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Volumn 95, Issue 7, 2013, Pages 1371-1378

ADAM9 silencing inhibits breast tumor cell invasion in vitro

Author keywords

ADAM9; Cancer; Cell adhesion; Disintegrin; Integrin; Metastasis; RNA silencing

Indexed keywords

A DISINTEGRIN AND METALLOPROTEASE 9 PROTEIN; ADAM PROTEIN; GELATINASE A; GELATINASE B; MATRIGEL; MESSENGER RNA; SMALL INTERFERING RNA; UNCLASSIFIED DRUG;

EID: 84878545072     PISSN: 03009084     EISSN: 61831638     Source Type: Journal    
DOI: 10.1016/j.biochi.2013.03.001     Document Type: Article
Times cited : (20)

References (48)
  • 1
    • 0026770377 scopus 로고
    • Integrins: Versatility, modulation, and signaling in cell adhesion
    • R.O. Hynes Integrins: versatility, modulation, and signaling in cell adhesion Cell 69 1992 11 25
    • (1992) Cell , vol.69 , pp. 11-25
    • Hynes, R.O.1
  • 2
    • 0028047388 scopus 로고
    • Focal adhesion as a signal transduction organelle
    • S.H. Lo, and L.B. Chen Focal adhesion as a signal transduction organelle Cancer Metastasis Rev. 13 1994 9 24
    • (1994) Cancer Metastasis Rev. , vol.13 , pp. 9-24
    • Lo, S.H.1    Chen, L.B.2
  • 5
    • 0027682591 scopus 로고
    • Adhesion molecules in cancer: The role of integrins
    • R.L. Juliano, and J.A. Varner Adhesion molecules in cancer: the role of integrins Curr. Opin. Cell. Biol. 5 1993 812 818
    • (1993) Curr. Opin. Cell. Biol. , vol.5 , pp. 812-818
    • Juliano, R.L.1    Varner, J.A.2
  • 6
    • 79951519159 scopus 로고    scopus 로고
    • Active metalloproteases of the A disintegrin and metalloprotease (ADAM) family: Biological function and structure
    • T. Klein, and R. Bischoff Active metalloproteases of the A disintegrin and metalloprotease (ADAM) family: biological function and structure J. Proteome Res. 10 2011 17 33
    • (2011) J. Proteome Res. , vol.10 , pp. 17-33
    • Klein, T.1    Bischoff, R.2
  • 8
    • 0028820623 scopus 로고
    • ADAM, a novel family of membrane proteins containing A disintegrin and metalloprotease domain: Multipotential functions in cell-cell and cell-matrix interactions
    • T.G. Wolfsberg, P. Primakoff, D.G. Myles, and J.M. White ADAM, a novel family of membrane proteins containing A disintegrin and metalloprotease domain: multipotential functions in cell-cell and cell-matrix interactions J. Cell. Biol. 131 1995 275 278
    • (1995) J. Cell. Biol. , vol.131 , pp. 275-278
    • Wolfsberg, T.G.1    Primakoff, P.2    Myles, D.G.3    White, J.M.4
  • 9
    • 0033933982 scopus 로고    scopus 로고
    • Meltrin gamma (ADAM-9) mediates cellular adhesion through alpha(6)beta(1)integrin, leading to a marked induction of fibroblast cell motility
    • D. Nath, P.M. Slocombe, A. Webster, P.E. Stephens, A.J. Docherty, and G. Murphy Meltrin gamma (ADAM-9) mediates cellular adhesion through alpha(6)beta(1)integrin, leading to a marked induction of fibroblast cell motility J. Cell Sci. 113 2000 2319 2328
    • (2000) J. Cell Sci. , vol.113 , pp. 2319-2328
    • Nath, D.1    Slocombe, P.M.2    Webster, A.3    Stephens, P.E.4    Docherty, A.J.5    Murphy, G.6
  • 10
    • 0034811643 scopus 로고    scopus 로고
    • MDC-9 (ADAM-9/meltrin gamma) functions as an adhesion molecule by binding the alpha(v)beta(5) integrin
    • M. Zhou, R. Graham, G. Russell, and P.I. Croucher MDC-9 (ADAM-9/meltrin gamma) functions as an adhesion molecule by binding the alpha(v)beta(5) integrin Biochem. Biophys. Res. Commun. 280 2001 574 580
    • (2001) Biochem. Biophys. Res. Commun. , vol.280 , pp. 574-580
    • Zhou, M.1    Graham, R.2    Russell, G.3    Croucher, P.I.4
  • 11
    • 67649656106 scopus 로고    scopus 로고
    • Inhibition of platelets and tumor cell adhesion by the disintegrin domain of human ADAM9 to collagen i under dynamic flow conditions
    • M.R. Cominetti, A.C. Martin, J.U. Ribeiro, I. Djaafri, F. Fauvel-Lafeve, M. Crepin, and H.S. Selistre-de-Araujo Inhibition of platelets and tumor cell adhesion by the disintegrin domain of human ADAM9 to collagen I under dynamic flow conditions Biochimie 91 2009 1045 1052
    • (2009) Biochimie , vol.91 , pp. 1045-1052
    • Cominetti, M.R.1    Martin, A.C.2    Ribeiro, J.U.3    Djaafri, I.4    Fauvel-Lafeve, F.5    Crepin, M.6    Selistre-De-Araujo, H.S.7
  • 12
    • 12844285639 scopus 로고    scopus 로고
    • The disintegrin domain of ADAM9: A ligand for multiple beta1 renal integrins
    • R.M. Mahimkar, O. Visaya, A.S. Pollock, and D.H. Lovett The disintegrin domain of ADAM9: a ligand for multiple beta1 renal integrins Biochem. J. 385 2005 461 468
    • (2005) Biochem. J. , vol.385 , pp. 461-468
    • Mahimkar, R.M.1    Visaya, O.2    Pollock, A.S.3    Lovett, D.H.4
  • 14
    • 79953198272 scopus 로고    scopus 로고
    • The disintegrin-like and cysteine-rich domains of ADAM-9 mediate interactions between melanoma cells and fibroblasts
    • P. Zigrino, R. Nischt, and C. Mauch The disintegrin-like and cysteine-rich domains of ADAM-9 mediate interactions between melanoma cells and fibroblasts J. Biol. Chem. 286 2011 6801 6807
    • (2011) J. Biol. Chem. , vol.286 , pp. 6801-6807
    • Zigrino, P.1    Nischt, R.2    Mauch, C.3
  • 19
    • 77954442704 scopus 로고    scopus 로고
    • Increased expression of a disintegrin and metalloprotease-9 in hepatocellular carcinoma: Implications for tumor progression and prognosis
    • K. Tao, N. Qian, Y. Tang, Z. Ti, W. Song, D. Cao, and K. Dou Increased expression of a disintegrin and metalloprotease-9 in hepatocellular carcinoma: implications for tumor progression and prognosis Jpn. J. Clin. Oncol. 40 2010 645 651
    • (2010) Jpn. J. Clin. Oncol. , vol.40 , pp. 645-651
    • Tao, K.1    Qian, N.2    Tang, Y.3    Ti, Z.4    Song, W.5    Cao, D.6    Dou, K.7
  • 21
    • 19644374948 scopus 로고    scopus 로고
    • The disintegrin-metalloproteinases ADAM9, ADAM12, and ADAM15 are upregulated in gastric cancer
    • S. Carl-McGrath, U. Lendeckel, M. Ebert, A. Roessner, and C. Rocken The disintegrin-metalloproteinases ADAM9, ADAM12, and ADAM15 are upregulated in gastric cancer Int. J. Oncol. 26 2005 17 24
    • (2005) Int. J. Oncol. , vol.26 , pp. 17-24
    • Carl-Mcgrath, S.1    Lendeckel, U.2    Ebert, M.3    Roessner, A.4    Rocken, C.5
  • 22
    • 67549094635 scopus 로고    scopus 로고
    • Expression of ADAM9 in CIN3 lesions and squamous cell carcinomas of the cervix
    • A. Zubel, C. Flechtenmacher, L. Edler, and A. Alonso Expression of ADAM9 in CIN3 lesions and squamous cell carcinomas of the cervix Gynecol. Oncol. 114 2009 332 336
    • (2009) Gynecol. Oncol. , vol.114 , pp. 332-336
    • Zubel, A.1    Flechtenmacher, C.2    Edler, L.3    Alonso, A.4
  • 23
    • 77953277942 scopus 로고    scopus 로고
    • RNAi-mediated ADAM9 gene silencing inhibits metastasis of adenoid cystic carcinoma cells
    • Q. Xu, X. Liu, Y. Cai, Y. Yu, and W. Chen RNAi-mediated ADAM9 gene silencing inhibits metastasis of adenoid cystic carcinoma cells Tumour Biol. 31 2010 217 224
    • (2010) Tumour Biol. , vol.31 , pp. 217-224
    • Xu, Q.1    Liu, X.2    Cai, Y.3    Yu, Y.4    Chen, W.5
  • 24
    • 23944436853 scopus 로고    scopus 로고
    • Adam-9 expression and regulation in human skin melanoma and melanoma cell lines
    • P. Zigrino, C. Mauch, J.W. Fox, and R. Nischt Adam-9 expression and regulation in human skin melanoma and melanoma cell lines Int. J. Cancer 116 2005 853 859
    • (2005) Int. J. Cancer , vol.116 , pp. 853-859
    • Zigrino, P.1    Mauch, C.2    Fox, J.W.3    Nischt, R.4
  • 26
    • 12844287338 scopus 로고    scopus 로고
    • Steroid hormones, polypeptide growth factors, hormone refractory prostate cancer, and the neuroendocrine phenotype
    • A.I. Evangelou, S.F. Winter, W.J. Huss, R.A. Bok, and N.M. Greenberg Steroid hormones, polypeptide growth factors, hormone refractory prostate cancer, and the neuroendocrine phenotype J. Cell. Biochem. 91 2004 671 683
    • (2004) J. Cell. Biochem. , vol.91 , pp. 671-683
    • Evangelou, A.I.1    Winter, S.F.2    Huss, W.J.3    Bok, R.A.4    Greenberg, N.M.5
  • 27
    • 0036680093 scopus 로고    scopus 로고
    • Down-regulation of (IIIb) and (IIIc) isoforms of fibroblast growth factor receptor 2 (FGFR2) is associated with malignant progression in human prostate
    • B. Naimi, A. Latil, G. Fournier, P. Mangin, O. Cussenot, and P. Berthon Down-regulation of (IIIb) and (IIIc) isoforms of fibroblast growth factor receptor 2 (FGFR2) is associated with malignant progression in human prostate Prostate 52 2002 245 252
    • (2002) Prostate , vol.52 , pp. 245-252
    • Naimi, B.1    Latil, A.2    Fournier, G.3    Mangin, P.4    Cussenot, O.5    Berthon, P.6
  • 28
    • 0032053825 scopus 로고    scopus 로고
    • Inhibition of growth of malignant rat prostate tumor cells by restoration of fibroblast growth factor receptor 2
    • A. Matsubara, M. Kan, S. Feng, and W.L. McKeehan Inhibition of growth of malignant rat prostate tumor cells by restoration of fibroblast growth factor receptor 2 Cancer Res. 58 1998 1509 1514
    • (1998) Cancer Res. , vol.58 , pp. 1509-1514
    • Matsubara, A.1    Kan, M.2    Feng, S.3    McKeehan, W.L.4
  • 32
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • U.K. Laemmli Cleavage of structural proteins during the assembly of the head of bacteriophage T4 Nature 227 1970 680 685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 33
    • 0021061819 scopus 로고
    • Rapid colorimetric assay for cellular growth and survival: Application to proliferation and cytotoxicity assays
    • T. Mosmann Rapid colorimetric assay for cellular growth and survival: application to proliferation and cytotoxicity assays J. Immunol. Methods 65 1983 55 63
    • (1983) J. Immunol. Methods , vol.65 , pp. 55-63
    • Mosmann, T.1
  • 34
    • 77952326078 scopus 로고    scopus 로고
    • A simplified method for quantifying cell migration/wound healing in 96-well plates
    • P.Y. Yue, E.P. Leung, N.K. Mak, and R.N. Wong A simplified method for quantifying cell migration/wound healing in 96-well plates J. Biomol. Screen. 15 2010 427 433
    • (2010) J. Biomol. Screen. , vol.15 , pp. 427-433
    • Yue, P.Y.1    Leung, E.P.2    Mak, N.K.3    Wong, R.N.4
  • 36
    • 0036488589 scopus 로고    scopus 로고
    • Role of integrins in cell invasion and migration
    • J.D. Hood, and D.A. Cheresh Role of integrins in cell invasion and migration Nat. Rev. Cancer 2 2002 91 100
    • (2002) Nat. Rev. Cancer , vol.2 , pp. 91-100
    • Hood, J.D.1    Cheresh, D.A.2
  • 37
    • 52049111209 scopus 로고    scopus 로고
    • Integrins in breast cancer dormancy
    • S.M. Pontier, and W.J. Muller Integrins in breast cancer dormancy APMIS 116 2008 677 684
    • (2008) APMIS , vol.116 , pp. 677-684
    • Pontier, S.M.1    Muller, W.J.2
  • 38
    • 34147105872 scopus 로고    scopus 로고
    • ADAMs in cancer cell proliferation and progression
    • S. Mochizuki, and Y. Okada ADAMs in cancer cell proliferation and progression Cancer Sci. 98 2007 621 628
    • (2007) Cancer Sci. , vol.98 , pp. 621-628
    • Mochizuki, S.1    Okada, Y.2
  • 39
    • 63049110385 scopus 로고    scopus 로고
    • EGFR and ADAMs cooperate to regulate shedding and endocytic trafficking of the desmosomal cadherin desmoglein 2
    • J.L. Klessner, B.V. Desai, E.V. Amargo, S. Getsios, and K.J. Green EGFR and ADAMs cooperate to regulate shedding and endocytic trafficking of the desmosomal cadherin desmoglein 2 Mol. Biol. Cell. 20 2009 328 337
    • (2009) Mol. Biol. Cell. , vol.20 , pp. 328-337
    • Klessner, J.L.1    Desai, B.V.2    Amargo, E.V.3    Getsios, S.4    Green, K.J.5
  • 41
    • 78049244413 scopus 로고    scopus 로고
    • Secreted and membrane-bound isoforms of protease ADAM9 have opposing effects on breast cancer cell migration
    • J.L. Fry, and A. Toker Secreted and membrane-bound isoforms of protease ADAM9 have opposing effects on breast cancer cell migration Cancer Res. 70 2010 8187 8198
    • (2010) Cancer Res. , vol.70 , pp. 8187-8198
    • Fry, J.L.1    Toker, A.2
  • 42
    • 0038581051 scopus 로고    scopus 로고
    • TACE cleavage of proamphiregulin regulates GPCR-induced proliferation and motility of cancer cells
    • A. Gschwind, S. Hart, O.M. Fischer, and A. Ullrich TACE cleavage of proamphiregulin regulates GPCR-induced proliferation and motility of cancer cells EMBO J. 22 2003 2411 2421
    • (2003) EMBO J. , vol.22 , pp. 2411-2421
    • Gschwind, A.1    Hart, S.2    Fischer, O.M.3    Ullrich, A.4
  • 44
    • 17444373968 scopus 로고    scopus 로고
    • A metalloprotease-disintegrin, MDC9/meltrin-gamma/ADAM9 and PKCdelta are involved in TPA-induced ectodomain shedding of membrane-anchored heparin-binding EGF-like growth factor
    • Y. Izumi, M. Hirata, H. Hasuwa, R. Iwamoto, T. Umata, K. Miyado, Y. Tamai, T. Kurisaki, A. Sehara-Fujisawa, S. Ohno, and E. Mekada A metalloprotease-disintegrin, MDC9/meltrin-gamma/ADAM9 and PKCdelta are involved in TPA-induced ectodomain shedding of membrane-anchored heparin-binding EGF-like growth factor EMBO J. 17 1998 7260 7272
    • (1998) EMBO J. , vol.17 , pp. 7260-7272
    • Izumi, Y.1    Hirata, M.2    Hasuwa, H.3    Iwamoto, R.4    Umata, T.5    Miyado, K.6    Tamai, Y.7    Kurisaki, T.8    Sehara-Fujisawa, A.9    Ohno, S.10    Mekada, E.11
  • 45
    • 14744304878 scopus 로고    scopus 로고
    • ADAM-integrin interactions: Potential integrin regulated ectodomain shedding activity
    • L.C. Bridges, and R.D. Bowditch ADAM-integrin interactions: potential integrin regulated ectodomain shedding activity Curr. Pharm. Des. 11 2005 837 847
    • (2005) Curr. Pharm. Des. , vol.11 , pp. 837-847
    • Bridges, L.C.1    Bowditch, R.D.2
  • 47
    • 0034105403 scopus 로고    scopus 로고
    • Identification, cellular distribution and potential function of the metalloprotease-disintegrin MDC9 in the kidney
    • R.M. Mahimkar, W.H. Baricos, O. Visaya, A.S. Pollock, and D.H. Lovett Identification, cellular distribution and potential function of the metalloprotease-disintegrin MDC9 in the kidney J. Am. Soc. Nephrol. 11 2000 595 603
    • (2000) J. Am. Soc. Nephrol. , vol.11 , pp. 595-603
    • Mahimkar, R.M.1    Baricos, W.H.2    Visaya, O.3    Pollock, A.S.4    Lovett, D.H.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.