falk-Marzillier, J., Schiraldi, O., Stetler-Stevenson, W. G. & Quaranta, V. Induction of cell migration by matrix metalloprotease-2 cleavage of laminin-5. Science 277, 225-228 (1997). Shows the association between laminin 332 processing and carcinoma cell migration.
  • 57
    • 0030587422 scopus 로고    scopus 로고
    • Laminin 5 deposition promotes keratinocyte motility
    • Zhang, K. & Kramer, R. H. Laminin 5 deposition promotes keratinocyte motility. Exp. Cell Res. 227, 309-322 (1996).
    • (1996) Exp. Cell Res , vol.227 , pp. 309-322
    • Zhang, K.1    Kramer, R.H.2
  • 58
    • 0027144778 scopus 로고    scopus 로고
    • Miyazaki, K., Kikkawa, Y., Nakamura, A., Yasumitsu, H. & Umeda, M. A large cell-adhesive scatter factor secreted by human gastric carcinoma cells. Proc. Natl Acad. Sci. USA 90, 11767-1171 (1993). Demonstration of the role of laminin 332 in tumour-cell migration.
    • Miyazaki, K., Kikkawa, Y., Nakamura, A., Yasumitsu, H. & Umeda, M. A large cell-adhesive scatter factor secreted by human gastric carcinoma cells. Proc. Natl Acad. Sci. USA 90, 11767-1171 (1993). Demonstration of the role of laminin 332 in tumour-cell migration.
  • 59
    • 2942735025 scopus 로고    scopus 로고
    • The basement membrane protein laminin-5 acts as a soluble cell motility factor
    • Kariya, Y. & Miyazaki, K. The basement membrane protein laminin-5 acts as a soluble cell motility factor. Exp. Cell Res. 297, 508-520 (2004).
    • (2004) Exp. Cell Res , vol.297 , pp. 508-520
    • Kariya, Y.1    Miyazaki, K.2
  • 60
    • 0034644687 scopus 로고    scopus 로고
    • Deposition of laminin 5 by keratinocytes regulates integrin adhesion and signaling
    • Nguyen, B. P., Gil, S. G. & Carter, W. G. Deposition of laminin 5 by keratinocytes regulates integrin adhesion and signaling. J. Biol. Chem. 275, 31896-31907 (2000).
    • (2000) J. Biol. Chem , vol.275 , pp. 31896-31907
    • Nguyen, B.P.1    Gil, S.G.2    Carter, W.G.3
  • 61
    • 0035941357 scopus 로고    scopus 로고
    • Ligation of integrin α3β1 by laminin 5 at the wound edge activates Rho-dependent adhesion of leading keratinocytes on collagen
    • Nguyen, B. P., Ren, X. D., Schwartz, M. A. & Carter, W. G. Ligation of integrin α3β1 by laminin 5 at the wound edge activates Rho-dependent adhesion of leading keratinocytes on collagen. J. Biol. Chem. 276, 43860-43870 (2001).
    • (2001) J. Biol. Chem , vol.276 , pp. 43860-43870
    • Nguyen, B.P.1    Ren, X.D.2    Schwartz, M.A.3    Carter, W.G.4
  • 62
    • 15444367651 scopus 로고    scopus 로고
    • Integrin engagement differentially modulates epithelial cell motility by RhoA/ROCK and PAK1
    • Zhou, H. & Kramer, R. H. Integrin engagement differentially modulates epithelial cell motility by RhoA/ROCK and PAK1. J. Biol. Chem. 280, 10624-10635 (2005).
    • (2005) J. Biol. Chem , vol.280 , pp. 10624-10635
    • Zhou, H.1    Kramer, R.H.2
  • 63
    • 0041326890 scopus 로고    scopus 로고
    • Alpha 6 beta 4 integrin regulates keratinocyte chemotaxis through differential GTPase activation and antagonism of alpha 3 beta 1 integrin
    • Russell, A. J. et al. Alpha 6 beta 4 integrin regulates keratinocyte chemotaxis through differential GTPase activation and antagonism of alpha 3 beta 1 integrin. J. Cell Sci. 116, 3543-3556 (2003).
    • (2003) J. Cell Sci , vol.116 , pp. 3543-3556
    • Russell, A.J.1
  • 64
    • 33750514792 scopus 로고    scopus 로고
    • β4 integrin and epidermal growth factor coordinately regulate electric field-mediated directional migration via Rac1
    • Pullar, C. E. et al. β4 integrin and epidermal growth factor coordinately regulate electric field-mediated directional migration via Rac1. Mol. Biol. Cell 17, 4925-4935 (2006).
    • (2006) Mol. Biol. Cell , vol.17 , pp. 4925-4935
    • Pullar, C.E.1
  • 65
    • 33845923906 scopus 로고    scopus 로고
    • Integrin β4 regulates migratory behavior of keratinocytes by determining laminin-332 organization
    • Sehgal, B. U. et al. Integrin β4 regulates migratory behavior of keratinocytes by determining laminin-332 organization. J. Biol. Chem. 46, 35487-35498 (2006).
    • (2006) J. Biol. Chem , vol.46 , pp. 35487-35498
    • Sehgal, B.U.1
  • 66
    • 0347363470 scopus 로고    scopus 로고
    • Autocrine laminin-5 ligates alpha6beta4 integrin and activates RAC and NFκB to mediate anchorage-independent survival of mammary tumors
    • Zahir, N. et al. Autocrine laminin-5 ligates alpha6beta4 integrin and activates RAC and NFκB to mediate anchorage-independent survival of mammary tumors. J. Cell Biol. 163, 1397-1407 (2003).
    • (2003) J. Cell Biol , vol.163 , pp. 1397-1407
    • Zahir, N.1
  • 67
    • 28544437707 scopus 로고    scopus 로고
    • The Rac activator Tiam1 is required for α3β1-mediated laminin-5 deposition, cell spreading, and cell migration
    • Hamelers, I. H. et al. The Rac activator Tiam1 is required for α3β1-mediated laminin-5 deposition, cell spreading, and cell migration. J. Cell Biol. 171, 871-881 (2005).
    • (2005) J. Cell Biol , vol.171 , pp. 871-881
    • Hamelers, I.H.1
  • 68
    • 0037142034 scopus 로고    scopus 로고
    • Mice deficient in the Rac activator Tiam1 are resistant to Ras-induced skin tumours
    • Malliri, A. et al. Mice deficient in the Rac activator Tiam1 are resistant to Ras-induced skin tumours. Nature 417, 867-871 (2002).
    • (2002) Nature , vol.417 , pp. 867-871
    • Malliri, A.1
  • 69
    • 18844424325 scopus 로고    scopus 로고
    • Integrins control motile strategy through a Rho-cofilin pathway
    • Danen, E. H. et al. Integrins control motile strategy through a Rho-cofilin pathway. J. Cell Biol. 169, 515-526 (2005).
    • (2005) J. Cell Biol , vol.169 , pp. 515-526
    • Danen, E.H.1
  • 70
    • 0026640262 scopus 로고    scopus 로고
    • Marinkovich, M. P., Lunstrum, G. P. & Burgeson, R. E. The anchoring filament protein kalinin is synthesized and secreted as a high molecular weight precursor. J. Biol. Chem. 267, 17900-17906 (1992). Characterization of the proteolytic processing of laminin 332.
    • Marinkovich, M. P., Lunstrum, G. P. & Burgeson, R. E. The anchoring filament protein kalinin is synthesized and secreted as a high molecular weight precursor. J. Biol. Chem. 267, 17900-17906 (1992). Characterization of the proteolytic processing of laminin 332.
  • 71
    • 0034725611 scopus 로고    scopus 로고
    • Bone morphogenetic protein 1 is an extracellular processing enzyme of the laminin 5 γ 2 chain
    • Amano, S. et al. Bone morphogenetic protein 1 is an extracellular processing enzyme of the laminin 5 γ 2 chain. J. Biol. Chem. 275, 22728-22735 (2000).
    • (2000) J. Biol. Chem , vol.275 , pp. 22728-22735
    • Amano, S.1
  • 73
    • 0037437146 scopus 로고    scopus 로고
    • Binding to EGF receptor of a laminin-5 EGF-like fragment liberated during MMP-dependent mammary gland involution
    • Schenk, S. et al. Binding to EGF receptor of a laminin-5 EGF-like fragment liberated during MMP-dependent mammary gland involution. J. Cell Biol. 161, 197-209 (2003).
    • (2003) J. Cell Biol , vol.161 , pp. 197-209
    • Schenk, S.1
  • 74
    • 0035085802 scopus 로고    scopus 로고
    • Keratinocyte migration requires alpha2beta1 integrin-mediated interaction with the laminin 5 γ2 chain
    • Decline, F. & Rousselle, P. Keratinocyte migration requires alpha2beta1 integrin-mediated interaction with the laminin 5 γ2 chain. J. Cell Sci. 114, 811-823 (2001).
    • (2001) J. Cell Sci , vol.114 , pp. 811-823
    • Decline, F.1    Rousselle, P.2
  • 75
    • 0035858887 scopus 로고    scopus 로고
    • The short arm of the laminin γ2 chain plays a pivotal role in the incorporation of laminin 5 into the extracellular matrix and in cell adhesion
    • Gagnoux-Palacios, L. et al. The short arm of the laminin γ2 chain plays a pivotal role in the incorporation of laminin 5 into the extracellular matrix and in cell adhesion. J. Cell Biol. 153, 835-850. (2001).
    • (2001) J. Cell Biol , vol.153 , pp. 835-850
    • Gagnoux-Palacios, L.1
  • 76
    • 5444255540 scopus 로고    scopus 로고
    • Globular domains 4/5 of the laminin α3 chain mediate deposition of precursor laminin 5
    • Sigle, R. O. et al. Globular domains 4/5 of the laminin α3 chain mediate deposition of precursor laminin 5. J. Cell Sci. 117, 4481-4494 (2004).
    • (2004) J. Cell Sci , vol.117 , pp. 4481-4494
    • Sigle, R.O.1
  • 77
    • 0037421484 scopus 로고    scopus 로고
    • Dajee, M. et al. NFκB blockade and oncogenic Ras trigger invasive human epidermal neoplasia. Nature 421, 639-643 (2003). Demonstration of the requirement for laminin 332 and α6β4 integrin in human SCC tumours.
    • Dajee, M. et al. NFκB blockade and oncogenic Ras trigger invasive human epidermal neoplasia. Nature 421, 639-643 (2003). Demonstration of the requirement for laminin 332 and α6β4 integrin in human SCC tumours.
  • 78
    • 34247506327 scopus 로고    scopus 로고
    • A laminin-collagen complex drives human epidermal carcinogenesis through phosphoinositol-3 kinase activation
    • in the press
    • Waterman, E. A. et al. A laminin-collagen complex drives human epidermal carcinogenesis through phosphoinositol-3 kinase activation. Cancer Res. (in the press 2007).
    • (2007) Cancer Res
    • Waterman, E.A.1
  • 79
    • 30344450039 scopus 로고    scopus 로고
    • Regulation of cell adhesion and type VII collagen binding by the β3 chain short arm of laminin-5: Effect of its proteolytic cleavage
    • Nakashima, Y., Kariya, Y., Yasuda, C. & Miyazaki, K. Regulation of cell adhesion and type VII collagen binding by the β3 chain short arm of laminin-5: effect of its proteolytic cleavage. J. Biochem. (Tokyo) 138, 539-552 (2005).
    • (2005) J. Biochem. (Tokyo) , vol.138 , pp. 539-552
    • Nakashima, Y.1    Kariya, Y.2    Yasuda, C.3    Miyazaki, K.4
  • 80
    • 0026596372 scopus 로고
    • Epidermolysis bullosa complicated by squamous cell carcinoma: Report of 10 cases
    • McGrath, J. A., Schofield, O. M., Mayou, B. J., McKee, P. H. & Eady, R. A. Epidermolysis bullosa complicated by squamous cell carcinoma: report of 10 cases. J. Cut. Pathol. 19, 116-123 (1992).
    • (1992) J. Cut. Pathol , vol.19 , pp. 116-123
    • McGrath, J.A.1    Schofield, O.M.2    Mayou, B.J.3    McKee, P.H.4    Eady, R.A.5
  • 81
    • 0026774671 scopus 로고
    • Squamous cell carcinoma secondary to recessive dystrophic epidermolysis bullosa. A report of 4 patients with 17 primary cutaneous alignancies
    • Newman, C., Wagner, R. F., Jr., Tyring, S. K. & Spigel, G. T. Squamous cell carcinoma secondary to recessive dystrophic epidermolysis bullosa. A report of 4 patients with 17 primary cutaneous alignancies. J. Dermatol. Surg. Oncol. 18, 301-305 (1992).
    • (1992) J. Dermatol. Surg. Oncol , vol.18 , pp. 301-305
    • Newman, C.1    Wagner Jr., R.F.2    Tyring, S.K.3    Spigel, G.T.4
  • 82
    • 20144385966 scopus 로고    scopus 로고
    • Ortiz-Urda, S. et al. Type VII collagen is required for Ras-driven human epidermal tumorigenesis. Science 307, 1773-1776 (2005). Demonstration of collagen VII requirement in human SCC tumours.
    • Ortiz-Urda, S. et al. Type VII collagen is required for Ras-driven human epidermal tumorigenesis. Science 307, 1773-1776 (2005). Demonstration of collagen VII requirement in human SCC tumours.
  • 83
    • 33746764457 scopus 로고    scopus 로고
    • β4 integrin amplifies ErbB2 signaling to promote mammary tumorigenesis
    • Guo, W. et al. β4 integrin amplifies ErbB2 signaling to promote mammary tumorigenesis. Cell 126, 489-502 (2006).
    • (2006) Cell , vol.126 , pp. 489-502
    • Guo, W.1
  • 84
    • 0035977147 scopus 로고    scopus 로고
    • A signaling adapter function for α6β4 integrin in the control of HGF-dependent invasive growth
    • Trusolino, L., Bertotti, A. & Comoglio, P. M. A signaling adapter function for α6β4 integrin in the control of HGF-dependent invasive growth. Cell 5, 643-654 (2001).
    • (2001) Cell , vol.5 , pp. 643-654
    • Trusolino, L.1    Bertotti, A.2    Comoglio, P.M.3
  • 85
    • 0242414749 scopus 로고    scopus 로고
    • Normal human keratinocytes bind to the α3LG4/5 domain of unprocessed laminin-5 through the receptor syndecan-1
    • Okamoto, O. et al. Normal human keratinocytes bind to the α3LG4/5 domain of unprocessed laminin-5 through the receptor syndecan-1. J. Biol. Chem. 278, 44168-44177 (2003).
    • (2003) J. Biol. Chem , vol.278 , pp. 44168-44177
    • Okamoto, O.1
  • 86
    • 0034735987 scopus 로고    scopus 로고
    • Isolation and activity of proteolytic fragment of laminin-5 α3 chain
    • Tsubota, Y. et al. Isolation and activity of proteolytic fragment of laminin-5 α3 chain. Biochem. Biophys. Res. Commun. 278, 614-620 (2000).
    • (2000) Biochem. Biophys. Res. Commun , vol.278 , pp. 614-620
    • Tsubota, Y.1
  • 87
    • 0038521319 scopus 로고    scopus 로고
    • Mammalian tolloid metalloproteinase, and not matrix metalloprotease 2 or membrane type 1 metalloprotease, processes laminin-5 in keratinocytes and skin
    • Veitch, D. P. et al. Mammalian tolloid metalloproteinase, and not matrix metalloprotease 2 or membrane type 1 metalloprotease, processes laminin-5 in keratinocytes and skin. J. Biol. Chem. 278, 15661-15668 (2003).
    • (2003) J. Biol. Chem , vol.278 , pp. 15661-15668
    • Veitch, D.P.1
  • 88
    • 3042749811 scopus 로고    scopus 로고
    • Epithelial cell motility on laminin-5: Regulation by matrix assembly, proteolysis, integrins and erbB receptors
    • Hintermann, E. & Quaranta, V. Epithelial cell motility on laminin-5: regulation by matrix assembly, proteolysis, integrins and erbB receptors. Matrix Biol. 23, 75-85 (2004).
    • (2004) Matrix Biol , vol.23 , pp. 75-85
    • Hintermann, E.1    Quaranta, V.2
  • 89
    • 0027454382 scopus 로고
    • Cellular origin of the dermalepidermal basement membrane
    • Marinkovich, M. P., Keene, D. R., Rimberg, C. S. & Burgeson, R. E. Cellular origin of the dermalepidermal basement membrane. Dev. Dyn. 197, 255-267 (1993).
    • (1993) Dev. Dyn , vol.197 , pp. 255-267
    • Marinkovich, M.P.1    Keene, D.R.2    Rimberg, C.S.3    Burgeson, R.E.4
  • 90
    • 0018691714 scopus 로고
    • Laminin-a glycoprotein from basement membranes
    • Timpl, R. et al. Laminin-a glycoprotein from basement membranes. J. Biol. Chem. 254, 9933-9937 (1979).
    • (1979) J. Biol. Chem , vol.254 , pp. 9933-9937
    • Timpl, R.1
  • 91
    • 0041858013 scopus 로고    scopus 로고
    • Complex between nidogen and laminin fragments reveals a paradigmatic β-propeller interface
    • Takagi, J., Yang, Y., Liu, J. H., Wang, J. H. & Springer, T. A. Complex between nidogen and laminin fragments reveals a paradigmatic β-propeller interface. Nature 424, 969-974 (2003).
    • (2003) Nature , vol.424 , pp. 969-974
    • Takagi, J.1    Yang, Y.2    Liu, J.H.3    Wang, J.H.4    Springer, T.A.5
  • 93
    • 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. et al. 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).
    • (1996) J. Cell Biol , vol.132 , pp. 1189-1198
    • Champliaud, M.F.1
  • 94
    • 0030855296 scopus 로고    scopus 로고
    • Laminin 5 binds the NC-1 domain of type VII collagen
    • Rousselle, P. et al. Laminin 5 binds the NC-1 domain of type VII collagen. J. Cell Biol. 138, 719-728 (1997).
    • (1997) J. Cell Biol , vol.138 , pp. 719-728
    • Rousselle, P.1
  • 95
    • 0030987772 scopus 로고    scopus 로고
    • Interactions of the amino-terminal noncollagenous (NC1) domain of type VII collagen with extracellular matrix components
    • Chen, M. et al. Interactions of the amino-terminal noncollagenous (NC1) domain of type VII collagen with extracellular matrix components. J. Biol. Chem. 272, 14516-14522 (1997).
    • (1997) J. Biol. Chem , vol.272 , pp. 14516-14522
    • Chen, M.1
  • 96
    • 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. & Quaranta, V. Role of cell surface metalloprotease MT1-MMP in epithelial cell migration over laminin-5. J. Cell Biol. 148, 615-624 (2000).
    • (2000) J. Cell Biol , vol.148 , pp. 615-624
    • Koshikawa, N.1    Giannelli, G.2    Cirulli, V.3    Miyazaki, K.4    Quaranta, V.5
  • 97
    • 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. & Jones, J. C. Processing of laminin-5 and its functional consequences: role of plasmin and tissue-type plasminogen activator. J. Cell Biol. 141, 255-265 (1998).
    • (1998) J. Cell Biol , vol.141 , pp. 255-265
    • Goldfinger, L.E.1    Stack, M.S.2    Jones, J.C.3
  • 98
    • 0034254083 scopus 로고    scopus 로고
    • Structure and function of laminin LG modules
    • Timpl, R. et al. Structure and function of laminin LG modules. Matrix Biol. 19, 309-317. (2000).
    • (2000) Matrix Biol , vol.19 , pp. 309-317
    • Timpl, R.1
  • 99
    • 0037145037 scopus 로고    scopus 로고
    • Integrins: Bidirectional, allosteric signaling machines
    • Hynes, R. O. Integrins: bidirectional, allosteric signaling machines. Cell 110, 673-687 (2002).
    • (2002) Cell , vol.110 , pp. 673-687
    • Hynes, R.O.1
  • 100
    • 0030782512 scopus 로고    scopus 로고
    • Localization of heparin binding activity in recombinant laminin G domain
    • Sung, U., O'Rear, J. J. & Yurchenco, P. D. Localization of heparin binding activity in recombinant laminin G domain. Eur. J. Biochem. 250, 138-143 (1997).
    • (1997) Eur. J. Biochem , vol.250 , pp. 138-143
    • Sung, U.1    O'Rear, J.J.2    Yurchenco, P.D.3
  • 101
    • 0032445403 scopus 로고    scopus 로고
    • A role for dystroglycan in basement membrane assembly
    • Henry, M. D. & Campbell, K. P. A role for dystroglycan in basement membrane assembly. Cell 95, 859-870 (1998).
    • (1998) Cell , vol.95 , pp. 859-870
    • Henry, M.D.1    Campbell, K.P.2
  • 102
    • 0032589487 scopus 로고    scopus 로고
    • Binding of integrin α6β4 to plectin prevents plectin association with F-actin but does not interfere with intermediate filament binding
    • Geerts, D. et al. Binding of integrin α6β4 to plectin prevents plectin association with F-actin but does not interfere with intermediate filament binding. J. Cell Biol. 147, 417-434 (1999).
    • (1999) J. Cell Biol , vol.147 , pp. 417-434
    • Geerts, D.1
  • 103
    • 0034110936 scopus 로고    scopus 로고
    • Formation of hemidesmosome-like structures in the absence of ligand binding by the α6β4 integrin requires binding of HD1/plectin to the cytoplasmic domain of the β4 integrin subunit
    • Nievers, M. G., Kuikman, I., Geerts, D., Leigh, I. M. & Sonnenberg, A. Formation of hemidesmosome-like structures in the absence of ligand binding by the α6β4 integrin requires binding of HD1/plectin to the cytoplasmic domain of the β4 integrin subunit. J. Cell Sci. 113, 963-973 (2000).
    • (2000) J. Cell Sci , vol.113 , pp. 963-973
    • Nievers, M.G.1    Kuikman, I.2    Geerts, D.3    Leigh, I.M.4    Sonnenberg, A.5
  • 104
    • 0034658462 scopus 로고    scopus 로고
    • The tetraspan molecule CD151, a novel constituent of hemidesmosomes, associates with the integrin α6β4 and may regulate the spatial organization of hemidesmosomes
    • Sterk, L. M. et al. The tetraspan molecule CD151, a novel constituent of hemidesmosomes, associates with the integrin α6β4 and may regulate the spatial organization of hemidesmosomes. J. Cell Biol. 149, 969-982 (2000).
    • (2000) J. Cell Biol , vol.149 , pp. 969-982
    • Sterk, L.M.1
  • 105
    • 0037087710 scopus 로고    scopus 로고
    • Association of the tetraspanin CD151 with the laminin-binding integrins α3β1, α6β1, α6β4 and α7β1 in cells in culture and in vivo
    • Sterk, L. M. et al. Association of the tetraspanin CD151 with the laminin-binding integrins α3β1, α6β1, α6β4 and α7β1 in cells in culture and in vivo. J. Cell Sci. 115, 1161-1173 (2002).
    • (2002) J. Cell Sci , vol.115 , pp. 1161-1173
    • Sterk, L.M.1


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