메뉴 건너뛰기




Volumn 41, Issue 12, 2008, Pages 858-862

Caveolin-1 inhibits membrane-type 1 matrix metalloproteinase activity

Author keywords

Caveolin 1; Cell migration; Collagen degradation; MMP 2; MT1 MMP

Indexed keywords


EID: 58149354851     PISSN: 12258687     EISSN: 02191024     Source Type: Journal    
DOI: 10.5483/bmbrep.2008.41.12.858     Document Type: Article
Times cited : (24)

References (20)
  • 1
    • 0033618337 scopus 로고    scopus 로고
    • Matrix metalloproteinases
    • Nagase, H. and Woessner, J.F., Jr. (1999) Matrix metalloproteinases.J. Biol. Chem. 274, 21491-21494.
    • (1999) J. Biol. Chem , vol.274 , pp. 21491-21494
    • Nagase, H.1    Woessner Jr., J.F.2
  • 2
    • 0028291737 scopus 로고
    • A matrix metalloproteinase expressed on the surface of invasive tumour cells
    • Sato, H., Takino, T., Okada, Y., Cao, J., Shinagawa, A., Yamamoto, E. and Seiki, M. (1994) A matrix metalloproteinase expressed on the surface of invasive tumour cells. Nature 370, 61-65.
    • (1994) Nature , vol.370 , pp. 61-65
    • Sato, H.1    Takino, T.2    Okada, Y.3    Cao, J.4    Shinagawa, A.5    Yamamoto, E.6    Seiki, M.7
  • 3
    • 0036512208 scopus 로고    scopus 로고
    • New functions for the matrix metalloproteinases in cancer progression
    • Egeblad, M. and Werb, Z. (2002) New functions for the matrix metalloproteinases in cancer progression. Nat. Rev. Cancer 2, 161-174.
    • (2002) Nat. Rev. Cancer , vol.2 , pp. 161-174
    • Egeblad, M.1    Werb, Z.2
  • 4
    • 0033944447 scopus 로고    scopus 로고
    • Regulation of membrane type-1 matrix metalloproteinase activation by proprotein convertases
    • Yana, I. and Weiss, S.J. (2000) Regulation of membrane type-1 matrix metalloproteinase activation by proprotein convertases. Mol. Biol. Cell 11, 2387-2401.
    • (2000) Mol. Biol. Cell , vol.11 , pp. 2387-2401
    • Yana, I.1    Weiss, S.J.2
  • 5
    • 0037063349 scopus 로고    scopus 로고
    • The cytoplasmic tail peptide sequence of membrane type-1 matrix metalloproteinase (MT1-MMP) directly binds to gC1qR, a compartment-specific chaperone-like regulatory protein
    • Rozanov, D.V., Ghebrehiwet, B., Ratnikov, B., Monosov, E.Z., Deryugina, E.I. and Strongin, A.Y, (2002) The cytoplasmic tail peptide sequence of membrane type-1 matrix metalloproteinase (MT1-MMP) directly binds to gC1qR, a compartment-specific chaperone-like regulatory protein. FEBS. Lett. 527, 51-57.
    • (2002) FEBS. Lett , vol.527 , pp. 51-57
    • Rozanov, D.V.1    Ghebrehiwet, B.2    Ratnikov, B.3    Monosov, E.Z.4    Deryugina, E.I.5    Strongin, A.Y.6
  • 6
    • 1842790801 scopus 로고    scopus 로고
    • Distinct roles for the catalytic and hemopexin domains of membrane type 1-matrix metalloproteinase in substrate degradation and cell migration
    • Cao, J., Kozarekar, P., Pavlaki, M., Chiarelli, C., Bahou, W.F. and Zucker, S. (2004) Distinct roles for the catalytic and hemopexin domains of membrane type 1-matrix metalloproteinase in substrate degradation and cell migration. J. Biol. Chem. 279, 14129-14139.
    • (2004) J. Biol. Chem , vol.279 , pp. 14129-14139
    • Cao, J.1    Kozarekar, P.2    Pavlaki, M.3    Chiarelli, C.4    Bahou, W.F.5    Zucker, S.6
  • 8
    • 0031727149 scopus 로고    scopus 로고
    • The activation of ProMMP-2 (gelatinase A) by HT1080 fibrosarcoma cells is promoted by culture on a fibronectin substrate and is concomitant with an increase in processing of MT1-MMP (MMP-14) to a 45 kDa form
    • Stanton, H., Gavrilovic, J., Atkinson, S.J., d' Ortho, M.P., Yamada, K.M., Zardi, L. and Murphy, G. (1998) The activation of ProMMP-2 (gelatinase A) by HT1080 fibrosarcoma cells is promoted by culture on a fibronectin substrate and is concomitant with an increase in processing of MT1-MMP (MMP-14) to a 45 kDa form. J. Cell Set. 111 (Pt 18), 2789-2798.
    • (1998) J. Cell Set , vol.111 , Issue.PART 18 , pp. 2789-2798
    • Stanton, H.1    Gavrilovic, J.2    Atkinson, S.J.3    d' Ortho, M.P.4    Yamada, K.M.5    Zardi, L.6    Murphy, G.7
  • 9
    • 0035252979 scopus 로고    scopus 로고
    • Localization of membrane-type 1 matrix metalloproteinase in caveolae membrane domains
    • Annabi, B., Lachambre, M., Bousquet-Gagnon, N., Page, M., Gingras, D. and Beliveau, R. (2001) Localization of membrane-type 1 matrix metalloproteinase in caveolae membrane domains. Biochem. J. 353, 547-553.
    • (2001) Biochem. J , vol.353 , pp. 547-553
    • Annabi, B.1    Lachambre, M.2    Bousquet-Gagnon, N.3    Page, M.4    Gingras, D.5    Beliveau, R.6
  • 10
    • 41149124594 scopus 로고    scopus 로고
    • Caveolae as organizers of pharmacologically relevant signal transduction molecules
    • Patel, H.H., Murray, F. and Insel, P.A. (2008) Caveolae as organizers of pharmacologically relevant signal transduction molecules. Annu. Rev. Pharmacol. Toxicol. 48, 359-391.
    • (2008) Annu. Rev. Pharmacol. Toxicol , vol.48 , pp. 359-391
    • Patel, H.H.1    Murray, F.2    Insel, P.A.3
  • 11
    • 3142582011 scopus 로고    scopus 로고
    • Caveolins: Structure and function in signal transduction
    • Krajewska, W.M. and Maslowska, I. (2004) Caveolins: structure and function in signal transduction. Cell Mol. Biol. Lett. 9, 195-220.
    • (2004) Cell Mol. Biol. Lett , vol.9 , pp. 195-220
    • Krajewska, W.M.1    Maslowska, I.2
  • 12
    • 0033945943 scopus 로고    scopus 로고
    • Caveolin proteins in signaling, oncogenic transformation and muscular dystrophy
    • Razani, B., Schlegel, A. and Lisanti, M.P. (2000) Caveolin proteins in signaling, oncogenic transformation and muscular dystrophy. J. Cell Sci. 113 (P112), 2103-2109.
    • (2000) J. Cell Sci , vol.113 , Issue.P112 , pp. 2103-2109
    • Razani, B.1    Schlegel, A.2    Lisanti, M.P.3
  • 13
    • 0036830114 scopus 로고    scopus 로고
    • Multiple functions of caveolin-1. j
    • Liu, P., Rudick, M. and Anderson, R.G. (2002) Multiple functions of caveolin-1. j. Biol. Chem. 277, 41295-41298.
    • (2002) Biol. Chem , vol.277 , pp. 41295-41298
    • Liu, P.1    Rudick, M.2    Anderson, R.G.3
  • 14
    • 10644229956 scopus 로고    scopus 로고
    • Src-mediated tyrosine phosphorylation of caveolin-1 induces its association with membrane type 1 matrix metalloproteinase
    • Labrecque, L., Nyalendo, C., Langlois, S., Durocher, Y., Roghi, C., Murphy, G., Gingras, D. and Beliveau, R. (2004) Src-mediated tyrosine phosphorylation of caveolin-1 induces its association with membrane type 1 matrix metalloproteinase. J. Biol. Chem. 279, 52132-52140.
    • (2004) J. Biol. Chem , vol.279 , pp. 52132-52140
    • Labrecque, L.1    Nyalendo, C.2    Langlois, S.3    Durocher, Y.4    Roghi, C.5    Murphy, G.6    Gingras, D.7    Beliveau, R.8
  • 15
    • 2442483850 scopus 로고    scopus 로고
    • Cellular cholesterol regulates MT1 MMP dependent activation of MMP 2 via MEK-1 in HT1080 fibrosarcoma cells
    • Atkinson, S.J., English, J.L., Holway, N. and Murphy, G. (2004) Cellular cholesterol regulates MT1 MMP dependent activation of MMP 2 via MEK-1 in HT1080 fibrosarcoma cells. FEBS. Lett. 566, 65-70.
    • (2004) FEBS. Lett , vol.566 , pp. 65-70
    • Atkinson, S.J.1    English, J.L.2    Holway, N.3    Murphy, G.4
  • 16
    • 0347951043 scopus 로고    scopus 로고
    • Aberrant, persistent inclusion into lipid rafts limits the tumorigenic function of membrane type-1 matrix metalloproteinase in malignant cells
    • Rozanov, D.V., Deryugina, E.I., Monosov, E.Z., Marchenko, N.D. and Strongin, A.Y. (2004) Aberrant, persistent inclusion into lipid rafts limits the tumorigenic function of membrane type-1 matrix metalloproteinase in malignant cells. Exp. Cell Res. 293, 81-95.
    • (2004) Exp. Cell Res , vol.293 , pp. 81-95
    • Rozanov, D.V.1    Deryugina, E.I.2    Monosov, E.Z.3    Marchenko, N.D.4    Strongin, A.Y.5
  • 17
    • 0028907318 scopus 로고
    • Mechanism of cell surface activation of 72-kDa type IV collagenase. Isolation of the activated form of the membrane metalloprotease
    • Strongin, A.Y., Collier, I., Bannikov, G., Marmer, B.L., Grant, G.A. and Goldberg, G.I. (1995) Mechanism of cell surface activation of 72-kDa type IV collagenase. Isolation of the activated form of the membrane metalloprotease. J. Biol. Chem. 270, 5331-5338.
    • (1995) J. Biol. Chem , vol.270 , pp. 5331-5338
    • Strongin, A.Y.1    Collier, I.2    Bannikov, G.3    Marmer, B.L.4    Grant, G.A.5    Goldberg, G.I.6
  • 18
    • 2142784516 scopus 로고    scopus 로고
    • Holmbeck, K., Bianco, P., Caterina, J., Yamada, S., Kromer, M., Kuznetsov, S.A., Mankani, M., Robey, P.G., Poole, A.R., Pidoux, I., Ward, J.M. and Birkedal-Hansen, H. (1999) MT1-MMP-deficient mice develop dwarfism, osteopenia, arthritis, and connective tissue disease due to inadequate collagen turnover. Cell 99, 81-92.
    • Holmbeck, K., Bianco, P., Caterina, J., Yamada, S., Kromer, M., Kuznetsov, S.A., Mankani, M., Robey, P.G., Poole, A.R., Pidoux, I., Ward, J.M. and Birkedal-Hansen, H. (1999) MT1-MMP-deficient mice develop dwarfism, osteopenia, arthritis, and connective tissue disease due to inadequate collagen turnover. Cell 99, 81-92.
  • 19
    • 0035801473 scopus 로고    scopus 로고
    • Homophilic complex formation of MT1-MMP facilitates proMMP-2 activation on the cell surface and promotes tumor cell invasion
    • Itoh, Y., Takamura, A., Ito, N., Maru, Y., Sato, H., Suenaga, N., Aoki, T. and Seiki, M. (2001) Homophilic complex formation of MT1-MMP facilitates proMMP-2 activation on the cell surface and promotes tumor cell invasion. EMBO J. 20, 4782-4793.
    • (2001) EMBO J , vol.20 , pp. 4782-4793
    • Itoh, Y.1    Takamura, A.2    Ito, N.3    Maru, Y.4    Sato, H.5    Suenaga, N.6    Aoki, T.7    Seiki, M.8
  • 20
    • 0027172634 scopus 로고
    • Plasma membrane-dependent activation of the 72-kDa type IV collagenase is prevented by complex formation with TlMP-2
    • Strongin, A.Y., Marmer, B.L., Grant, G.A. and Goldberg, G.I. (1993) Plasma membrane-dependent activation of the 72-kDa type IV collagenase is prevented by complex formation with TlMP-2. J. Biol. Chem. 268, 14033-14039.
    • (1993) J. Biol. Chem , vol.268 , pp. 14033-14039
    • Strongin, A.Y.1    Marmer, B.L.2    Grant, G.A.3    Goldberg, G.I.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.