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Volumn 27, Issue 3, 2008, Pages 220-231

Src kinase regulates metalloproteinase-9 secretion induced by type IV collagen in MCF-7 human breast cancer cells

Author keywords

Basement membrane; Breast cancer; Collagen; FAK; MCF 7; MMP 9; Src

Indexed keywords

COLLAGEN TYPE 4; FAK KINASE; GELATINASE B; PROTEIN ANTIBODY; PROTEIN KINASE; PROTEIN TYROSINE KINASE; UNCLASSIFIED DRUG;

EID: 40649088574     PISSN: 0945053X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.matbio.2007.11.003     Document Type: Article
Times cited : (63)

References (88)
  • 4
    • 0031908852 scopus 로고    scopus 로고
    • Structure and biological activity of the extracellular matrix
    • Aumailley M., and Gayraud B. Structure and biological activity of the extracellular matrix. J. Mol. Med. 76 (1998) 253-265
    • (1998) J. Mol. Med. , vol.76 , pp. 253-265
    • Aumailley, M.1    Gayraud, B.2
  • 6
    • 0242270610 scopus 로고    scopus 로고
    • Membrane type-1 matrix metalloproteinase (MT1-MMP) processing of pro-alphav integrin regulates cross-talk between alphavbeta3 and alpha2beta1 integrins in breast carcinoma cells
    • Baciu P.C., Suleiman E.A., Deryugina E.I., and Strongin A.Y. Membrane type-1 matrix metalloproteinase (MT1-MMP) processing of pro-alphav integrin regulates cross-talk between alphavbeta3 and alpha2beta1 integrins in breast carcinoma cells. Exp. Cell Res. 291 (2003) 167-175
    • (2003) Exp. Cell Res. , vol.291 , pp. 167-175
    • Baciu, P.C.1    Suleiman, E.A.2    Deryugina, E.I.3    Strongin, A.Y.4
  • 7
    • 0038547793 scopus 로고    scopus 로고
    • Matrix metalloproteinase expression in breast cancer
    • Bartsch J.E., Staren E.D., and Appert H.E. Matrix metalloproteinase expression in breast cancer. J. Surg. Res. 110 (2003) 383-392
    • (2003) J. Surg. Res. , vol.110 , pp. 383-392
    • Bartsch, J.E.1    Staren, E.D.2    Appert, H.E.3
  • 8
    • 0031663622 scopus 로고    scopus 로고
    • Roles of the matrix metalloproteinases in mammary gland development and cancer
    • Benaud C., Dickson R.B., and Thompson E.W. Roles of the matrix metalloproteinases in mammary gland development and cancer. Breast Cancer Res. Treat. 50 (1998) 97-116
    • (1998) Breast Cancer Res. Treat. , vol.50 , pp. 97-116
    • Benaud, C.1    Dickson, R.B.2    Thompson, E.W.3
  • 10
    • 33745186855 scopus 로고    scopus 로고
    • Loss of beta4 integrin subunit reduces the tumorigenicity of MCF7 mammary cells and causes apoptosis upon hormone deprivation
    • Bon G., Folgiero V., Bossi G., Felicioni L., Marchetti A., Sacchi A., and Falcioni R. Loss of beta4 integrin subunit reduces the tumorigenicity of MCF7 mammary cells and causes apoptosis upon hormone deprivation. Clin. Cancer Res. 12 (2006) 3280-3287
    • (2006) Clin. Cancer Res. , vol.12 , pp. 3280-3287
    • Bon, G.1    Folgiero, V.2    Bossi, G.3    Felicioni, L.4    Marchetti, A.5    Sacchi, A.6    Falcioni, R.7
  • 12
    • 0028927484 scopus 로고
    • Suppression of ICE and apoptosis in mammary epithelial cells by extracellular matrix
    • Boudreau N., Sympson C.J., Werb Z., and Bissell M.J. Suppression of ICE and apoptosis in mammary epithelial cells by extracellular matrix. Science 267 (1995) 891-893
    • (1995) Science , vol.267 , pp. 891-893
    • Boudreau, N.1    Sympson, C.J.2    Werb, Z.3    Bissell, M.J.4
  • 13
    • 0029896163 scopus 로고    scopus 로고
    • Regulation, substrates and functions of Src
    • Brown M.T., and Cooper J.A. Regulation, substrates and functions of Src. Biochim. Biophys. Acta 1287 (1996) 121-149
    • (1996) Biochim. Biophys. Acta , vol.1287 , pp. 121-149
    • Brown, M.T.1    Cooper, J.A.2
  • 14
    • 0034044795 scopus 로고    scopus 로고
    • Immunohistochemical analyses of focal adhesion kinase expression in benign and malignant human breast and colon tissues: correlation with preinvasive and invasive phenotypes
    • Cance W.G., Harris J.E., Iacocca M.V., Roche E., Yang X., Chang J., Simkins S., and Xu L. Immunohistochemical analyses of focal adhesion kinase expression in benign and malignant human breast and colon tissues: correlation with preinvasive and invasive phenotypes. Clin. Cancer Res. 6 (2000) 2417-2423
    • (2000) Clin. Cancer Res. , vol.6 , pp. 2417-2423
    • Cance, W.G.1    Harris, J.E.2    Iacocca, M.V.3    Roche, E.4    Yang, X.5    Chang, J.6    Simkins, S.7    Xu, L.8
  • 15
    • 0031657969 scopus 로고    scopus 로고
    • Cell migration and MMP-9 secretion are increased by epidermal growth factor in HaCaT-ras transfected cells
    • Charvat S., Chignol M.C., Souchier C., Le Griel C., Schmitt D., and Serres M. Cell migration and MMP-9 secretion are increased by epidermal growth factor in HaCaT-ras transfected cells. Exp. Dermatol. 7 (1998) 184-190
    • (1998) Exp. Dermatol. , vol.7 , pp. 184-190
    • Charvat, S.1    Chignol, M.C.2    Souchier, C.3    Le Griel, C.4    Schmitt, D.5    Serres, M.6
  • 16
    • 0025728412 scopus 로고
    • Isolation and characterization of a 70-kDa metalloprotease (gelatinase) that is elevated in Rous sarcoma virus-transformed chicken embryo fibroblasts
    • Chen J.M., Aimes R.T., Ward G.R., Youngleib G.L., and Quigley J.P. Isolation and characterization of a 70-kDa metalloprotease (gelatinase) that is elevated in Rous sarcoma virus-transformed chicken embryo fibroblasts. J. Biol. Chem. 266 (1991) 5113-5121
    • (1991) J. Biol. Chem. , vol.266 , pp. 5113-5121
    • Chen, J.M.1    Aimes, R.T.2    Ward, G.R.3    Youngleib, G.L.4    Quigley, J.P.5
  • 17
    • 0037192458 scopus 로고    scopus 로고
    • Matrix metalloproteinase inhibitors and cancer: trials and tribulations
    • Coussens L.M., Fingleton B., and Matrisian L.M. Matrix metalloproteinase inhibitors and cancer: trials and tribulations. Science 295 (2002) 2387-2392
    • (2002) Science , vol.295 , pp. 2387-2392
    • Coussens, L.M.1    Fingleton, B.2    Matrisian, L.M.3
  • 18
    • 0032850365 scopus 로고    scopus 로고
    • Matrix metalloproteinases in tumour invasion and metastasis
    • Curran S., and Murray G.I. Matrix metalloproteinases in tumour invasion and metastasis. J. Pathol. 189 (1999) 300-308
    • (1999) J. Pathol. , vol.189 , pp. 300-308
    • Curran, S.1    Murray, G.I.2
  • 19
    • 0033624445 scopus 로고    scopus 로고
    • Matrix metalloproteinases: molecular aspects of their roles in tumour invasion and metastasis
    • Curran S., and Murray G.I. Matrix metalloproteinases: molecular aspects of their roles in tumour invasion and metastasis. Eur. J. Cancer 36 (2000) 1621-1630
    • (2000) Eur. J. Cancer , vol.36 , pp. 1621-1630
    • Curran, S.1    Murray, G.I.2
  • 20
    • 0030827411 scopus 로고    scopus 로고
    • Tumor cell invasion through matrigel is regulated by activated matrix metalloproteinase-2
    • Deryugina E.I., Luo G.X., Reisfeld R.A., Bourdon M.A., and Strongin A. Tumor cell invasion through matrigel is regulated by activated matrix metalloproteinase-2. Anticancer Res. 17 (1997) 3201-3210
    • (1997) Anticancer Res. , vol.17 , pp. 3201-3210
    • Deryugina, E.I.1    Luo, G.X.2    Reisfeld, R.A.3    Bourdon, M.A.4    Strongin, A.5
  • 22
    • 0036512208 scopus 로고    scopus 로고
    • New functions for the matrix metalloproteinases in cancer progression
    • Egeblad M., and Werb Z. New functions for the matrix metalloproteinases in cancer progression. Nat. Rev. Cancer 2 (2002) 161-174
    • (2002) Nat. Rev. Cancer , vol.2 , pp. 161-174
    • Egeblad, M.1    Werb, Z.2
  • 23
    • 5444219883 scopus 로고    scopus 로고
    • Matrix metalloproteinases in cancer: from new functions to improved inhibition strategies
    • Folgueras A.R., Pendas A.M., Sanchez L.M., and Lopez-Otin C. Matrix metalloproteinases in cancer: from new functions to improved inhibition strategies. Int. J. Dev. Biol. 48 (2004) 411-424
    • (2004) Int. J. Dev. Biol. , vol.48 , pp. 411-424
    • Folgueras, A.R.1    Pendas, A.M.2    Sanchez, L.M.3    Lopez-Otin, C.4
  • 26
    • 0032502667 scopus 로고    scopus 로고
    • Glomerular basement membrane. Identification of a novel disulfide-cross-linked network of alpha3, alpha4, and alpha5 chains of type IV collagen and its implications for the pathogenesis of Alport syndrome
    • Gunwar S., Ballester F., Noelken M.E., Sado Y., Ninomiya Y., and Hudson B.G. Glomerular basement membrane. Identification of a novel disulfide-cross-linked network of alpha3, alpha4, and alpha5 chains of type IV collagen and its implications for the pathogenesis of Alport syndrome. J. Biol. Chem. 273 (1998) 8767-8775
    • (1998) J. Biol. Chem. , vol.273 , pp. 8767-8775
    • Gunwar, S.1    Ballester, F.2    Noelken, M.E.3    Sado, Y.4    Ninomiya, Y.5    Hudson, B.G.6
  • 27
    • 0027954475 scopus 로고
    • Activation of the c-Src tyrosine kinase is required for the induction of mammary tumors in transgenic mice
    • Guy C.T., Muthuswamy S.K., Cardiff R.D., Soriano P., and Muller W.J. Activation of the c-Src tyrosine kinase is required for the induction of mammary tumors in transgenic mice. Genes Dev. 8 (1994) 23-32
    • (1994) Genes Dev. , vol.8 , pp. 23-32
    • Guy, C.T.1    Muthuswamy, S.K.2    Cardiff, R.D.3    Soriano, P.4    Muller, W.J.5
  • 29
    • 0018854046 scopus 로고
    • Electrophoretic analysis of plasminogen activators in polyacrylamide gels containing sodium dodecyl sulfate and copolymerized substrates
    • Heussen C., and Dowdle E.B. Electrophoretic analysis of plasminogen activators in polyacrylamide gels containing sodium dodecyl sulfate and copolymerized substrates. Anal. Biochem. 102 (1980) 196-202
    • (1980) Anal. Biochem. , vol.102 , pp. 196-202
    • Heussen, C.1    Dowdle, E.B.2
  • 30
    • 0037427072 scopus 로고    scopus 로고
    • Melanoma cell migration to type IV collagen requires activation of NF-kappaB
    • Hodgson L., Henderson A.J., and Dong C. Melanoma cell migration to type IV collagen requires activation of NF-kappaB. Oncogene 22 (2003) 98-108
    • (2003) Oncogene , vol.22 , pp. 98-108
    • Hodgson, L.1    Henderson, A.J.2    Dong, C.3
  • 31
    • 33747680992 scopus 로고    scopus 로고
    • Homophilic interactions of Tetraspanin CD151 up-regulate motility and matrix metalloproteinase-9 expression of human melanoma cells through adhesion-dependent c-Jun activation signaling pathways
    • Hong I.K., Jin Y.J., Byun H.J., Jeoung D.I., Kim Y.M., and Lee H. Homophilic interactions of Tetraspanin CD151 up-regulate motility and matrix metalloproteinase-9 expression of human melanoma cells through adhesion-dependent c-Jun activation signaling pathways. J. Biol. Chem. 281 (2006) 24279-24292
    • (2006) J. Biol. Chem. , vol.281 , pp. 24279-24292
    • Hong, I.K.1    Jin, Y.J.2    Byun, H.J.3    Jeoung, D.I.4    Kim, Y.M.5    Lee, H.6
  • 33
    • 0026770377 scopus 로고
    • Integrins: versatility, modulation, and signaling in cell adhesion
    • Hynes R.O. Integrins: versatility, modulation, and signaling in cell adhesion. Cell 69 (1992) 11-25
    • (1992) Cell , vol.69 , pp. 11-25
    • Hynes, R.O.1
  • 34
    • 0030037734 scopus 로고    scopus 로고
    • Production of matrix metalloproteinases and tissue inhibitors of metalloproteinases in human breast carcinomas
    • Iwata H., Kobayashi S., Iwase H., Masaoka A., Fujimoto N., and Okada Y. Production of matrix metalloproteinases and tissue inhibitors of metalloproteinases in human breast carcinomas. Jpn. J. Cancer Res. 87 (1996) 602-611
    • (1996) Jpn. J. Cancer Res. , vol.87 , pp. 602-611
    • Iwata, H.1    Kobayashi, S.2    Iwase, H.3    Masaoka, A.4    Fujimoto, N.5    Okada, Y.6
  • 35
    • 0032835899 scopus 로고    scopus 로고
    • Expression of MMP-2 and MMP-9, their inhibitors, and the activator MT1-MMP in primary breast carcinomas
    • Jones J.L., Glynn P., and Walker R.A. Expression of MMP-2 and MMP-9, their inhibitors, and the activator MT1-MMP in primary breast carcinomas. J. Pathol. 189 (1999) 161-168
    • (1999) J. Pathol. , vol.189 , pp. 161-168
    • Jones, J.L.1    Glynn, P.2    Walker, R.A.3
  • 36
    • 0027324296 scopus 로고
    • Role and regulation of expression of 92-kDa type-IV collagenase (MMP-9) in 2 invasive squamous-cell-carcinoma cell lines of the oral cavity
    • Juarez J., Clayman G., Nakajima M., Tanabe K.K., Saya H., Nicolson G.L., and Boyd D. Role and regulation of expression of 92-kDa type-IV collagenase (MMP-9) in 2 invasive squamous-cell-carcinoma cell lines of the oral cavity. Int. J. Cancer 55 (1993) 10-18
    • (1993) Int. J. Cancer , vol.55 , pp. 10-18
    • Juarez, J.1    Clayman, G.2    Nakajima, M.3    Tanabe, K.K.4    Saya, H.5    Nicolson, G.L.6    Boyd, D.7
  • 37
    • 0141482096 scopus 로고    scopus 로고
    • p38 kinase is a key signaling molecule for H-Ras-induced cell motility and invasive phenotype in human breast epithelial cells
    • Kim M.S., Lee E.J., Kim H.R., and Moon A. p38 kinase is a key signaling molecule for H-Ras-induced cell motility and invasive phenotype in human breast epithelial cells. Cancer Res. 63 (2003) 5454-5461
    • (2003) Cancer Res. , vol.63 , pp. 5454-5461
    • Kim, M.S.1    Lee, E.J.2    Kim, H.R.3    Moon, A.4
  • 38
    • 30644461913 scopus 로고    scopus 로고
    • Hirsutenone inhibits phorbol ester-induced upregulation of COX-2 and MMP-9 in cultured human mammary epithelial cells: NF-kappaB as a potential molecular target
    • Kim J.H., Lee K.W., Lee M.W., Lee H.J., Kim S.H., and Surh Y.J. Hirsutenone inhibits phorbol ester-induced upregulation of COX-2 and MMP-9 in cultured human mammary epithelial cells: NF-kappaB as a potential molecular target. FEBS Lett. 580 (2006) 385-392
    • (2006) FEBS Lett. , vol.580 , pp. 385-392
    • Kim, J.H.1    Lee, K.W.2    Lee, M.W.3    Lee, H.J.4    Kim, S.H.5    Surh, Y.J.6
  • 39
    • 0031657454 scopus 로고    scopus 로고
    • Focal adhesion kinase and its potential involvement in tumor invasion and metastasis
    • Kornberg L.J. Focal adhesion kinase and its potential involvement in tumor invasion and metastasis. Head Neck 20 (1998) 745-752
    • (1998) Head Neck , vol.20 , pp. 745-752
    • Kornberg, L.J.1
  • 40
    • 0029886352 scopus 로고    scopus 로고
    • Comparative analysis of the expression patterns of metalloproteinases and their inhibitors in breast neoplasia, sporadic colorectal neoplasia, pulmonary carcinomas and malignant non-Hodgkin's lymphomas in humans
    • Kossakowska A.E., Huchcroft S.A., Urbanski S.J., and Edwards D.R. Comparative analysis of the expression patterns of metalloproteinases and their inhibitors in breast neoplasia, sporadic colorectal neoplasia, pulmonary carcinomas and malignant non-Hodgkin's lymphomas in humans. Br. J. Cancer 73 (1996) 1401-1408
    • (1996) Br. J. Cancer , vol.73 , pp. 1401-1408
    • Kossakowska, A.E.1    Huchcroft, S.A.2    Urbanski, S.J.3    Edwards, D.R.4
  • 41
    • 0035902141 scopus 로고    scopus 로고
    • The microenvironment of the tumour-host interface
    • Liotta L.A., and Kohn E.C. The microenvironment of the tumour-host interface. Nature 411 (2001) 375-379
    • (2001) Nature , vol.411 , pp. 375-379
    • Liotta, L.A.1    Kohn, E.C.2
  • 42
    • 0026027556 scopus 로고
    • Cancer metastasis and angiogenesis: an imbalance of positive and negative regulation
    • Liotta L.A., Steeg P.S., and Stetler-Stevenson W.G. Cancer metastasis and angiogenesis: an imbalance of positive and negative regulation. Cell 64 (1991) 327-336
    • (1991) Cell , vol.64 , pp. 327-336
    • Liotta, L.A.1    Steeg, P.S.2    Stetler-Stevenson, W.G.3
  • 43
    • 0032513136 scopus 로고    scopus 로고
    • Inhibition of matrix metalloproteinase 2 maturation and HT1080 invasiveness by a synthetic furin inhibitor
    • Maquoi E., Noel A., Frankenne F., Angliker H., Murphy G., and Foidart J.M. Inhibition of matrix metalloproteinase 2 maturation and HT1080 invasiveness by a synthetic furin inhibitor. FEBS Lett. 424 (1998) 262-266
    • (1998) FEBS Lett. , vol.424 , pp. 262-266
    • Maquoi, E.1    Noel, A.2    Frankenne, F.3    Angliker, H.4    Murphy, G.5    Foidart, J.M.6
  • 45
    • 0024150414 scopus 로고
    • Extracellular matrix assembly
    • McDonald J.A. Extracellular matrix assembly. Annu. Rev. Cell Biol. 4 (1988) 183-207
    • (1988) Annu. Rev. Cell Biol. , vol.4 , pp. 183-207
    • McDonald, J.A.1
  • 46
    • 24744464071 scopus 로고    scopus 로고
    • Expression of MMP2, MMP9 and MMP3 in breast cancer brain metastasis in a rat model
    • Mendes O., Kim H.T., and Stoica G. Expression of MMP2, MMP9 and MMP3 in breast cancer brain metastasis in a rat model. Clin. Exp. Metastasis 22 (2005) 237-246
    • (2005) Clin. Exp. Metastasis , vol.22 , pp. 237-246
    • Mendes, O.1    Kim, H.T.2    Stoica, G.3
  • 48
    • 0028080914 scopus 로고
    • Promotion of cell adhesion by single-stranded and triple-helical peptide models of basement membrane collagen alpha 1(IV)531-543. Evidence for conformationally dependent and conformationally independent type IV collagen cell adhesion sites
    • Miles A.J., Skubitz A.P., Furcht L.T., and Fields G.B. Promotion of cell adhesion by single-stranded and triple-helical peptide models of basement membrane collagen alpha 1(IV)531-543. Evidence for conformationally dependent and conformationally independent type IV collagen cell adhesion sites. J. Biol. Chem. 269 (1994) 30939-30945
    • (1994) J. Biol. Chem. , vol.269 , pp. 30939-30945
    • Miles, A.J.1    Skubitz, A.P.2    Furcht, L.T.3    Fields, G.B.4
  • 49
    • 0035136029 scopus 로고    scopus 로고
    • Expression of metastasis-associated mts1 gene is co-induced with membrane type-1 matrix metalloproteinase (MT1-MMP) during oncogenic transformation and tubular formation of Madin Darby canine kidney (MDCK) epithelial cells
    • Miyamori H., Hasegawa K., Kim K.R., and Sato H. Expression of metastasis-associated mts1 gene is co-induced with membrane type-1 matrix metalloproteinase (MT1-MMP) during oncogenic transformation and tubular formation of Madin Darby canine kidney (MDCK) epithelial cells. Clin. Exp. Metastasis 18 (2000) 51-56
    • (2000) Clin. Exp. Metastasis , vol.18 , pp. 51-56
    • Miyamori, H.1    Hasegawa, K.2    Kim, K.R.3    Sato, H.4
  • 50
    • 33746122371 scopus 로고    scopus 로고
    • A role for focal adhesion kinase signaling in tumor necrosis factor-alpha-dependent matrix metalloproteinase-9 production in a cholangiocarcinoma cell line, CCKS1
    • Mon N.N., Hasegawa H., Thant A.A., Huang P., Tanimura Y., Senga T., and Hamaguchi M. A role for focal adhesion kinase signaling in tumor necrosis factor-alpha-dependent matrix metalloproteinase-9 production in a cholangiocarcinoma cell line, CCKS1. Cancer Res. 66 (2006) 6778-6784
    • (2006) Cancer Res. , vol.66 , pp. 6778-6784
    • Mon, N.N.1    Hasegawa, H.2    Thant, A.A.3    Huang, P.4    Tanimura, Y.5    Senga, T.6    Hamaguchi, M.7
  • 51
    • 0020056915 scopus 로고
    • The collagenase of Entamoeba histolytica
    • Munoz M.L., Calderon J., and Rojkind M. The collagenase of Entamoeba histolytica. J. Exp. Med. 155 (1982) 42-51
    • (1982) J. Exp. Med. , vol.155 , pp. 42-51
    • Munoz, M.L.1    Calderon, J.2    Rojkind, M.3
  • 52
    • 0032586951 scopus 로고    scopus 로고
    • Division of labor among the alpha6beta4 integrin, beta1 integrins, and an E3 laminin receptor to signal morphogenesis and beta-casein expression in mammary epithelial cells
    • Muschler J., Lochter A., Roskelley C.D., Yurchenco P., and Bissell M.J. Division of labor among the alpha6beta4 integrin, beta1 integrins, and an E3 laminin receptor to signal morphogenesis and beta-casein expression in mammary epithelial cells. Mol. Biol. Cell 10 (1999) 2817-2828
    • (1999) Mol. Biol. Cell , vol.10 , pp. 2817-2828
    • Muschler, J.1    Lochter, A.2    Roskelley, C.D.3    Yurchenco, P.4    Bissell, M.J.5
  • 53
    • 0032801783 scopus 로고    scopus 로고
    • Overexpression of tissue inhibitor of matrix metalloproteinases-1 (TIMP-1) in metastatic MDCK cells transformed by v-src
    • Noritake H., Miyamori H., Goto C., Seiki M., and Sato H. Overexpression of tissue inhibitor of matrix metalloproteinases-1 (TIMP-1) in metastatic MDCK cells transformed by v-src. Clin. Exp. Metastasis 17 (1999) 105-110
    • (1999) Clin. Exp. Metastasis , vol.17 , pp. 105-110
    • Noritake, H.1    Miyamori, H.2    Goto, C.3    Seiki, M.4    Sato, H.5
  • 54
    • 0026674221 scopus 로고
    • Characterization of protein tyrosine kinases from human breast cancer: involvement of the c-src oncogene product
    • Ottenhoff-Kalff A.E., Rijksen G., van Beurden E.A., Hennipman A., Michels A.A., and Staal G.E. Characterization of protein tyrosine kinases from human breast cancer: involvement of the c-src oncogene product. Cancer Res. 52 (1992) 4773-4778
    • (1992) Cancer Res. , vol.52 , pp. 4773-4778
    • Ottenhoff-Kalff, A.E.1    Rijksen, G.2    van Beurden, E.A.3    Hennipman, A.4    Michels, A.A.5    Staal, G.E.6
  • 56
    • 0034284266 scopus 로고    scopus 로고
    • Protein kinase C activation by phorbol ester increases in vitro invasion through regulation of matrix metalloproteinases/tissue inhibitors of metalloproteinases system in D54 human glioblastoma cells
    • Park M.J., Park I.C., Hur J.H., Rhee C.H., Choe T.B., Yi D.H., Hong S.I., and Lee S.H. Protein kinase C activation by phorbol ester increases in vitro invasion through regulation of matrix metalloproteinases/tissue inhibitors of metalloproteinases system in D54 human glioblastoma cells. Neurosci. Lett. 290 (2000) 201-204
    • (2000) Neurosci. Lett. , vol.290 , pp. 201-204
    • Park, M.J.1    Park, I.C.2    Hur, J.H.3    Rhee, C.H.4    Choe, T.B.5    Yi, D.H.6    Hong, S.I.7    Lee, S.H.8
  • 57
    • 1642302311 scopus 로고    scopus 로고
    • Activated Src increases adhesion, survival and alpha2-integrin expression in human breast cancer cells
    • Park H.B., Golubovskaya V., Xu L., Yang X., Lee J.W., Scully II S., Craven R.J., and Cance W.G. Activated Src increases adhesion, survival and alpha2-integrin expression in human breast cancer cells. Biochem J. 378 (2004) 559-567
    • (2004) Biochem J. , vol.378 , pp. 559-567
    • Park, H.B.1    Golubovskaya, V.2    Xu, L.3    Yang, X.4    Lee, J.W.5    Scully II, S.6    Craven, R.J.7    Cance, W.G.8
  • 58
    • 0029965695 scopus 로고    scopus 로고
    • Integrin-mediated signalling: regulation by protein tyrosine kinases and small GTP-binding proteins
    • Parsons J.T. Integrin-mediated signalling: regulation by protein tyrosine kinases and small GTP-binding proteins. Curr. Opin. Cell Biol. 8 (1996) 146-152
    • (1996) Curr. Opin. Cell Biol. , vol.8 , pp. 146-152
    • Parsons, J.T.1
  • 60
    • 9344271530 scopus 로고    scopus 로고
    • Expression of matrix metalloproteinase (MMP)-2 and MMP-9 in breast cancer with a special reference to activator protein-2, HER2, and prognosis
    • Pellikainen J.M., Ropponen K.M., Kataja V.V., Kellokoski J.K., Eskelinen M.J., and Kosma V.M. Expression of matrix metalloproteinase (MMP)-2 and MMP-9 in breast cancer with a special reference to activator protein-2, HER2, and prognosis. Clin. Cancer Res. 10 (2004) 7621-7628
    • (2004) Clin. Cancer Res. , vol.10 , pp. 7621-7628
    • Pellikainen, J.M.1    Ropponen, K.M.2    Kataja, V.V.3    Kellokoski, J.K.4    Eskelinen, M.J.5    Kosma, V.M.6
  • 61
    • 0029257377 scopus 로고
    • Signal transduction through integrins: a central role for focal adhesion kinase?
    • Richardson A., and Parsons J.T. Signal transduction through integrins: a central role for focal adhesion kinase?. Bioessays 17 (1995) 229-236
    • (1995) Bioessays , vol.17 , pp. 229-236
    • Richardson, A.1    Parsons, J.T.2
  • 62
    • 26644432498 scopus 로고    scopus 로고
    • Type IV collagen induces STAT5 activation in MCF7 human breast cancer cells
    • Robledo T., Arriaga-Pizano L., Lopez-Perez M., and Salazar E.P. Type IV collagen induces STAT5 activation in MCF7 human breast cancer cells. Matrix Biol. 24 (2005) 469-477
    • (2005) Matrix Biol. , vol.24 , pp. 469-477
    • Robledo, T.1    Arriaga-Pizano, L.2    Lopez-Perez, M.3    Salazar, E.P.4
  • 63
    • 0343340035 scopus 로고    scopus 로고
    • Phosphospecific antibodies reveal focal adhesion kinase activation loop phosphorylation in nascent and mature focal adhesions and requirement for the autophosphorylation site
    • Ruest P.J., Roy S., Shi E., Mernaugh R.L., and Hanks S.K. Phosphospecific antibodies reveal focal adhesion kinase activation loop phosphorylation in nascent and mature focal adhesions and requirement for the autophosphorylation site. Cell Growth Differ. 11 (2000) 41-48
    • (2000) Cell Growth Differ. , vol.11 , pp. 41-48
    • Ruest, P.J.1    Roy, S.2    Shi, E.3    Mernaugh, R.L.4    Hanks, S.K.5
  • 64
    • 0035947577 scopus 로고    scopus 로고
    • Src family kinases are required for integrin-mediated but not for G protein-coupled receptor stimulation of focal adhesion kinase autophosphorylation at Tyr-397
    • Salazar E.P., and Rozengurt E. Src family kinases are required for integrin-mediated but not for G protein-coupled receptor stimulation of focal adhesion kinase autophosphorylation at Tyr-397. J. Biol. Chem. 276 (2001) 17788-17795
    • (2001) J. Biol. Chem. , vol.276 , pp. 17788-17795
    • Salazar, E.P.1    Rozengurt, E.2
  • 65
    • 0034531398 scopus 로고    scopus 로고
    • Collagen IV-dependent ERK activation in human Caco-2 intestinal epithelial cells requires focal adhesion kinase
    • Sanders M.A., and Basson M.D. Collagen IV-dependent ERK activation in human Caco-2 intestinal epithelial cells requires focal adhesion kinase. J. Biol. Chem. 275 (2000) 38040-38047
    • (2000) J. Biol. Chem. , vol.275 , pp. 38040-38047
    • Sanders, M.A.1    Basson, M.D.2
  • 66
    • 0020008537 scopus 로고
    • Platelet-collagen adhesion
    • Santoro S.A., and Cunningham L.W. Platelet-collagen adhesion. Methods Enzymol. 82 Pt A (1982) 509-513
    • (1982) Methods Enzymol. , vol.82 , Issue.PART A , pp. 509-513
    • Santoro, S.A.1    Cunningham, L.W.2
  • 67
    • 0027438302 scopus 로고
    • v-Src activates the expression of 92-kDa type IV collagenase gene through the AP-1 site and the GT box homologous to retinoblastoma control elements. A mechanism regulating gene expression independent of that by inflammatory cytokines
    • Sato H., Kita M., and Seiki M. v-Src activates the expression of 92-kDa type IV collagenase gene through the AP-1 site and the GT box homologous to retinoblastoma control elements. A mechanism regulating gene expression independent of that by inflammatory cytokines. J. Biol. Chem. 268 (1993) 23460-23468
    • (1993) J. Biol. Chem. , vol.268 , pp. 23460-23468
    • Sato, H.1    Kita, M.2    Seiki, M.3
  • 68
    • 0035948579 scopus 로고    scopus 로고
    • Biochemical signals and biological responses elicited by the focal adhesion kinase
    • Schaller M.D. Biochemical signals and biological responses elicited by the focal adhesion kinase. Biochim. Biophys. Acta 1540 (2001) 1-21
    • (2001) Biochim. Biophys. Acta , vol.1540 , pp. 1-21
    • Schaller, M.D.1
  • 69
    • 0027439594 scopus 로고
    • Autonomous expression of a noncatalytic domain of the focal adhesion-associated protein tyrosine kinase pp125FAK
    • Schaller M.D., Borgman C.A., and Parsons J.T. Autonomous expression of a noncatalytic domain of the focal adhesion-associated protein tyrosine kinase pp125FAK. Mol. Cell Biol. 13 (1993) 785-791
    • (1993) Mol. Cell Biol. , vol.13 , pp. 785-791
    • Schaller, M.D.1    Borgman, C.A.2    Parsons, J.T.3
  • 72
    • 0032520916 scopus 로고    scopus 로고
    • Inhibition of the p38 mitogen-activated protein kinase by SB 203580 blocks PMA-induced Mr 92,000 type IV collagenase secretion and in vitro invasion
    • Simon C., Goepfert H., and Boyd D. Inhibition of the p38 mitogen-activated protein kinase by SB 203580 blocks PMA-induced Mr 92,000 type IV collagenase secretion and in vitro invasion. Cancer Res. 58 (1998) 1135-1139
    • (1998) Cancer Res. , vol.58 , pp. 1135-1139
    • Simon, C.1    Goepfert, H.2    Boyd, D.3
  • 73
    • 0028306295 scopus 로고
    • 72 KD and 92 KD type IV collagenase, type IV collagen, and laminin mRNAs in breast cancer: a study by in situ hybridization
    • Soini Y., Hurskainen T., Hoyhtya M., Oikarinen A., and Autio-Harmainen H. 72 KD and 92 KD type IV collagenase, type IV collagen, and laminin mRNAs in breast cancer: a study by in situ hybridization. J. Histochem. Cytochem. 42 (1994) 945-951
    • (1994) J. Histochem. Cytochem. , vol.42 , pp. 945-951
    • Soini, Y.1    Hurskainen, T.2    Hoyhtya, M.3    Oikarinen, A.4    Autio-Harmainen, H.5
  • 74
    • 32244434925 scopus 로고    scopus 로고
    • Plasma concentration and activity of matrix metalloproteinase 2 and 9 in patients with breast disease, breast cancer and at risk of developing breast cancer
    • Somiari S.B., Shriver C.D., Heckman C., Olsen C., Hu H., Jordan R., Arciero C., Russell S., Garguilo G., Hooke J., and Somiari R.I. Plasma concentration and activity of matrix metalloproteinase 2 and 9 in patients with breast disease, breast cancer and at risk of developing breast cancer. Cancer Lett. 233 (2006) 98-107
    • (2006) Cancer Lett. , vol.233 , pp. 98-107
    • Somiari, S.B.1    Shriver, C.D.2    Heckman, C.3    Olsen, C.4    Hu, H.5    Jordan, R.6    Arciero, C.7    Russell, S.8    Garguilo, G.9    Hooke, J.10    Somiari, R.I.11
  • 76
    • 0035188727 scopus 로고    scopus 로고
    • How matrix metalloproteinases regulate cell behavior
    • Sternlicht M.D., and Werb Z. How matrix metalloproteinases regulate cell behavior. Annu. Rev. Cell Dev. Biol. 17 (2001) 463-516
    • (2001) Annu. Rev. Cell Dev. Biol. , vol.17 , pp. 463-516
    • Sternlicht, M.D.1    Werb, Z.2
  • 77
    • 0036595629 scopus 로고    scopus 로고
    • Epithelial-mesenchymal transitions in tumour progression
    • Thiery J.P. Epithelial-mesenchymal transitions in tumour progression. Nat. Rev. Cancer 2 (2002) 442-454
    • (2002) Nat. Rev. Cancer , vol.2 , pp. 442-454
    • Thiery, J.P.1
  • 78
    • 22244492306 scopus 로고    scopus 로고
    • Carcinoma invasion and metastasis: a role for epithelial-mesenchymal transition?
    • discussion 5995
    • Thompson E.W., Newgreen D.F., and Tarin D. Carcinoma invasion and metastasis: a role for epithelial-mesenchymal transition?. Cancer Res. 65 (2005) 5991-5995 discussion 5995
    • (2005) Cancer Res. , vol.65 , pp. 5991-5995
    • Thompson, E.W.1    Newgreen, D.F.2    Tarin, D.3
  • 81
    • 0038700554 scopus 로고    scopus 로고
    • Host microenvironment in breast cancer development: epithelial-mesenchymal transition in breast cancer development
    • Vincent-Salomon A., and Thiery J.P. Host microenvironment in breast cancer development: epithelial-mesenchymal transition in breast cancer development. Breast Cancer Res. 5 (2003) 101-106
    • (2003) Breast Cancer Res. , vol.5 , pp. 101-106
    • Vincent-Salomon, A.1    Thiery, J.P.2
  • 82
    • 0029964065 scopus 로고    scopus 로고
    • src-related tyrosine kinases regulate transcriptional activation of the interstitial collagenase gene, MMP-1, in interleukin-1-stimulated synovial fibroblasts
    • Vincenti M.P., Coon C.I., White L.A., Barchowsky A., and Brinckerhoff C.E. src-related tyrosine kinases regulate transcriptional activation of the interstitial collagenase gene, MMP-1, in interleukin-1-stimulated synovial fibroblasts. Arthritis Rheum. 39 (1996) 574-582
    • (1996) Arthritis Rheum. , vol.39 , pp. 574-582
    • Vincenti, M.P.1    Coon, C.I.2    White, L.A.3    Barchowsky, A.4    Brinckerhoff, C.E.5
  • 83
    • 0031965888 scopus 로고    scopus 로고
    • V-src activation of the collagenase-1 (matrix metalloproteinase-1) promoter through PEA3 and STAT: requirement of extracellular signal-regulated kinases and inhibition by retinoic acid receptors
    • Vincenti M.P., Schroen D.J., Coon C.I., and Brinckerhoff C.E. V-src activation of the collagenase-1 (matrix metalloproteinase-1) promoter through PEA3 and STAT: requirement of extracellular signal-regulated kinases and inhibition by retinoic acid receptors. Mol. Carcinog. 21 (1998) 194-204
    • (1998) Mol. Carcinog. , vol.21 , pp. 194-204
    • Vincenti, M.P.1    Schroen, D.J.2    Coon, C.I.3    Brinckerhoff, C.E.4
  • 84
    • 13644270390 scopus 로고    scopus 로고
    • SHP-2 promoting migration and metastasis of MCF-7 with loss of E-cadherin, dephosphorylation of FAK and secretion of MMP-9 induced by IL-1beta in vivo and in vitro
    • Wang F.M., Liu H.Q., Liu S.R., Tang S.P., Yang L., and Feng G.S. SHP-2 promoting migration and metastasis of MCF-7 with loss of E-cadherin, dephosphorylation of FAK and secretion of MMP-9 induced by IL-1beta in vivo and in vitro. Breast Cancer Res. Treat. 89 (2005) 5-14
    • (2005) Breast Cancer Res. Treat. , vol.89 , pp. 5-14
    • Wang, F.M.1    Liu, H.Q.2    Liu, S.R.3    Tang, S.P.4    Yang, L.5    Feng, G.S.6
  • 85
    • 0036726312 scopus 로고    scopus 로고
    • Beta4 integrin-dependent formation of polarized three-dimensional architecture confers resistance to apoptosis in normal and malignant mammary epithelium
    • Weaver V.M., Lelievre S., Lakins J.N., Chrenek M.A., Jones J.C., Giancotti F., Werb Z., and Bissell M.J. Beta4 integrin-dependent formation of polarized three-dimensional architecture confers resistance to apoptosis in normal and malignant mammary epithelium. Cancer Cell 2 (2002) 205-216
    • (2002) Cancer Cell , vol.2 , pp. 205-216
    • Weaver, V.M.1    Lelievre, S.2    Lakins, J.N.3    Chrenek, M.A.4    Jones, J.C.5    Giancotti, F.6    Werb, Z.7    Bissell, M.J.8
  • 86
    • 0026473835 scopus 로고
    • Type IV collagen of Engelbreth-Holm-Swarm tumor matrix: identification of constituent chains
    • Wisdom Jr. B.J., Gunwar S., Hudson M.D., Noelken M.E., and Hudson B.G. Type IV collagen of Engelbreth-Holm-Swarm tumor matrix: identification of constituent chains. Connect Tissue Res. 27 (1992) 225-234
    • (1992) Connect Tissue Res. , vol.27 , pp. 225-234
    • Wisdom Jr., B.J.1    Gunwar, S.2    Hudson, M.D.3    Noelken, M.E.4    Hudson, B.G.5
  • 87
    • 2942618768 scopus 로고    scopus 로고
    • A renaissance for SRC
    • Yeatman T.J. A renaissance for SRC. Nat. Rev. Cancer 4 (2004) 470-480
    • (2004) Nat. Rev. Cancer , vol.4 , pp. 470-480
    • Yeatman, T.J.1
  • 88
    • 0027787888 scopus 로고
    • Role of alpha 3 beta 1 and alpha 2 beta 1 integrins in melanoma cell migration
    • Yoshinaga I.G., Vink J., Dekker S.K., Mihm Jr. M.C., and Byers H.R. Role of alpha 3 beta 1 and alpha 2 beta 1 integrins in melanoma cell migration. Melanoma Res. 3 (1993) 435-441
    • (1993) Melanoma Res. , vol.3 , pp. 435-441
    • Yoshinaga, I.G.1    Vink, J.2    Dekker, S.K.3    Mihm Jr., M.C.4    Byers, H.R.5


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