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Volumn 36, Issue 10, 2000, Pages 1258-1268

Interactions between tumour cells and stromal cells and proteolytic modification of the extracellular matrix by metalloproteinases in cancer

Author keywords

Extracellular matrix; Metalloproteinases; Tissue inhibitor of metalloproteinases; Tumour invasion

Indexed keywords

DISINTEGRIN; MATRIX METALLOPROTEINASE; METALLOPROTEINASE; TISSUE INHIBITOR OF METALLOPROTEINASE;

EID: 0034123653     PISSN: 09598049     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0959-8049(00)00094-0     Document Type: Conference Paper
Times cited : (122)

References (92)
  • 1
    • 0022656975 scopus 로고
    • Tumor invasion and metastases-role of the extracellular matrix: Rhoads Memorial Award lecture
    • Liotta LA. Tumor invasion and metastases-role of the extracellular matrix: Rhoads Memorial Award lecture. Cancer Res 1986, 46, 1-7.
    • (1986) Cancer Res , vol.46 , pp. 1-7
    • Liotta, L.A.1
  • 2
    • 0019195010 scopus 로고
    • Metastatic potential correlates with enzymatic degradation of basement membrane collagen
    • Liotta LA, Tryggvason K, Garbisa S, Hart I, Foltz CM, Shafie S. Metastatic potential correlates with enzymatic degradation of basement membrane collagen. Nature 1980, 284, 67-68.
    • (1980) Nature , vol.284 , pp. 67-68
    • Liotta, L.A.1    Tryggvason, K.2    Garbisa, S.3    Hart, I.4    Foltz, C.M.5    Shafie, S.6
  • 3
    • 0022450555 scopus 로고
    • Primary rat embryo cells transformed by one or two oncogenes show different metastatic potentials
    • Pozzatti R, Muschel RJ, Williams J, et al. Primary rat embryo cells transformed by one or two oncogenes show different metastatic potentials. Science 1986, 232, 223-227.
    • (1986) Science , vol.232 , pp. 223-227
    • Pozzatti, R.1    Muschel, R.J.2    Williams, J.3
  • 4
    • 0024195894 scopus 로고
    • Type IV collagenolytic activity linkage with the metastatic phenotype induced by ras transfection
    • Garbisa S, Negro A, Kalebic T, et al. Type IV collagenolytic activity linkage with the metastatic phenotype induced by ras transfection. Adv Exp Med Biol 1988, 233, 179-186.
    • (1988) Adv Exp Med Biol , vol.233 , pp. 179-186
    • Garbisa, S.1    Negro, A.2    Kalebic, T.3
  • 5
    • 0025413394 scopus 로고
    • Cathepsin B and cystatins: Evidence for a role in cancer progression
    • Sloane BF. Cathepsin B and cystatins: evidence for a role in cancer progression. Semin Cancer Biol 1990, 1, 137-152.
    • (1990) Semin Cancer Biol , vol.1 , pp. 137-152
    • Sloane, B.F.1
  • 6
    • 0023270938 scopus 로고
    • Degradation of basement membrane type IV collagen and lung subendothelial matrix by rat mammary adenocarcinoma cell clones of differing metastatic potentials
    • Nakajima M, Welch DR, Belloni PN, Nicolson GL. Degradation of basement membrane type IV collagen and lung subendothelial matrix by rat mammary adenocarcinoma cell clones of differing metastatic potentials. Cancer Res 1987, 47, 4869-4876.
    • (1987) Cancer Res , vol.47 , pp. 4869-4876
    • Nakajima, M.1    Welch, D.R.2    Belloni, P.N.3    Nicolson, G.L.4
  • 7
    • 0003931970 scopus 로고    scopus 로고
    • Barrett AJ, Rawlings ND, Woessner JF, eds. Academic Press
    • Barrett AJ, Rawlings ND, Woessner JF, eds. Handbook of Proteolytic Enzymes. Academic Press, 1998.
    • (1998) Handbook of Proteolytic Enzymes
  • 8
    • 0033618337 scopus 로고    scopus 로고
    • Matrix metalloproteinases
    • Nagase H, Woessner JF. Matrix metalloproteinases. J Biol Chem 1999, 274, 21491-21494.
    • (1999) J Biol Chem , vol.274 , pp. 21491-21494
    • Nagase, H.1    Woessner, J.F.2
  • 11
    • 0026793281 scopus 로고
    • Differential expression of metalloproteinase and tissue inhibitor of metalloproteinase genes in aged human fibroblasts
    • Millis AJ, Hoyle M, McCue HM, Martini H. Differential expression of metalloproteinase and tissue inhibitor of metalloproteinase genes in aged human fibroblasts. Exp Cell Res 1992, 201, 373-379.
    • (1992) Exp Cell Res , vol.201 , pp. 373-379
    • Millis, A.J.1    Hoyle, M.2    McCue, H.M.3    Martini, H.4
  • 12
    • 0030957218 scopus 로고    scopus 로고
    • Activation mechanisms of matrix metalloproteinases
    • Nagase H. Activation mechanisms of matrix metalloproteinases. Biol Chem Hoppe Seyler 1997, 378, 151-160.
    • (1997) Biol Chem Hoppe Seyler , vol.378 , pp. 151-160
    • Nagase, H.1
  • 13
    • 0025653088 scopus 로고
    • Integrins and tumor invasion
    • Dedhar S. Integrins and tumor invasion. Bioessays 1990, 12, 583-590.
    • (1990) Bioessays , vol.12 , pp. 583-590
    • Dedhar, S.1
  • 14
    • 0028794828 scopus 로고
    • Activation of precursors for matrix metalloproteinases 1 (interstitial collagenase) and 3 (stromelysin) by rat mast-cell proteinases I and II
    • Suzuki K, Lees M, Newlands GFJ, Nagase H, Woolley DE. Activation of precursors for matrix metalloproteinases 1 (interstitial collagenase) and 3 (stromelysin) by rat mast-cell proteinases I and II. Blochem J 1995, 305, 301-306.
    • (1995) Blochem J , vol.305 , pp. 301-306
    • Suzuki, K.1    Lees, M.2    Newlands, G.F.J.3    Nagase, H.4    Woolley, D.E.5
  • 16
    • 0025837660 scopus 로고
    • Binding of latent and high Mr active forms of stromelysin to collagen is mediated by the C-terminal domain
    • Allan JA, Hembry RM, Angal S, Reynolds JJ, Murphy G. Binding of latent and high Mr active forms of stromelysin to collagen is mediated by the C-terminal domain. J Cell Sci 1991, 99, 789-795.
    • (1991) J Cell Sci , vol.99 , pp. 789-795
    • Allan, J.A.1    Hembry, R.M.2    Angal, S.3    Reynolds, J.J.4    Murphy, G.5
  • 17
    • 0342502272 scopus 로고    scopus 로고
    • The C-terminal (haemopexin-like) domain structure of human gelatinase A (MMP2): Structural implications for its function
    • Gohlke U, Gomis Ruth FX, Crabbe T, Murphy G, Docherty AJ, Bode W. The C-terminal (haemopexin-like) domain structure of human gelatinase A (MMP2): structural implications for its function. FEES Lett 1996, 378, 126-130.
    • (1996) FEES Lett , vol.378 , pp. 126-130
    • Gohlke, U.1    Gomis Ruth, F.X.2    Crabbe, T.3    Murphy, G.4    Docherty, A.J.5    Bode, W.6
  • 18
    • 0343812072 scopus 로고    scopus 로고
    • Relating matrix metalloproteinase structure to function: Why the "hemopexin" domain?
    • Murphy G, Knäuper V. Relating matrix metalloproteinase structure to function: why the "hemopexin" domain? Matrix Biol 1997, 15, 511-518.
    • (1997) Matrix Biol , vol.15 , pp. 511-518
    • Murphy, G.1    Knäuper, V.2
  • 19
    • 15844420283 scopus 로고    scopus 로고
    • Localization of matrix metalloproteinase MMP-2 to the surface of invasive cells by interaction with integrin alpha v beta 3
    • Brooks PC, Stromblad S, Sanders LC, et al. Localization of matrix metalloproteinase MMP-2 to the surface of invasive cells by interaction with integrin alpha v beta 3. Cell 1996, 85, 683-693.
    • (1996) Cell , vol.85 , pp. 683-693
    • Brooks, P.C.1    Stromblad, S.2    Sanders, L.C.3
  • 20
    • 0022254467 scopus 로고
    • Tumorpromoting phorbol esters and cell proliferation stimulate secretion of basement membrane (type IV) collagen-degrading metalloproteinase by human fibroblasts
    • Salo T, Turpeenniemi Hujanen T, Tryggvason K. Tumorpromoting phorbol esters and cell proliferation stimulate secretion of basement membrane (type IV) collagen-degrading metalloproteinase by human fibroblasts. J Biol Chem 1985, 260, 8526-8531.
    • (1985) J Biol Chem , vol.260 , pp. 8526-8531
    • Salo, T.1    Turpeenniemi Hujanen, T.2    Tryggvason, K.3
  • 21
    • 0023919959 scopus 로고
    • H-ras oncogenetransformed human bronchial epithelial cells (TBE-1) secrete a single metalloprotease capable of degrading basement membrane collagen
    • Collier IE, Wilhelm SM, Eisen AZ, et al. H-ras oncogenetransformed human bronchial epithelial cells (TBE-1) secrete a single metalloprotease capable of degrading basement membrane collagen. J Biol Chem 1988, 263, 6579-6587.
    • (1988) J Biol Chem , vol.263 , pp. 6579-6587
    • Collier, I.E.1    Wilhelm, S.M.2    Eisen, A.Z.3
  • 22
    • 0006506596 scopus 로고
    • Human 72-kilodalton type IV collagenase forms a complex with a tissue inhibitor of metalloproteases designated TIMP-2
    • Goldberg GI, Marmer BL, Grant GA, Eisen AZ, Wilhelm S, He CS. Human 72-kilodalton type IV collagenase forms a complex with a tissue inhibitor of metalloproteases designated TIMP-2. Proc Natl Acad Sci USA 1989, 86, 8207-8211.
    • (1989) Proc Natl Acad Sci USA , vol.86 , pp. 8207-8211
    • Goldberg, G.I.1    Marmer, B.L.2    Grant, G.A.3    Eisen, A.Z.4    Wilhelm, S.5    He, C.S.6
  • 24
    • 0028291737 scopus 로고
    • A matrix metalloproteinase expressed on the surface of invasive tumour cells
    • Sato H, Takino T, Okada Y, et al. A matrix metalloproteinase expressed on the surface of invasive tumour cells. Nature 1994, 370, 61-65.
    • (1994) Nature , vol.370 , pp. 61-65
    • Sato, H.1    Takino, T.2    Okada, Y.3
  • 25
    • 0029014101 scopus 로고
    • Furin-dependent intracellular activation of the human stromelysin-3 zymogen
    • Pei D, Weiss SJ. Furin-dependent intracellular activation of the human stromelysin-3 zymogen. Nature 1995, 375, 244-247.
    • (1995) Nature , vol.375 , pp. 244-247
    • Pei, D.1    Weiss, S.J.2
  • 26
    • 0028907318 scopus 로고
    • Mechanism of cell surface activation of 72-kDa type IV collagenase. Isolation of the activated form of the membrane metalloprotease
    • Strongin AY, Collier I, Bannikov G, Marmer BL, Grant GA, Goldberg GI. Mechanism of cell surface activation of 72-kDa type IV collagenase. Isolation of the activated form of the membrane metalloprotease. J Biol Chem 1995, 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
  • 27
    • 0032568932 scopus 로고    scopus 로고
    • TIMP-2 promotes activation of progelatinase a by membrane-type 1 matrix metalloproteinase immobilized on agarose beads
    • Kinoshita T, Sato H, Okada A, et al. TIMP-2 promotes activation of progelatinase a by membrane-type 1 matrix metalloproteinase immobilized on agarose beads. J Biol Chem 1998, 273, 16098-16103.
    • (1998) J Biol Chem , vol.273 , pp. 16098-16103
    • Kinoshita, T.1    Sato, H.2    Okada, A.3
  • 28
    • 0033214433 scopus 로고    scopus 로고
    • Regulation of intestinal α-defensin activation by the metalloproteinase matrilysin in innate host defense
    • Wilson CL, Ouellette AJ, Satchell DP, et al. Regulation of intestinal α-defensin activation by the metalloproteinase matrilysin in innate host defense. Science 1999, 286, 113-117.
    • (1999) Science , vol.286 , pp. 113-117
    • Wilson, C.L.1    Ouellette, A.J.2    Satchell, D.P.3
  • 29
    • 0032534596 scopus 로고    scopus 로고
    • Matrix metalloproteinases generate angiostatin: Effects on neovascularization
    • Cornelius LA, Nehring LC, Harding E, et al. Matrix metalloproteinases generate angiostatin: effects on neovascularization. J Immunol 1998, 161, 6845-6852.
    • (1998) J Immunol , vol.161 , pp. 6845-6852
    • Cornelius, L.A.1    Nehring, L.C.2    Harding, E.3
  • 30
    • 0022382006 scopus 로고
    • Sequence of human tissue inhibitor of metalloproteinases and its identify to erythroidpotentiating activity
    • Docherty AJ, Lyons A, Smith BJ, et al. Sequence of human tissue inhibitor of metalloproteinases and its identify to erythroidpotentiating activity. Nature 1985, 318, 66-69.
    • (1985) Nature , vol.318 , pp. 66-69
    • Docherty, A.J.1    Lyons, A.2    Smith, B.J.3
  • 31
    • 0025304303 scopus 로고
    • cDNA cloning and expression of a metalloproteinase inhibitor related to tissue inhibitor of metalloproteinases
    • Boone TC, Johnson MJ, DeClerck YA, Langley KE. cDNA cloning and expression of a metalloproteinase inhibitor related to tissue inhibitor of metalloproteinases. Proc Natl Acad Sci USA 1990, 87, 2800-2804.
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 2800-2804
    • Boone, T.C.1    Johnson, M.J.2    Declerck, Y.A.3    Langley, K.E.4
  • 32
    • 0028125576 scopus 로고
    • Cloning of the cDNA encoding human tissue inhibitor of metalloproteinases-3 (TIMP-3) and mapping of the TIMP3 gene to chromosome 22
    • Apte SS, Mattei MG, Olsen BR. Cloning of the cDNA encoding human tissue inhibitor of metalloproteinases-3 (TIMP-3) and mapping of the TIMP3 gene to chromosome 22. Genomics 1994, 19, 86-90.
    • (1994) Genomics , vol.19 , pp. 86-90
    • Apte, S.S.1    Mattei, M.G.2    Olsen, B.R.3
  • 33
    • 0029806813 scopus 로고    scopus 로고
    • Molecular cloning and characterization of human tissue inhibitor of metalloproteinase 4
    • Greene J, Wang M, Liu YE, Raymond LA, Rosen C, Shi YE. Molecular cloning and characterization of human tissue inhibitor of metalloproteinase 4. J Biol Chem 1996, 271, 30375-30380.
    • (1996) J Biol Chem , vol.271 , pp. 30375-30380
    • Greene, J.1    Wang, M.2    Liu, Y.E.3    Raymond, L.A.4    Rosen, C.5    Shi, Y.E.6
  • 34
    • 0027269425 scopus 로고
    • Structural analysis of tissue inhibitor of metalloproteinases-1 (TIMP-1) by tryptic peptide mapping
    • Williamson RA, Smith BJ, Angal S, Murphy G, Freedman RB. Structural analysis of tissue inhibitor of metalloproteinases-1 (TIMP-1) by tryptic peptide mapping. Biochim Biophys Acta 1993, 1164, 8-16.
    • (1993) Biochim Biophys Acta , vol.1164 , pp. 8-16
    • Williamson, R.A.1    Smith, B.J.2    Angal, S.3    Murphy, G.4    Freedman, R.B.5
  • 35
    • 1842377505 scopus 로고    scopus 로고
    • Mechanism of inhibition of the human matrix metalloproteinase stromelysin-1 by TIMP-1
    • Gomis-Rüth FX, Maskos K, Betz M, et al. Mechanism of inhibition of the human matrix metalloproteinase stromelysin-1 by TIMP-1. Nature 1997, 389, 77-81.
    • (1997) Nature , vol.389 , pp. 77-81
    • Gomis-Rüth, F.X.1    Maskos, K.2    Betz, M.3
  • 36
    • 0025944065 scopus 로고
    • The N-terminal domain of tissue inhibitor of metalloproteinases retains metalloproteinase inhibitory activity
    • Murphy G, Houbrechts A, Cockett MI, Williamson RA, O'Shea M, Docherty AJ. The N-terminal domain of tissue inhibitor of metalloproteinases retains metalloproteinase inhibitory activity. Biochemistry 1991, 30, 8097-8102.
    • (1991) Biochemistry , vol.30 , pp. 8097-8102
    • Murphy, G.1    Houbrechts, A.2    Cockett, M.I.3    Williamson, R.A.4    O'Shea, M.5    Docherty, A.J.6
  • 37
    • 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
    • Wolfsberg TG, Primakoff P, Myles DG, White JM. 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 1995, 131, 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
  • 38
    • 0029045064 scopus 로고
    • ADAM, a widely distributed and developmentally regulated gene family encoding membrane proteins with a disintegrin and metalloprotease domain
    • Wolfsberg TG, Straight PD, Gerena RL, et al. ADAM, a widely distributed and developmentally regulated gene family encoding membrane proteins with a disintegrin and metalloprotease domain. Dev Biol 1995, 169, 378-383.
    • (1995) Dev Biol , vol.169 , pp. 378-383
    • Wolfsberg, T.G.1    Straight, P.D.2    Gerena, R.L.3
  • 39
    • 0032809940 scopus 로고    scopus 로고
    • Structure-function analysis of the ADAM family of disintegrin-like and metalloproteinase containing proteins (review)
    • Stone AL, Kroeger M, Sang QXA. Structure-function analysis of the ADAM family of disintegrin-like and metalloproteinase containing proteins (review). J Protein Chem 1999, 18, 447-465.
    • (1999) J Protein Chem , vol.18 , pp. 447-465
    • Stone, A.L.1    Kroeger, M.2    Sang, Q.X.A.3
  • 40
    • 0031698581 scopus 로고    scopus 로고
    • ADAMs: Focus on the protease domain
    • Black RA, White JM. ADAMs: focus on the protease domain. Curr Opin Cell Biol 1998, 10, 654-659.
    • (1998) Curr Opin Cell Biol , vol.10 , pp. 654-659
    • Black, R.A.1    White, J.M.2
  • 41
    • 0032508675 scopus 로고    scopus 로고
    • TNF-α converting enzyme (TACE) is inhibited by TIMP-3
    • Amour A, Slocombe PM, Webster A, et al. TNF-α converting enzyme (TACE) is inhibited by TIMP-3. FEES Lett 1998, 435, 39-44.
    • (1998) FEES Lett , vol.435 , pp. 39-44
    • Amour, A.1    Slocombe, P.M.2    Webster, A.3
  • 42
    • 0032815883 scopus 로고    scopus 로고
    • Adamalysins. A family of metzincins including TNF-alpha converting enzyme (TACE)
    • Killar L, White J, Black R, Peschon J. Adamalysins. A family of metzincins including TNF-alpha converting enzyme (TACE). Ann NY Acad Sci 1999, 878, 442-452.
    • (1999) Ann NY Acad Sci , vol.878 , pp. 442-452
    • Killar, L.1    White, J.2    Black, R.3    Peschon, J.4
  • 43
    • 8044257704 scopus 로고    scopus 로고
    • A metalloproteinase disintegrin that releases tumour-necrosis factor-a from cells
    • Black RA, Rauch CT, Kozlosky CJ, et al. A metalloproteinase disintegrin that releases tumour-necrosis factor-a from cells. Nature 1997, 385, 729-733.
    • (1997) Nature , vol.385 , pp. 729-733
    • Black, R.A.1    Rauch, C.T.2    Kozlosky, C.J.3
  • 44
    • 0029788321 scopus 로고    scopus 로고
    • KUZ, a conserved metalloprotease-disintegrin protein with two roles in Drosophila neurogenesis
    • Rooke J, Pan D, Xu T, Rubin GM. KUZ, a conserved metalloprotease-disintegrin protein with two roles in Drosophila neurogenesis. Science 1996, 273, 1227-1231.
    • (1996) Science , vol.273 , pp. 1227-1231
    • Rooke, J.1    Pan, D.2    Xu, T.3    Rubin, G.M.4
  • 45
    • 0032908446 scopus 로고    scopus 로고
    • Cysteine-rich domain of human ADAM 12 (meltrin alpha) supports tumor cell adhesion
    • Iba K, Albrechtsen R, Gilpin BJ, Loechel F, Wewer UM. Cysteine-rich domain of human ADAM 12 (meltrin alpha) supports tumor cell adhesion. Am J Pathol 1999, 154, 1489-1501.
    • (1999) Am J Pathol , vol.154 , pp. 1489-1501
    • Iba, K.1    Albrechtsen, R.2    Gilpin, B.J.3    Loechel, F.4    Wewer, U.M.5
  • 46
    • 0031801882 scopus 로고    scopus 로고
    • Human metalloprotease-disintegrin Kuzbanian regulates sympathoadrenal cell fate in development and neoplasia
    • Yavari R, Adida C, Bray-Ward P, Brines M, Xu T. Human metalloprotease-disintegrin Kuzbanian regulates sympathoadrenal cell fate in development and neoplasia. Hum Mol Genet 1998, 7, 1161-1167.
    • (1998) Hum Mol Genet , vol.7 , pp. 1161-1167
    • Yavari, R.1    Adida, C.2    Bray-Ward, P.3    Brines, M.4    Xu, T.5
  • 47
    • 0031577162 scopus 로고    scopus 로고
    • Expression of members of the novel membrane linked metalloproteinase family ADAM in cells derived from a range of haematological malignancies
    • Wu E, Croucher PI, McKie N. Expression of members of the novel membrane linked metalloproteinase family ADAM in cells derived from a range of haematological malignancies. Biochem Biophys Res Commun 1997, 235, 437-442.
    • (1997) Biochem Biophys Res Commun , vol.235 , pp. 437-442
    • Wu, E.1    Croucher, P.I.2    McKie, N.3
  • 48
    • 0033603356 scopus 로고    scopus 로고
    • ADAMTS-1 is an active metalloproteinase associated extracellular matrix
    • Kuno K, Terashima Y, Matsushima K. ADAMTS-1 is an active metalloproteinase associated extracellular matrix. J Biol Chem 1999, 274, 18821-18826.
    • (1999) J Biol Chem , vol.274 , pp. 18821-18826
    • Kuno, K.1    Terashima, Y.2    Matsushima, K.3
  • 49
    • 0033551844 scopus 로고    scopus 로고
    • Cloning and characterization of ADAMTS11, an aggrecanase from the ADAMTS family
    • Abbaszade I, Liu RQ, Yang F, et al. Cloning and characterization of ADAMTS11, an aggrecanase from the ADAMTS family. J Biol Chem 1999, 274, 23443-23450.
    • (1999) J Biol Chem , vol.274 , pp. 23443-23450
    • Abbaszade, I.1    Liu, R.Q.2    Yang, F.3
  • 50
    • 0345211445 scopus 로고    scopus 로고
    • Purification and cloning of aggrecanase-1: A member of the ADAMTS family of proteins
    • Tortorella MD, Burn TC, Pratta MA, et al. Purification and cloning of aggrecanase-1: a member of the ADAMTS family of proteins. Science 1999, 284, 1664-1666.
    • (1999) Science , vol.284 , pp. 1664-1666
    • Tortorella, M.D.1    Burn, T.C.2    Pratta, M.A.3
  • 51
    • 0038757017 scopus 로고    scopus 로고
    • METH-1, a human ortholog of ADAMTS-1, and METH-2 are members of a new family of proteins with angio-inhibitory activity
    • Vazquez F, Hastings G, Ortega MA, et al. METH-1, a human ortholog of ADAMTS-1, and METH-2 are members of a new family of proteins with angio-inhibitory activity. J Biol Chem 1999, 274, 23349-23357.
    • (1999) J Biol Chem , vol.274 , pp. 23349-23357
    • Vazquez, F.1    Hastings, G.2    Ortega, M.A.3
  • 52
    • 0026646159 scopus 로고
    • Stromal expression of 72 kda type IV collagenase (MMP-2) and TIMP-2 mRNAs in colorectal neoplasia
    • Poulsom R, Pignatelli M, Stetler-Stevenson WG, et al. Stromal expression of 72 kda type IV collagenase (MMP-2) and TIMP-2 mRNAs in colorectal neoplasia. Am J Pathol 1992, 141, 389-396.
    • (1992) Am J Pathol , vol.141 , pp. 389-396
    • Poulsom, R.1    Pignatelli, M.2    Stetler-Stevenson, W.G.3
  • 53
    • 0027076036 scopus 로고
    • Expression of the stromelysin-3 gene in fibroblastic cells of invasive carcinomas of the breast and other human tissues: A review
    • Basset P, Wolf C, Chambon P. Expression of the stromelysin-3 gene in fibroblastic cells of invasive carcinomas of the breast and other human tissues: a review. Breast Cancer Res Treat 1993, 24, 185-193.
    • (1993) Breast Cancer Res Treat , vol.24 , pp. 185-193
    • Basset, P.1    Wolf, C.2    Chambon, P.3
  • 54
    • 0030938479 scopus 로고    scopus 로고
    • Matrix metalloproteinases as stromal effectors of human carcinoma progression: Therapeutic implications
    • Basset P, Okada A, Chenard MP, et al. Matrix metalloproteinases as stromal effectors of human carcinoma progression: therapeutic implications. Matrix Biol 1997, 15, 535-541.
    • (1997) Matrix Biol , vol.15 , pp. 535-541
    • Basset, P.1    Okada, A.2    Chenard, M.P.3
  • 55
    • 0032833307 scopus 로고    scopus 로고
    • Metastatic and non-metastatic colorectal cancer (CRC) cells induce host metalloproteinase production in vivo
    • McDonnell S, Chaudhry V, Mansilla-Soto J, Zeng ZS, Shu WP, Guillem JG. Metastatic and non-metastatic colorectal cancer (CRC) cells induce host metalloproteinase production in vivo. Clin Exp Metastasis 1999, 17, 341-349.
    • (1999) Clin Exp Metastasis , vol.17 , pp. 341-349
    • McDonnell, S.1    Chaudhry, V.2    Mansilla-Soto, J.3    Zeng, Z.S.4    Shu, W.P.5    Guillem, J.G.6
  • 56
    • 0028928485 scopus 로고
    • Overexpression of matrix metalloproteinase-7 mRNA in human colon carcinomas
    • Mori M, Barnard GF, Mimori K, Ueo H, Akiyoshi T, Sugimachi K. Overexpression of matrix metalloproteinase-7 mRNA in human colon carcinomas. Cancer 1995, 75, 1516-1519.
    • (1995) Cancer , vol.75 , pp. 1516-1519
    • Mori, M.1    Barnard, G.F.2    Mimori, K.3    Ueo, H.4    Akiyoshi, T.5    Sugimachi, K.6
  • 57
    • 0028100681 scopus 로고
    • Expression and localization of matrix-degrading metalloproteinases during colorectal tumorigenesis
    • Newell KJ, Witty JP, Rodgers WH, Matrisian LM. Expression and localization of matrix-degrading metalloproteinases during colorectal tumorigenesis. Mol Carcinog 1994, 10, 199-206.
    • (1994) Mol Carcinog , vol.10 , pp. 199-206
    • Newell, K.J.1    Witty, J.P.2    Rodgers, W.H.3    Matrisian, L.M.4
  • 58
    • 0040351696 scopus 로고    scopus 로고
    • Regulation of collagenase-3 expression in human breast carcinomas is mediated by stromal-epithelial cell interactions
    • Una JA, Stahle-Backdahl M, Seiki M, Fueyo A, Lopez-Otin C. Regulation of collagenase-3 expression in human breast carcinomas is mediated by stromal-epithelial cell interactions. Cancer Res 1997, 57, 4882-4888.
    • (1997) Cancer Res , vol.57 , pp. 4882-4888
    • Una, J.A.1    Stahle-Backdahl, M.2    Seiki, M.3    Fueyo, A.4    Lopez-Otin, C.5
  • 59
    • 0028347399 scopus 로고
    • Immunohistochemical localization of matrix metalloproteinase 2 and its specific inhibitor TIMP-2 in neoplastic tissues with monoclonal antibodies
    • Hoyhtyea M, Fridman R, Komarek D, et al. Immunohistochemical localization of matrix metalloproteinase 2 and its specific inhibitor TIMP-2 in neoplastic tissues with monoclonal antibodies. Int J Cancer 1994, 56, 500-505.
    • (1994) Int J Cancer , vol.56 , pp. 500-505
    • Hoyhtyea, M.1    Fridman, R.2    Komarek, D.3
  • 60
    • 0030030963 scopus 로고    scopus 로고
    • Expression and localization of 92 kDa type IV collagenase/gelatinase B (MMP-9) in human gliomas
    • Rao JS, Yamamoto M, Mohanam S, et al. Expression and localization of 92 kDa type IV collagenase/gelatinase B (MMP-9) in human gliomas. Clin Exp Metastasis 1996, 14, 12-18.
    • (1996) Clin Exp Metastasis , vol.14 , pp. 12-18
    • Rao, J.S.1    Yamamoto, M.2    Mohanam, S.3
  • 61
    • 0032523792 scopus 로고    scopus 로고
    • Matrix metalloproteinases-2 and -9 are expressed in human neuroblastoma: Contribution of stromal cells to their production and correlation with metastasis
    • Sugiura Y, Shimada H, Seeger RC, Laug WE, DeClerck YA. Matrix metalloproteinases-2 and -9 are expressed in human neuroblastoma: contribution of stromal cells to their production and correlation with metastasis. Cancer Res 1998, 58, 2209-2216.
    • (1998) Cancer Res , vol.58 , pp. 2209-2216
    • Sugiura, Y.1    Shimada, H.2    Seeger, R.C.3    Laug, W.E.4    DeClerck, Y.A.5
  • 62
    • 0029946569 scopus 로고    scopus 로고
    • Expression of most matrix metalloproteinase family members in breast cancer represents a tumor-induced host response
    • Heppner KJ, Matrisian LM, Jensen RA, Rodgers WH. Expression of most matrix metalloproteinase family members in breast cancer represents a tumor-induced host response. Am J Pathol 1996, 149, 273-282.
    • (1996) Am J Pathol , vol.149 , pp. 273-282
    • Heppner, K.J.1    Matrisian, L.M.2    Jensen, R.A.3    Rodgers, W.H.4
  • 63
    • 0033151608 scopus 로고    scopus 로고
    • Inflammatory mast cells up-regulate angiogenesis during squamous epithelial carcinogenesis
    • Coussens LM, Raymond WW, Bergers G, et al. Inflammatory mast cells up-regulate angiogenesis during squamous epithelial carcinogenesis. Genes Dev 1999, 13, 1382-1397.
    • (1999) Genes Dev , vol.13 , pp. 1382-1397
    • Coussens, L.M.1    Raymond, W.W.2    Bergers, G.3
  • 64
    • 0030067654 scopus 로고    scopus 로고
    • 92 kDa type IV collagenase (MMP-9) is expressed in neutrophils and macrophages but not in malignant epithelial cells in human colon cancer
    • Nielsen BS, Timshel S, Kjeldsen L, et al. 92 kDa type IV collagenase (MMP-9) is expressed in neutrophils and macrophages but not in malignant epithelial cells in human colon cancer. Int J Cancer 1996, 65, 57-62.
    • (1996) Int J Cancer , vol.65 , pp. 57-62
    • Nielsen, B.S.1    Timshel, S.2    Kjeldsen, L.3
  • 65
    • 0028326346 scopus 로고
    • Induction of fibroblast 92 kDa gelatinase/type IV collagenase expression by direct contact with metastatic tumor cells
    • Himelstein BP, Canete Soler R, Bernhard EJ, Muschel RJ. Induction of fibroblast 92 kDa gelatinase/type IV collagenase expression by direct contact with metastatic tumor cells. J Cell Sci 1994, 107, 477-486.
    • (1994) J Cell Sci , vol.107 , pp. 477-486
    • Himelstein, B.P.1    Canete Soler, R.2    Bernhard, E.J.3    Muschel, R.J.4
  • 66
    • 0028656467 scopus 로고
    • Tumour collagenase-stimulating factor: A paracrine stimulator of fibroblast production of matrix metalloproteinases in cancer
    • Zucker S, Biswas C. Tumour collagenase-stimulating factor: a paracrine stimulator of fibroblast production of matrix metalloproteinases in cancer. Bull Inst Pasteur 1994, 92, 284-290.
    • (1994) Bull Inst Pasteur , vol.92 , pp. 284-290
    • Zucker, S.1    Biswas, C.2
  • 67
    • 0028795147 scopus 로고
    • The human tumor cellderived collagenase stimulatory factor (renamed EMMPRIN) is a member of the immunoglobulin superfamily
    • Biswas C, Zhang Y, DeCastro R, et al. The human tumor cellderived collagenase stimulatory factor (renamed EMMPRIN) is a member of the immunoglobulin superfamily. Cancer Res 1995, 55, 434-439.
    • (1995) Cancer Res , vol.55 , pp. 434-439
    • Biswas, C.1    Zhang, Y.2    DeCastro, R.3
  • 68
    • 0032487394 scopus 로고    scopus 로고
    • Characterization of the gene for human EMMPRIN, a tumor cell surface inducer of matrix metalloproteinases
    • Guo H, Majmudar G, Jensen TC, Biswas C, Toole BP, Gordon MK. Characterization of the gene for human EMMPRIN, a tumor cell surface inducer of matrix metalloproteinases. Gene 1998, 220, 99-108.
    • (1998) Gene , vol.220 , pp. 99-108
    • Guo, H.1    Majmudar, G.2    Jensen, T.C.3    Biswas, C.4    Toole, B.P.5    Gordon, M.K.6
  • 69
    • 0031738172 scopus 로고    scopus 로고
    • Regulation of matrix metalloproteinases (MMP-2, -3, -9, and -13) by interleukin-1 and interleukin-6 in mouse calvaria: Association of MMP induction with bone resorption
    • Kusano K, Miyaura C, Inada M, et al. Regulation of matrix metalloproteinases (MMP-2, -3, -9, and -13) by interleukin-1 and interleukin-6 in mouse calvaria: association of MMP induction with bone resorption. Endocrinology 1998, 139, 1338-1345.
    • (1998) Endocrinology , vol.139 , pp. 1338-1345
    • Kusano, K.1    Miyaura, C.2    Inada, M.3
  • 70
    • 0032547763 scopus 로고    scopus 로고
    • Vascular endothelial growth factor upregulates the expression of matrix metalloproteinases in vascular smooth muscle cells -Role of flt-1
    • Wang H, Keiser JA. Vascular endothelial growth factor upregulates the expression of matrix metalloproteinases in vascular smooth muscle cells -Role of flt-1. Circ Res 1998, 83, 832-840.
    • (1998) Circ Res , vol.83 , pp. 832-840
    • Wang, H.1    Keiser, J.A.2
  • 71
    • 0031870786 scopus 로고    scopus 로고
    • Vascular endothelial growth factor increases release of gelatinase a and decreases release of tissue inhibitor of metalloproteinases by microvascular endothelial cells in vitro
    • Lamoreaux WJ, Fitzgerald MEC, Reiner A, Hasty KA, Charles ST. Vascular endothelial growth factor increases release of gelatinase a and decreases release of tissue inhibitor of metalloproteinases by microvascular endothelial cells in vitro. Microvasc Res 1998, 55, 29-42.
    • (1998) Microvasc Res , vol.55 , pp. 29-42
    • Lamoreaux, W.J.1    Fitzgerald, M.E.C.2    Reiner, A.3    Hasty, K.A.4    Charles, S.T.5
  • 72
    • 0027535914 scopus 로고
    • Biology and biochemistry of proteinases in tumor invasion
    • Mignatti P, Rifkin DB. Biology and biochemistry of proteinases in tumor invasion. Physiol Rev 1993, 73, 161-195.
    • (1993) Physiol Rev , vol.73 , pp. 161-195
    • Mignatti, P.1    Rifkin, D.B.2
  • 73
    • 0032816628 scopus 로고    scopus 로고
    • Inhibition of endothelial cell migration by gene transfer of tissue inhibitor of metalloproteinases-1
    • Fernandez HA, Kallenbach K, Seghezzi G, et al. Inhibition of endothelial cell migration by gene transfer of tissue inhibitor of metalloproteinases-1. J Surg Res 1999, 82, 156-162.
    • (1999) J Surg Res , vol.82 , pp. 156-162
    • Fernandez, H.A.1    Kallenbach, K.2    Seghezzi, G.3
  • 74
    • 0032211804 scopus 로고    scopus 로고
    • ECM signalling: Orchestrating cell behaviour and misbehaviour
    • Lukashev ME, Werb Z. ECM signalling: orchestrating cell behaviour and misbehaviour. Trends Cell Biol 1998, 8, 437-441.
    • (1998) Trends Cell Biol , vol.8 , pp. 437-441
    • Lukashev, M.E.1    Werb, Z.2
  • 75
    • 0029119564 scopus 로고
    • A hierarchy of ECMmediated signalling regulates tissue-specific gene expression
    • Roskelley CD, Srebrow A, Bissell MJ. A hierarchy of ECMmediated signalling regulates tissue-specific gene expression. Curr Opin Cell Biol 1995, 7, 736-747.
    • (1995) Curr Opin Cell Biol , vol.7 , pp. 736-747
    • Roskelley, C.D.1    Srebrow, A.2    Bissell, M.J.3
  • 76
    • 0030715322 scopus 로고    scopus 로고
    • ECM and cell surface proteolysis: Regulating cellular ecology
    • Werb Z. ECM and cell surface proteolysis: regulating cellular ecology. Cell 1997, 91, 439-442.
    • (1997) Cell , vol.91 , pp. 439-442
    • Werb, Z.1
  • 77
    • 0027973543 scopus 로고
    • Goals for signal transduction pathways: Linking up with transcriptional regulation
    • Sassone Corsi P. Goals for signal transduction pathways: linking up with transcriptional regulation. EMBO J 1994, 13, 4717-4728.
    • (1994) EMBO J , vol.13 , pp. 4717-4728
    • Sassone Corsi, P.1
  • 78
    • 0028557342 scopus 로고
    • Extracellular matrixdependent tissue-specific gene expression in mammary epithelial cells requires both physical and biochemical signal transduction
    • Roskelley CD, Desprez PY, Bissell MJ. Extracellular matrixdependent tissue-specific gene expression in mammary epithelial cells requires both physical and biochemical signal transduction. Proc Natl Acad Sci USA 1994, 91, 12378-12382.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 12378-12382
    • Roskelley, C.D.1    Desprez, P.Y.2    Bissell, M.J.3
  • 79
    • 0028927484 scopus 로고
    • Suppression of ICE and apoptosis in mammary epithelial cells by extracellular matrix
    • Boudreau N, Sympson CJ, Werb Z, Bissell MJ. Suppression of ICE and apoptosis in mammary epithelial cells by extracellular matrix. Science 1995, 267, 891-893.
    • (1995) Science , vol.267 , pp. 891-893
    • Boudreau, N.1    Sympson, C.J.2    Werb, Z.3    Bissell, M.J.4
  • 80
    • 0029312344 scopus 로고
    • Mammary gland tumor formation in transgenic mice overexpressing stromelysin-1
    • Sympson CJ, Bissell MJ, Werb Z. Mammary gland tumor formation in transgenic mice overexpressing stromelysin-1. Semin Cancer Biol 1995, 6, 159-163.
    • (1995) Semin Cancer Biol , vol.6 , pp. 159-163
    • Sympson, C.J.1    Bissell, M.J.2    Werb, Z.3
  • 81
    • 0030454231 scopus 로고    scopus 로고
    • Rescue of mammary epithelial cell apoptosis and entactin degradation by a tissue inhibitor of metalloproteinases-1 transgene
    • Alexander CM, Howard EW, Bissell MJ, Werb Z. Rescue of mammary epithelial cell apoptosis and entactin degradation by a tissue inhibitor of metalloproteinases-1 transgene. J Cell Biology 1996, 135, 1669-1677.
    • (1996) J Cell Biology , vol.135 , pp. 1669-1677
    • Alexander, C.M.1    Howard, E.W.2    Bissell, M.J.3    Werb, Z.4
  • 82
    • 0029916820 scopus 로고    scopus 로고
    • Suppression of apoptosis by basement membrane requires three-dimensional tissue organiza-tion and withdrawal from the cell cycle
    • Boudreau N, Werb Z, Bissell MJ. Suppression of apoptosis by basement membrane requires three-dimensional tissue organiza-tion and withdrawal from the cell cycle. Proc Natl Acad Sci USA 1996, 93, 3509-3513.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 3509-3513
    • Boudreau, N.1    Werb, Z.2    Bissell, M.J.3
  • 83
    • 0031713433 scopus 로고    scopus 로고
    • Extracellular matrix signaling: Integration of form and function in normal and malignant cells
    • Boudreau N, Bissell MJ. Extracellular matrix signaling: integration of form and function in normal and malignant cells. Curr Opin Cell Biol 1998, 10, 640-646.
    • (1998) Curr Opin Cell Biol , vol.10 , pp. 640-646
    • Boudreau, N.1    Bissell, M.J.2
  • 84
    • 0032559362 scopus 로고    scopus 로고
    • Rho GTPases and the actin cytoskeleton
    • Hall A. Rho GTPases and the actin cytoskeleton. Science 1998, 279, 509-514.
    • (1998) Science , vol.279 , pp. 509-514
    • Hall, A.1
  • 86
    • 0028670298 scopus 로고
    • Integrin alpha v beta 3 rescues melanoma cells from apoptosis in three-dimensional dermal collagen
    • Montgomery AM, Reisfeld RA, Cheresh DA. Integrin alpha v beta 3 rescues melanoma cells from apoptosis in three-dimensional dermal collagen. Proc Natl Acad Sci USA 1994, 91, 8856-8860.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 8856-8860
    • Montgomery, A.M.1    Reisfeld, R.A.2    Cheresh, D.A.3
  • 87
    • 0344731256 scopus 로고    scopus 로고
    • Integrin alpha(v)beta3 promotes M21 melanoma growth in human skin by regulating tumor cell survival
    • Petitclerc E, Stromblad S, von Schalscha TL, et al. Integrin alpha(v)beta3 promotes M21 melanoma growth in human skin by regulating tumor cell survival. Cancer Res 1999, 59, 2724-2730.
    • (1999) Cancer Res , vol.59 , pp. 2724-2730
    • Petitclerc, E.1    Stromblad, S.2    Von Schalscha, T.L.3
  • 88
    • 0028978457 scopus 로고
    • Re-expression of the alpha 2 beta 1 integrin abrogates the malignant phenotype of breast carcinoma cells
    • Zutter MM, Santoro SA, Staatz WD, Tsung YL. Re-expression of the alpha 2 beta 1 integrin abrogates the malignant phenotype of breast carcinoma cells. Proc Natl Acad Sci USA 1995, 92, 7411-7415.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 7411-7415
    • Zutter, M.M.1    Santoro, S.A.2    Staatz, W.D.3    Tsung, Y.L.4
  • 89
    • 0028104790 scopus 로고
    • Effect of tissue inhibitor of the matrix metalloproteinases-2 expression on the growth and spontaneous metastasis of a human melanoma cell line
    • Montgomery AM, Mueller BM, Reisfeld RA, Taylor SM, DeClerck YA. Effect of tissue inhibitor of the matrix metalloproteinases-2 expression on the growth and spontaneous metastasis of a human melanoma cell line. Cancer Res 1994, 54, 5467-5473.
    • (1994) Cancer Res , vol.54 , pp. 5467-5473
    • Montgomery, A.M.1    Mueller, B.M.2    Reisfeld, R.A.3    Taylor, S.M.4    DeClerck, Y.A.5
  • 90
    • 0033003988 scopus 로고    scopus 로고
    • Tissue inhibitors of metalloproteinases (TIMP) in invasion and proliferation
    • Henriet P, Blavier L, DeClerck YA. Tissue inhibitors of metalloproteinases (TIMP) in invasion and proliferation. APMIS 1999, 107, 111-119.
    • (1999) APMIS , vol.107 , pp. 111-119
    • Henriet, P.1    Blavier, L.2    DeClerck, Y.A.3
  • 91
    • 0033032317 scopus 로고    scopus 로고
    • Extracellular matrix proteins protect small cell lung cancer cells against apoptosis: A mechanism for small cell lung cancer growth and drug resistance in vivo
    • Sethi T, Rintoul RC, Moore SM, et al. Extracellular matrix proteins protect small cell lung cancer cells against apoptosis: a mechanism for small cell lung cancer growth and drug resistance in vivo. Natl Med 1999, 5, 662-668.
    • (1999) Natl Med , vol.5 , pp. 662-668
    • Sethi, T.1    Rintoul, R.C.2    Moore, S.M.3
  • 92
    • 0034614637 scopus 로고    scopus 로고
    • The hallmarks of cancer
    • Hanahan D, Weinberg RA. The hallmarks of cancer. Cell 2000, 100, 57-70.
    • (2000) Cell , vol.100 , pp. 57-70
    • Hanahan, D.1    Weinberg, R.A.2


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