메뉴 건너뛰기




Volumn 3, Issue 3, 2002, Pages 207-214

Matrix metalloproteinases: A tail of a frog that became a prince

Author keywords

[No Author keywords available]

Indexed keywords

MATRIX METALLOPROTEINASE; PROTEINASE INHIBITOR;

EID: 0036516460     PISSN: 14710072     EISSN: None     Source Type: Journal    
DOI: 10.1038/nrm763     Document Type: Review
Times cited : (993)

References (104)
  • 1
    • 0345935809 scopus 로고
    • Collagenolytic activity in amphibian tissues: A tissue culture assay
    • Gross, J. & Lapiere, C. M. Collagenolytic activity in amphibian tissues: a tissue culture assay. Proc. Natl Acad. Sci. USA 48, 1014-1022 (1962).
    • (1962) Proc. Natl. Acad. Sci. USA , vol.48 , pp. 1014-1022
    • Gross, J.1    Lapiere, C.M.2
  • 4
    • 0012530895 scopus 로고    scopus 로고
    • ed. Clark. I. M.
    • Matrix Metalloproteinase Protocols (ed. Clark. I. M.); Methods in Molecular Biology (ed. Walker, J, M.) Vol. 151. (Humana, New Jersey. 2001).
    • Matrix Metalloproteinase Protocols
  • 5
    • 0002789436 scopus 로고    scopus 로고
    • (ed. Walker, J. M.) (Humana, New Jersey)
    • Matrix Metalloproteinase Protocols (ed. Clark. I. M.); Methods in Molecular Biology (ed. Walker, J. M.) Vol. 151. (Humana, New Jersey. 2001).
    • (2001) Methods in Molecular Biology , vol.151
  • 6
    • 0035479845 scopus 로고    scopus 로고
    • Matrix metalloproteinases: They're not just for matrix anymore!
    • McCawley, L. J. & Matrisian, L. M. Matrix metalloproteinases: they're not just for matrix anymore! Curr. Opin. Cell Biol. 13. 534-540 (2001).
    • (2001) Curr. Opin. Cell Biol. , vol.13 , pp. 534-540
    • McCawley, L.J.1    Matrisian, L.M.2
  • 7
    • 0027025213 scopus 로고
    • Nomenclature and glossary of the matrix metalloproteinases
    • Nagase, H., Barrett, A. J. & Woessner, J. F. Jr. Nomenclature and glossary of the matrix metalloproteinases. Matrix Suppl. 1, 421-424 (1992).
    • (1992) Matrix Suppl. , vol.1 , pp. 421-424
    • Nagase, H.1    Barrett, A.J.2    Woessner J.F., Jr.3
  • 8
    • 0014958391 scopus 로고
    • Immunologic relationship of a purified human skin collagenase to other human and animal collagenases
    • Bauer, E. A., Eisen, A. Z, & Jeffrey, J. J. Immunologic relationship of a purified human skin collagenase to other human and animal collagenases. Biochim. Biophys. Acta 206, 152-160 (1970).
    • (1970) Biochim. Biophys. Acta , vol.206 , pp. 152-160
    • Bauer, E.A.1    Eisen, A.Z.2    Jeffrey, J.J.3
  • 9
    • 0014955598 scopus 로고
    • Coliagenase from rat uterus isolation and partial characterization
    • Jeffrey, J. J. & Gross, J, Coliagenase from rat uterus isolation and partial characterization. Biochemistry 9, 268-273 (1970).
    • (1970) Biochemistry , vol.9 , pp. 268-273
    • Jeffrey, J.J.1    Gross, J.2
  • 10
    • 0020808164 scopus 로고
    • Purification and properties of rat uterine procollagenase
    • Roswit, W. T., Halme, J. & Jeffrey. J. J. Purification and properties of rat uterine procollagenase. Arch. Biochem. Biophys. 225, 285-295 (1983).
    • (1983) Arch. Biochem. Biophys. , vol.225 , pp. 285-295
    • Roswit, W.T.1    Halme, J.2    Jeffrey, J.J.3
  • 11
    • 0015209394 scopus 로고
    • The zymogen of tadpole collagenase
    • Harper, E., Bloch, K. J. & Gross, J. The zymogen of tadpole collagenase. Biochemistry 10, 3035-3041 (1971).
    • (1971) Biochemistry , vol.10 , pp. 3035-3041
    • Harper, E.1    Bloch, K.J.2    Gross, J.3
  • 13
    • 0025025442 scopus 로고
    • The cysteine switch: A principle of regulation of metaltoproteinase activity with potential applicability to the entire matrix metalloproteinase gene family
    • Van Wart, H. E. & Birkedal-Hansen, H. The cysteine switch: a principle of regulation of metaltoproteinase activity with potential applicability to the entire matrix metalloproteinase gene family. Proc. Natl Acad. Sci. USA 87, 5578-5582 (1990).
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 5578-5582
    • Van Wart, H.E.1    Birkedal-Hansen, H.2
  • 14
    • 0024232938 scopus 로고
    • Evidence that human rheumatoid synovial matrix metalloproteinase 3 is an endogenous activator of procollagenase
    • Ito, A. & Nagase, H. Evidence that human rheumatoid synovial matrix metalloproteinase 3 is an endogenous activator of procollagenase. Arch. Biochem. Biophys. 267, 211-216 (1988).
    • (1988) Arch. Biochem. Biophys. , vol.267 , pp. 211-216
    • Ito, A.1    Nagase, H.2
  • 15
    • 0022879018 scopus 로고
    • Purification and characterization of collagenase activator protein synthesized by articular cartilage
    • Treadwell, B. V. et al. Purification and characterization of collagenase activator protein synthesized by articular cartilage. Arch. Biochem. Biophys. 251, 715-723 (1986).
    • (1986) Arch. Biochem. Biophys. , vol.251 , pp. 715-723
    • Treadwell, B.V.1
  • 16
    • 0004553618 scopus 로고
    • Tissue cooperation in a proteolytic cascade activating human interstitial collagenase
    • He, C. et al. Tissue cooperation in a proteolytic cascade activating human interstitial collagenase. Proc. Natl Acad. Sci. USA 88, 2632-2636 (1989).
    • (1989) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 2632-2636
    • He, C.1
  • 17
    • 0028291737 scopus 로고
    • A matrix metalloproteinase expressed on the surface of invasive tumour cells
    • Sato, H. et al. A matrix metalloproteinase expressed on the surface of invasive tumour cells. Nature 370, 61-64 (1994).
    • (1994) Nature , vol.370 , pp. 61-64
    • Sato, H.1
  • 18
    • 0029014101 scopus 로고
    • Furin-dependent intracellular activation of the human stromelysin-3 zymogen
    • Pei, D. & Weiss, S. J. Furin-dependent intracellular activation of the human stromelysin-3 zymogen. Nature 375, 244-247 (1995).
    • (1995) Nature , vol.375 , pp. 244-247
    • Pei, D.1    Weiss, S.J.2
  • 19
    • 0018392458 scopus 로고
    • A specific inhibitor of vertebrate collagenase produced by human skin fibroblasts
    • Welgus, H. G. et al. A specific inhibitor of vertebrate collagenase produced by human skin fibroblasts. J. Biol. Chem. 254, 1938-1943 (1979).
    • (1979) J. Biol. Chem. , vol.254 , pp. 1938-1943
    • Welgus, H.G.1
  • 20
    • 0022382006 scopus 로고
    • Sequence of human tissue inhibitor of metalloproteinases and its identity to erythroid-potentiating activity
    • Docherty, A. J. P. et al. Sequence of human tissue inhibitor of metalloproteinases and its identity to erythroid-potentiating activity, Nature 318, 66-69 (1985).
    • (1985) Nature , vol.318 , pp. 66-69
    • Docherty, A.J.P.1
  • 21
    • 1842377505 scopus 로고    scopus 로고
    • Mechanism of inhibition of the human matrix metalloproteinase stromelysin-1 by TIMP-1
    • Gomis-Rüth, FX. et al. Mechanism of inhibition of the human matrix metalloproteinase stromelysin-1 by TIMP-1. Nature 389, 77-81 (1997).
    • (1997) Nature , vol.389 , pp. 77-81
    • Gomis-Rüth, F.X.1
  • 22
    • 0006506596 scopus 로고
    • Human 72-kilodalton type IV collagenase forms a complex with a tissue inhibitor of metalloproteinases designated TIMP-2
    • Goldberg, G. I. et al. Human 72-kilodalton type IV collagenase forms a complex with a tissue inhibitor of metalloproteinases designated TIMP-2. Proc. Natl Acad. Sci. USA 86, 8207-8211 (1989).
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 8207-8211
    • Goldberg, G.I.1
  • 23
    • 0026630048 scopus 로고
    • Interaction of 92-kDa type IV collagenase with the tissue inhibitor of metalloproteinases prevents dimerization, complex formation with interstitial collagenase, and activation of the proenzyme with stromelysin
    • Goldberg, G. I., Strongin, A., Collier, I. E., Genrich, L. T. & Marmer, B. L. Interaction of 92-kDa type IV collagenase with the tissue inhibitor of metalloproteinases prevents dimerization, complex formation with interstitial collagenase, and activation of the proenzyme with stromelysin. J. Biol. Chem. 287, 4583-4591 (1992).
    • (1992) J. Biol. Chem. , vol.287 , pp. 4583-4591
    • Goldberg, G.I.1    Strongin, A.2    Collier, I.E.3    Genrich, L.T.4    Marmer, B.L.5
  • 24
    • 0026568011 scopus 로고
    • Growth-promoting activity of tissue inhibitor of metalloproteinases-1 (TIMP-1) for a wide range of cells
    • Hayakawa, T., Yamashita, K., Tanzawa, K., Uchijima, E. & Iwata, K. Growth-promoting activity of tissue inhibitor of metalloproteinases-1 (TIMP-1) for a wide range of cells. FEBS Lett. 298, 29-32 (1992).
    • (1992) FEBS Lett. , vol.298 , pp. 29-32
    • Hayakawa, T.1    Yamashita, K.2    Tanzawa, K.3    Uchijima, E.4    Iwata, K.5
  • 25
    • 0028047686 scopus 로고
    • Structure of the catalytic domain of fibroblast collagenase complexed with an inhibitor
    • Lovejoy, B. et al, Structure of the catalytic domain of fibroblast collagenase complexed with an inhibitor. Science 263, 375-377 (1994).
    • (1994) Science , vol.263 , pp. 375-377
    • Lovejoy, B.1
  • 27
    • 0026640236 scopus 로고
    • The role of the C-terminal domain in collagenase and stromelysin specificity
    • Murphy, G. et al. The role of the C-terminal domain in collagenase and stromelysin specificity. J. Biol. Chem, 267, 9612-9618 (1992).
    • (1992) J. Biol. Chem. , vol.267 , pp. 9612-9618
    • Murphy, G.1
  • 28
    • 0027533506 scopus 로고
    • Structure-function relationship of human neutrophil collagenase: Identification of regions responsible for substrate specificity and general proteinase activity
    • Hirose, T., Patterson, C., Pourmotabbed, T., Mainardi, C. L. & Hasty, K. A. Structure-function relationship of human neutrophil collagenase: identification of regions responsible for substrate specificity and general proteinase activity. Proc. Natl Acad. Sci. USA 90, 2569-2573 (1993).
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 2569-2573
    • Hirose, T.1    Patterson, C.2    Pourmotabbed, T.3    Mainardi, C.L.4    Hasty, K.A.5
  • 30
    • 0033523040 scopus 로고    scopus 로고
    • Structure of human pro-matrix metalloproteinase-2: Activation mechanism revealed
    • Morgunova, E. et al. Structure of human pro-matrix metalloproteinase-2: activation mechanism revealed, Science 284, 1667-1670 (1999).
    • (1999) Science , vol.284 , pp. 1667-1670
    • Morgunova, E.1
  • 31
    • 0007711678 scopus 로고
    • Isolation of a collagenase cDNA clone and measurement of changing collagenase mRNA levels during induction in rabbit synovial fibroblasts
    • Gross, R. H., Sheldon, L. A., Fletcher, C. F. & Brinckerhoff, C. E. Isolation of a collagenase cDNA clone and measurement of changing collagenase mRNA levels during induction in rabbit synovial fibroblasts. Proc. Natl Acad. Sci. USA 81, 1981-1985 (1984).
    • (1984) Proc. Natl. Acad. Sci. USA , vol.81 , pp. 1981-1985
    • Gross, R.H.1    Sheldon, L.A.2    Fletcher, C.F.3    Brinckerhoff, C.E.4
  • 32
    • 0022085068 scopus 로고
    • Epidermal growth factor and oncogenes induce transcription of the same cellular mRNA in rat fibroblasts
    • Matrisian, L. M., Glaichenhaus, N., Gesnel, M. C. & Breathnach, R. Epidermal growth factor and oncogenes induce transcription of the same cellular mRNA in rat fibroblasts. EMBO J. 4, 1435-1440 (1985).
    • (1985) EMBO J. , vol.4 , pp. 1435-1440
    • Matrisian, L.M.1    Glaichenhaus, N.2    Gesnel, M.C.3    Breathnach, R.4
  • 33
    • 0022996811 scopus 로고
    • Human fibroblast collagenase. Complete primary structure and homology to an oncogene transformation-induced rat protein
    • Goldberg, G. I. et al. Human fibroblast collagenase. Complete primary structure and homology to an oncogene transformation-induced rat protein. J. Biol. Chem. 261, 6600-6605 (1986).
    • (1986) J. Biol. Chem. , vol.261 , pp. 6600-6605
    • Goldberg, G.I.1
  • 34
    • 0022917253 scopus 로고
    • Comparison of human stromelysin and collagenase by cloning and sequence analysis
    • Whitham, S. E. et al. Comparison of human stromelysin and collagenase by cloning and sequence analysis. Biochem. J. 240, 913-916 (1986).
    • (1986) Biochem. J. , vol.240 , pp. 913-916
    • Whitham, S.E.1
  • 35
    • 0022892609 scopus 로고
    • The mRNA coding for the secreted protease transin is expressed more abundantly in malignant than in benign tumors
    • Matnsian, L. M. et al. The mRNA coding for the secreted protease transin is expressed more abundantly in malignant than in benign tumors. Proc. Natl Acad. Sci. USA 83, 9413-9417 (1986).
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 9413-9417
    • Matnsian, L.M.1
  • 37
    • 0023107287 scopus 로고
    • Sequences coding for part of oncogene-induced transin are highly conserved in a related rat gene
    • Breathnach, R., Matrisian, L. M., Gesnel, M. C., Staub, A. & Leroy, P. Sequences coding for part of oncogene-induced transin are highly conserved in a related rat gene. Nucleic Acids Res. 15, 1139-1151 (1987).
    • (1987) Nucleic Acids Res. , vol.15 , pp. 1139-1151
    • Breathnach, R.1    Matrisian, L.M.2    Gesnel, M.C.3    Staub, A.4    Leroy, P.5
  • 38
    • 0031656460 scopus 로고    scopus 로고
    • Matrix metalloproteinases: Structures, evolution, and diversification
    • Massova, I., Kotra, L P., Fridman, R. & Mobashery, S. Matrix metalloproteinases: structures, evolution, and diversification. FASEB J. 12, 1075-1095 (1998).
    • (1998) FASEB J. , vol.12 , pp. 1075-1095
    • Massova, I.1    Kotra, L.P.2    Fridman, R.3    Mobashery, S.4
  • 39
    • 0026096865 scopus 로고
    • On the structure and chromosome location of the 72- and 92-kDa human type IV collagenasegenes
    • Collier. I. E., Bruns, G. A. P., Goldberg. G. I. & Gerhard, D. S. On the structure and chromosome location of the 72- and 92-kDa human type IV collagenase genes. Genomics 9, 429-434 (1991).
    • (1991) Genomics , vol.9 , pp. 429-434
    • Collier, I.E.1    Bruns, G.A.P.2    Goldberg, G.I.3    Gerhard, D.S.4
  • 40
    • 0025614357 scopus 로고
    • Rat collagenase cloning, amino acid sequence comparison, and parathyroid hormone regulation in osteoblastic cells
    • Quinn, C. O. et al, Rat collagenase cloning, amino acid sequence comparison, and parathyroid hormone regulation in osteoblastic cells. J. Biol. Chem. 265, 22342-22347 (1990).
    • (1990) J. Biol. Chem. , vol.265 , pp. 22342-22347
    • Quinn, C.O.1
  • 41
    • 0028322352 scopus 로고
    • R et al. Molecular cloning and expression of collagenase-3, a novel human matrix metalloproteinase produced by breast carcinomas
    • Freije, J. M. R et al. Molecular cloning and expression of collagenase-3, a novel human matrix metalloproteinase produced by breast carcinomas. J. Biol. Chem. 269, 16766-16773 (1994).
    • (1994) J. Biol. Chem. , vol.269 , pp. 16766-16773
    • Freije, J.M.1
  • 42
    • 85047691853 scopus 로고    scopus 로고
    • Identification and enzymatic characterization of two diverging murine counterparts of human interstitial collagenase (MMP-1) expressed at sites of embryo implantation
    • Balbin, M. et al. Identification and enzymatic characterization of two diverging murine counterparts of human interstitial collagenase (MMP-1) expressed at sites of embryo implantation. J. Biol. Chem. 276, 10253-10262 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 10253-10262
    • Balbin, M.1
  • 44
    • 0002789436 scopus 로고    scopus 로고
    • (ed. Walker, J. M.) (Humana, New Jersey)
    • Methods in Molecular Biology (ed. Walker, J. M.) Vol. 151, (Humana, New Jersey, 2001).
    • (2001) Methods in Molecular Biology , vol.151
  • 45
    • 0033152980 scopus 로고    scopus 로고
    • Identification and characterization of human MT5-MMP, a new membrane-bound activator of progelatinase A overexpressed in brain tumors
    • Llano, E. et al. Identification and characterization of human MT5-MMP, a new membrane-bound activator of progelatinase A overexpressed in brain tumors. Cancer Res. 59, 2570-2576 (1999).
    • (1999) Cancer Res. , vol.59 , pp. 2570-2576
    • Llano, E.1
  • 46
    • 0030022539 scopus 로고    scopus 로고
    • Molecular cloning of a novel membrane-type matrix metalloproteinase from a human breast carcinoma
    • Puente, X. S., Pendas, A. M., Llano, E., Velasco, G. & Lopez-Otin, C. Molecular cloning of a novel membrane-type matrix metalloproteinase from a human breast carcinoma. Cancer Res. 56, 944-949 (1996).
    • (1996) Cancer Res. , vol.56 , pp. 944-949
    • Puente, X.S.1    Pendas, A.M.2    Llano, E.3    Velasco, G.4    Lopez-Otin, C.5
  • 47
    • 0033607524 scopus 로고    scopus 로고
    • Membrane type 4 matrix metalloproteinase (MT4-MMP, MMP-17) is a glycosylphosphatidylinositol-anchored proteinase
    • Itoh, Y. et al. Membrane type 4 matrix metalloproteinase (MT4-MMP, MMP-17) is a glycosylphosphatidylinositol-anchored proteinase. J. Biol. Chem. 274, 34260-34266 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 34260-34266
    • Itoh, Y.1
  • 48
    • 0034652623 scopus 로고    scopus 로고
    • Human MT6-matrix metalloproteinase: Identification, progelatinase A activation, and expression in brain tumors
    • Velasco, G. et al. Human MT6-matrix metalloproteinase: identification, progelatinase A activation, and expression in brain tumors. Cancer Res. 60, 877-882 (2000).
    • (2000) Cancer Res. , vol.60 , pp. 877-882
    • Velasco, G.1
  • 49
    • 0023625090 scopus 로고
    • Phorbol ester-inducible genes contain a common cis element recognized by a TPA-modulated trans-acting factor
    • Angel, P. et al. Phorbol ester-inducible genes contain a common cis element recognized by a TPA-modulated trans-acting factor. Cell 49, 729-739 (1987).
    • (1987) Cell , vol.49 , pp. 729-739
    • Angel, P.1
  • 50
    • 0023355884 scopus 로고
    • 12-O-tetradecanoyl-phorbol-13-acetate induction of the human collagenase gene is mediated by an inducible enhancer element located in the 5′-flanking region
    • Angel, P. et al. 12-O-tetradecanoyl-phorbol-13-acetate induction of the human collagenase gene is mediated by an inducible enhancer element located in the 5′-flanking region. Mol. Cell. Biol. 7, 2256-2266 (1987).
    • (1987) Mol. Cell. Biol. , vol.7 , pp. 2256-2266
    • Angel, P.1
  • 51
    • 0025346113 scopus 로고
    • The collagenase gene promoter contains a TPA and oncogene-responsive unit encompassing the PEA3 and AP-1 binding sites
    • Gutmann, A. & Wasylyk, B. The collagenase gene promoter contains a TPA and oncogene-responsive unit encompassing the PEA3 and AP-1 binding sites, EMBO J. 9, 2241-2246 (1990).
    • (1990) EMBO J. , vol.9 , pp. 2241-2246
    • Gutmann, A.1    Wasylyk, B.2
  • 52
    • 0030932125 scopus 로고    scopus 로고
    • The AP-1 site and MMP gene regulation: What is all the fuss about?
    • Benbow, U. & Brinckerhoff, C. E. The AP-1 site and MMP gene regulation: what is all the fuss about? Matrix Biol. 15, 519-526 (1997).
    • (1997) Matrix Biol. , vol.15 , pp. 519-526
    • Benbow, U.1    Brinckerhoff, C.E.2
  • 53
    • 0029899015 scopus 로고    scopus 로고
    • Mechanisms controlling the transcription of matrix metalloproteinase genes in normal and neoplastic cells
    • Crawford, H. C. & Matrisian, L. M. Mechanisms controlling the transcription of matrix metalloproteinase genes in normal and neoplastic cells. Enzyme Protein 49, 20-37 (1996).
    • (1996) Enzyme Protein , vol.49 , pp. 20-37
    • Crawford, H.C.1    Matrisian, L.M.2
  • 55
    • 0033742833 scopus 로고    scopus 로고
    • Polymorphism in matrix metalloproteinase gene promoters: Implication in regulation of gene expression and susceptibility of various diseases
    • Ye, S. Polymorphism in matrix metalloproteinase gene promoters: implication in regulation of gene expression and susceptibility of various diseases. Matrix Biol. 19, 623-629(2000).
    • (2000) Matrix Biol. , vol.19 , pp. 623-629
    • Ye, S.1
  • 56
    • 15844406034 scopus 로고    scopus 로고
    • Progression of coronary atherosclerosis is associated with a common genetic variant of the human stromelysin-1 promoter which results expression
    • Ye, S. et al. Progression of coronary atherosclerosis is associated with a common genetic variant of the human stromelysin-1 promoter which results expression. J. Biol. Chem. 271, 13055-13060 (1996).
    • (1996) J. Biol. Chem. , vol.271 , pp. 13055-13060
    • Ye, S.1
  • 57
    • 0032404174 scopus 로고    scopus 로고
    • A single nucleotide polymorphism in the matrix metalloproteinase-1 promoter creates an Ets binding site and augments transcription
    • Rutter, J. L. et al. A single nucleotide polymorphism in the matrix metalloproteinase-1 promoter creates an Ets binding site and augments transcription. Cancer Res. 58, 5321-5325 (1998).
    • (1998) Cancer Res. , vol.58 , pp. 5321-5325
    • Rutter, J.L.1
  • 58
    • 0017071174 scopus 로고
    • Extraction of collagenase from the involuting rat uterus
    • Weeks, J. G., Halme, J. & Woessner, J. E Jr. Extraction of collagenase from the involuting rat uterus. Biochim. Biophys. Acta 445, 205-214 (1976).
    • (1976) Biochim. Biophys. Acta , vol.445 , pp. 205-214
    • Weeks, J.G.1    Halme, J.2    Woessner J.E., Jr.3
  • 59
    • 0030630628 scopus 로고    scopus 로고
    • Matrix metalloproteinases as mediators of reproductive function
    • Hulboy, D. L., Rudolph, L. A. & Matrisian, L. M. Matrix metalloproteinases as mediators of reproductive function. Mol. Hum. Reprod. 3, 27-45 (1997).
    • (1997) Mol. Hum. Reprod. , vol.3 , pp. 27-45
    • Hulboy, D.L.1    Rudolph, L.A.2    Matrisian, L.M.3
  • 60
    • 14444285039 scopus 로고    scopus 로고
    • Susceptibility of stromelysin 1-deficient mice to collagen-induced arthritis and cartilage destruction
    • Mudgett, J. S. et al. Susceptibility of stromelysin 1-deficient mice to collagen-induced arthritis and cartilage destruction. Arthritis Rheum. 41, 110-121 (1998).
    • (1998) Arthritis Rheum. , vol.41 , pp. 110-121
    • Mudgett, J.S.1
  • 61
    • 0030884231 scopus 로고    scopus 로고
    • Unaltered secretion of β-amyloid precursor protein in gelatinase A (matrix metalloproteinase 2)-deficient mice
    • Itoh, T. et al. Unaltered secretion of β-amyloid precursor protein in gelatinase A (matrix metalloproteinase 2)-deficient mice. J. Biol. Chem. 272, 22389-22392 (1997).
    • (1997) J. Biol. Chem. , vol.272 , pp. 22389-22392
    • Itoh, T.1
  • 64
    • 0032559821 scopus 로고    scopus 로고
    • In vivo evidence that the stromelysin-3 metalloproteinase contributes in a paracrine manner to epithelial cell malignancy
    • Masson, R. et al. In vivo evidence that the stromelysin-3 metalloproteinase contributes in a paracrine manner to epithelial cell malignancy. J. Cell Biol. 140, 1535-1541 (1998).
    • (1998) J. Cell Biol. , vol.140 , pp. 1535-1541
    • Masson, R.1
  • 65
    • 0346963598 scopus 로고    scopus 로고
    • MMP-9/Gelatinase B is a key regulator of growth plate angiogenesis and apoptosis of hypertrophic chondrocytes
    • Vu, T. H. et al. MMP-9/Gelatinase B is a key regulator of growth plate angiogenesis and apoptosis of hypertrophic chondrocytes. Cell 93, 411-422 (1998).
    • (1998) Cell , vol.93 , pp. 411-422
    • Vu, T.H.1
  • 66
    • 2142784516 scopus 로고    scopus 로고
    • MT1-MMP-deficient mice develop dwarfism, osteopenia, arthritis, and connective tissue disease due to inadequate collagen turnover
    • Holmbeck, K. et al. MT1-MMP-deficient mice develop dwarfism, osteopenia, arthritis, and connective tissue disease due to inadequate collagen turnover. Cell 99, 81-92 (1999).
    • (1999) Cell , vol.99 , pp. 81-92
    • Holmbeck, K.1
  • 67
    • 0028097367 scopus 로고
    • Mutations in the tissue inhibitor of metalloproteinases-3 (TIMP3) in patients with Sorsby's fundus dystrophy
    • Weber, B. H. F., Vogt, G., Pruett, R. C., Stohr, H. & Felbor, U. Mutations in the tissue inhibitor of metalloproteinases-3 (TIMP3) in patients with Sorsby's fundus dystrophy, Nature Genet. 8, 352-356 (1994).
    • (1994) Nature Genet. , vol.8 , pp. 352-356
    • Weber, B.H.F.1    Vogt, G.2    Pruett, R.C.3    Stohr, H.4    Felbor, U.5
  • 68
    • 0034946637 scopus 로고    scopus 로고
    • Mutation of the matrix metalloproteinase 2 gene (MMP2) causes a multicentric osteolysis and arthritis syndrome
    • Martignetti, J. A. et al. Mutation of the matrix metalloproteinase 2 gene (MMP2) causes a multicentric osteolysis and arthritis syndrome. Nature Genet. 28, 261-265 (2001).
    • (2001) Nature Genet. , vol.28 , pp. 261-265
    • Martignetti, J.A.1
  • 69
    • 0030823772 scopus 로고    scopus 로고
    • Requirement for macrophage elastase for cigarette smoke-induced emphysema in mice
    • Hautamaki, R. D., Kobayashi, D. K., Senior, R. M. & Shapiro, S. D. Requirement for macrophage elastase for cigarette smoke-induced emphysema in mice. Science 277, 2002-2004 (1997).
    • (1997) Science , vol.277 , pp. 2002-2004
    • Hautamaki, R.D.1    Kobayashi, D.K.2    Senior, R.M.3    Shapiro, S.D.4
  • 70
    • 0033999308 scopus 로고    scopus 로고
    • Matrix metalloproteinases: Biologic activity and clinical implications
    • Nelson, A. R., Fingleton, B., Rothenberg, M. L. & Matrisian, L. M. Matrix metalloproteinases: biologic activity and clinical implications. J. Clin. Oncol. 18, 1135-1149 (2000).
    • (2000) J. Clin. Oncol. , vol.18 , pp. 1135-1149
    • Nelson, A.R.1    Fingleton, B.2    Rothenberg, M.L.3    Matrisian, L.M.4
  • 73
    • 0015526559 scopus 로고
    • An endopeptidase from rheumatoid synovial tissue culture
    • Harris, E. D. Jr & Krane, S. M. An endopeptidase from rheumatoid synovial tissue culture. Biochim. Biophys. Acta 258, 566-576 (1972).
    • (1972) Biochim. Biophys. Acta , vol.258 , pp. 566-576
    • Harris E.D., Jr.1    Krane, S.M.2
  • 74
    • 0017325645 scopus 로고
    • Collagenase production by rheumatoid synovial cells: Stimulation by a human lymphocyte factor
    • Dayer, J. M., Graham, R., Russell, G. & Krane, S. M. Collagenase production by rheumatoid synovial cells: stimulation by a human lymphocyte factor. Science 195, 181-183 (1977).
    • (1977) Science , vol.195 , pp. 181-183
    • Dayer, J.M.1    Graham, R.2    Russell, G.3    Krane, S.M.4
  • 75
    • 0004280034 scopus 로고    scopus 로고
    • (eds Kelley, W., Harris, E. D. J., Ruddy, S. & Sledge, S.) (W. B. Saunders, Philadelphia)
    • Firestein, G. in Textbook of Rheumatology (eds Kelley, W., Harris, E. D. J., Ruddy, S. & Sledge, S.) 851-897 (W. B. Saunders, Philadelphia, 1997).
    • (1997) Textbook of Rheumatology , pp. 851-897
    • Firestein, G.1
  • 76
    • 0019195010 scopus 로고
    • Metastatic potential correlates with enzymatic degradation of basement membrane collagen
    • Liotta, L. A. et al. Metastatic potential correlates with enzymatic degradation of basement membrane collagen. Nature 284, 67-68 (1980).
    • (1980) Nature , vol.284 , pp. 67-68
    • Liotta, L.A.1
  • 77
    • 0000546937 scopus 로고    scopus 로고
    • Matrix metalloproteinases as emerging targets in anticancer therapy: Status and prospects
    • Sternlicht, M. D. & Bergers, G. Matrix metalloproteinases as emerging targets in anticancer therapy: status and prospects. Emerging Therapeutic Targets 4, 609-633 (2000).
    • (2000) Emerging Therapeutic Targets , vol.4 , pp. 609-633
    • Sternlicht, M.D.1    Bergers, G.2
  • 78
    • 0025641098 scopus 로고
    • A novel metalloproteinase gene specifically expressed in stromal cells of breast carcinomas
    • Basset, P. et al. A novel metalloproteinase gene specifically expressed in stromal cells of breast carcinomas. Nature 348, 699-704 (1990).
    • (1990) Nature , vol.348 , pp. 699-704
    • Basset, P.1
  • 79
    • 0028129494 scopus 로고
    • Overexpression of metalloproteinase inhibitor in B 16F10 cells does not affect extravasation but reduces tumor growth
    • Koop, S. et al. Overexpression of metalloproteinase inhibitor in B16F10 cells does not affect extravasation but reduces tumor growth. CancerRes. 54, 4791-4797 (1994).
    • (1994) Cancer Res. , vol.54 , pp. 4791-4797
    • Koop, S.1
  • 80
    • 0033134622 scopus 로고    scopus 로고
    • Matrix metalloproteinases in angiogenesis: A moving target for therapeutic intervention
    • Stetler-Stevenson, W. G. Matrix metalloproteinases in angiogenesis: a moving target for therapeutic intervention. J. Clin. Invest. 103, 1237-1241 (1999).
    • (1999) J. Clin. Invest. , vol.103 , pp. 1237-1241
    • Stetler-Stevenson, W.G.1
  • 81
    • 0001651169 scopus 로고    scopus 로고
    • Design and therapeutic application of matrix metalloproteinase inhibitors
    • Whittaker, M., Floyd, C. D., Brown, P. & Gearing, A. J. H. Design and therapeutic application of matrix metalloproteinase inhibitors. Chem. Rev. 99, 2735-2776 (1999).
    • (1999) Chem. Rev. , vol.99 , pp. 2735-2776
    • Whittaker, M.1    Floyd, C.D.2    Brown, P.3    Gearing, A.J.H.4
  • 82
    • 0024201509 scopus 로고
    • Inhibitors of collagenase IV and cell adhesion reduce the invasive activity of malignant tumour cells
    • Reich, R. et al. Inhibitors of collagenase IV and cell adhesion reduce the invasive activity of malignant tumour cells. Ciba Found. Symp. 141, 193-210 (1988).
    • (1988) Ciba Found. Symp. , vol.141 , pp. 193-210
    • Reich, R.1
  • 84
    • 0141873599 scopus 로고    scopus 로고
    • Matrix metalloproteinases: Trials and tribulations
    • in the press
    • Coussens, L. M., Fingleton, B. & Matrisian, L. M. Matrix metalloproteinases: trials and tribulations. Science (in the press).
    • Science
    • Coussens, L.M.1    Fingleton, B.2    Matrisian, L.M.3
  • 85
    • 0032612133 scopus 로고    scopus 로고
    • Latest FDA approvals for dentistry
    • Wynn, R. L. Latest FDA approvals for dentistry. Gen. Dent. 47, 19-22 (1999).
    • (1999) Gen. Dent. , vol.47 , pp. 19-22
    • Wynn, R.L.1
  • 86
    • 2442724379 scopus 로고
    • Transforming growth factor β modulates the expression of collagenase and metalloproteinase inhibitor
    • Edwards, D. R. et al. Transforming growth factor β modulates the expression of collagenase and metalloproteinase inhibitor. EMBO J. 6, 1899-1904 (1987).
    • (1987) EMBO J. , vol.6 , pp. 1899-1904
    • Edwards, D.R.1
  • 87
    • 0025344028 scopus 로고
    • TGF-β1 inhibition of transin-stromelysin gene expression is mediated through a los fos binding sequence
    • Kerr, L. D., Miller, D. B. & Matrisian, L. M. TGF-β1 inhibition of transin-stromelysin gene expression is mediated through a los fos binding sequence. Cell 61, 267-278 (1990).
    • (1990) Cell , vol.61 , pp. 267-278
    • Kerr, L.D.1    Miller, D.B.2    Matrisian, L.M.3
  • 88
    • 0040945730 scopus 로고    scopus 로고
    • Differential effects of transforming growth factor-β on the expression of collagenase-1 and collagenase-3 in human fibroblasts
    • t998
    • Uria, J. A., Jimenez, M. G., Balbin, M., Freije, J. M. & Lopez-Otin, C. Differential effects of transforming growth factor-β on the expression of collagenase-1 and collagenase-3 in human fibroblasts. J. Biol. Chem. 273, 9769-9777 (t998).
    • J. Biol. Chem. , vol.273 , pp. 9769-9777
    • Uria, J.A.1    Jimenez, M.G.2    Balbin, M.3    Freije, J.M.4    Lopez-Otin, C.5
  • 89
    • 0033953612 scopus 로고    scopus 로고
    • Transforming growth factor β inhibitory element in the rabbit matrix metalloproteinase-1 (collagenase-1) gene functions as a repressor of constitutive transcription
    • White, L. A., Mitchell, T. I. & Brinckerhoff, C. E. Transforming growth factor β inhibitory element in the rabbit matrix metalloproteinase-1 (collagenase-1) gene functions as a repressor of constitutive transcription. Biochim. Biophys. Acta 1490, 259-268 (2000).
    • (2000) Biochim. Biophys. Acta , vol.1490 , pp. 259-268
    • White, L.A.1    Mitchell, T.I.2    Brinckerhoff, C.E.3
  • 90
    • 0025015647 scopus 로고
    • Anti-tumor promotion and anti-inflammation: Down-modulation of AP-1 (Fos/Jun) activity by glucocorticoid hormone
    • Jonat, C. et al. Anti-tumor promotion and anti-inflammation: down-modulation of AP-1 (Fos/Jun) activity by glucocorticoid hormone. Cell 62, 1189-1204 (1990).
    • (1990) Cell , vol.62 , pp. 1189-1204
    • Jonat, C.1
  • 91
    • 0025188132 scopus 로고
    • Transcriptional interference between c-Jun and the glucocorticoid receptor: Mutual inhibition of DNA binding due to direct protein-protein interaction
    • Yang-Yen, H. F. et al. Transcriptional interference between c-Jun and the glucocorticoid receptor: mutual inhibition of DNA binding due to direct protein-protein interaction. Cell 62, 1205-1215 (1990).
    • (1990) Cell , vol.62 , pp. 1205-1215
    • Yang-Yen, H.F.1
  • 92
    • 0025130179 scopus 로고
    • Functional antagonism between oncoprotein c-Jun and the glucocorticoid receptor
    • Schüle, R. et al. Functional antagonism between oncoprotein c-Jun and the glucocorticoid receptor. Cell 62, 1217-1226(1990).
    • (1990) Cell , vol.62 , pp. 1217-1226
    • Schüle, R.1
  • 93
    • 0019312874 scopus 로고
    • Inhibition by retinoic acid of collagenase production in rheumatoid synovial cells
    • Brinckerhoff, C. E., McMillan, R. M., Dayer, J. M. & Harris, E. D. Jr. Inhibition by retinoic acid of collagenase production in rheumatoid synovial cells. N. Engl. J. Med. 303, 432-436 (1980).
    • (1980) N. Engl. J. Med. , vol.303 , pp. 432-436
    • Brinckerhoff, C.E.1    McMillan, R.M.2    Dayer, J.M.3    Harris E.D., Jr.4
  • 94
    • 0025602652 scopus 로고
    • Negative regulation of the rat stromelysin gene promoter by retinoic acid is mediated by an AP1 binding site
    • Nicholson, R. C. et al. Negative regulation of the rat stromelysin gene promoter by retinoic acid is mediated by an AP1 binding site. EMBO J. 9, 4443-4454 (1990).
    • (1990) EMBO J. , vol.9 , pp. 4443-4454
    • Nicholson, R.C.1
  • 95
    • 0025883418 scopus 로고
    • Retinoic acid is a negative regulator of AP-1-responsive genes
    • Schule, R. et al. Retinoic acid is a negative regulator of AP-1-responsive genes. Proc. Natl Acad. Sci. USA 88, 6092-6096 (1991).
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 6092-6096
    • Schule, R.1
  • 96
    • 0030069213 scopus 로고    scopus 로고
    • Molecular basis of sun-induced premature skin ageing and retinoid antagonism
    • Fisher, G. J. et al. Molecular basis of sun-induced premature skin ageing and retinoid antagonism. Nature 379, 335-339 (1996).
    • (1996) Nature , vol.379 , pp. 335-339
    • Fisher, G.J.1
  • 97
    • 0030695138 scopus 로고    scopus 로고
    • Pathophysiology of premature skin aging induced by ultraviolet light
    • Fisher, G. J. et al. Pathophysiology of premature skin aging induced by ultraviolet light. N. Engl. J. Med. 337, 1419-1428 (1997).
    • (1997) N. Engl. J. Med. , vol.337 , pp. 1419-1428
    • Fisher, G.J.1
  • 98
    • 0029740183 scopus 로고    scopus 로고
    • Activation of specific RXR heterodimers by an antagonist of RXR homodimers
    • Lala, D. S. et al. Activation of specific RXR heterodimers by an antagonist of RXR homodimers. Nature 383, 450-453 (1996).
    • (1996) Nature , vol.383 , pp. 450-453
    • Lala, D.S.1
  • 99
    • 0030795335 scopus 로고    scopus 로고
    • Specific activation of retinoic acid receptors (RARs) and retinoid X receptors reveals a unique role for RARγ in induction of differentiation and apoptosis of S 91 melanoma cells
    • Spanjaard. R. A. et al. Specific activation of retinoic acid receptors (RARs) and retinoid X receptors reveals a unique role for RARγ in induction of differentiation and apoptosis of S91 melanoma cells. J. Biol. Chem. 272, 18990-18999 (1997).
    • (1997) J. Biol. Chem. , vol.272 , pp. 18990-18999
    • Spanjaard, R.A.1
  • 100
    • 0035030872 scopus 로고    scopus 로고
    • A synthetic triterpenoid selectively inhibits the induction of matrix metalloproteinases 1 and 13 by inflammatory cytokines
    • Mix, K. S. et al. A synthetic triterpenoid selectively inhibits the induction of matrix metalloproteinases 1 and 13 by inflammatory cytokines. Arthritis Rheum. 44, 1096-1104 (2001).
    • (2001) Arthritis Rheum. , vol.44 , pp. 1096-1104
    • Mix, K.S.1
  • 101
    • 0028625431 scopus 로고
    • Low molecular weight inhibitors in corneal ulceration
    • Galardy. R. E. et al. Low molecular weight inhibitors in corneal ulceration. Ann. NY Acad. Sci. 732, 315-323 (1994).
    • (1994) Ann. NY Acad. Sci. , vol.732 , pp. 315-323
    • Galardy, R.E.1
  • 102
    • 0141977428 scopus 로고    scopus 로고
    • British Biotech PLC. http://www.britishbiotech.com/product.htm.2002.
    • (2002)
  • 103
    • 0013804986 scopus 로고
    • Specific degradation of the collagen molecule by tadpole collagenolytic enzyme
    • Gross, J. & Nagai, Y. Specific degradation of the collagen molecule by tadpole collagenolytic enzyme. Proc. Natl Acad. Sci. USA 54, 1197-1204 (1965).
    • (1965) Proc. Natl. Acad. Sci. USA , vol.54 , pp. 1197-1204
    • Gross, J.1    Nagai, Y.2
  • 104
    • 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. et al. 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).
    • (2001) EMBO J. , vol.20 , pp. 4782-4793
    • Itoh, Y.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.