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Volumn 10, Issue 3, 2000, Pages 121-128

Matrix-degrading metalloproteinases and their roles in joint destruction

Author keywords

A disintegrin and metalloproteinase; Joint destruction; Matrix degradation; Matrix metalloproteinase; Osteoarthritis; Rheumatoid arthritis

Indexed keywords


EID: 84995629928     PISSN: 14397595     EISSN: 14397609     Source Type: Journal    
DOI: 10.3109/s101650070018     Document Type: Review
Times cited : (27)

References (83)
  • 1
    • 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 – 42.
    • (1997) Cell , vol.91 , pp. 439-442
    • Werb, Z.1
  • 2
    • 0031760698 scopus 로고    scopus 로고
    • Extracellular matrix remodeling during morphogenesis
    • Werb Z, Chin JR. Extracellular matrix remodeling during morphogenesis. Ann N Y Acad Sci 1998; 857: 110 – 8.
    • (1998) Ann N Y Acad Sci , vol.857 , pp. 110-118
    • Werb, Z.1    Chin, J.R.2
  • 3
    • 0026342205 scopus 로고
    • The collagens of articular cartilage
    • Eyre DR. The collagens of articular cartilage. Semin Arthritis Rheum 1991; 21: 2 – 11.
    • (1991) Semin Arthritis Rheum , vol.21 , pp. 2-11
    • Eyre, D.R.1
  • 4
    • 0027267162 scopus 로고
    • Function of proteoglycans in the extracellular matrix
    • Yanagishita M. Function of proteoglycans in the extracellular matrix. Acta Pathol Jpn 1993; 43: 283 – 93.
    • (1993) Acta Pathol Jpn , vol.43 , pp. 283-293
    • Yanagishita, M.1
  • 6
    • 0025226011 scopus 로고
    • Localization of type VI collagen in the lining cell layer of normal and rheumatoid synovium
    • Okada Y, Naka K, Minamoto T, Ueda Y, Oda Y, Nakanishi I, et al. Localization of type VI collagen in the lining cell layer of normal and rheumatoid synovium. Lab Invest 1990; 63: 647 – 56.
    • (1990) Lab Invest , vol.63 , pp. 647-656
    • Okada, Y.1    Naka, K.2    Minamoto, T.3    Ueda, Y.4    Oda, Y.5    Nakanishi, I.6
  • 7
    • 0025847582 scopus 로고
    • Matrix metalloproteinases and their inhibitors in connective tissue remodeling
    • Woessner JF, Jr. Matrix metalloproteinases and their inhibitors in connective tissue remodeling. Faseb J 1991; 5: 2145 – 54.
    • (1991) Faseb J , vol.5 , pp. 2145-2154
    • Woessner, J.F.1
  • 8
    • 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 – 9.
    • (1998) Curr Opin Cell Biol , vol.10 , pp. 654-659
    • Black, R.A.1    White, J.M.2
  • 9
    • 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, et al. A matrix metalloproteinase expressed on the surface of invasive tumour cells. Nature 1994; 370: 61 – 5.
    • (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
  • 10
    • 0029133344 scopus 로고
    • cDNA sequence and mFtNA tissue distribution of a novel human matrix metalloproteinase with a potential transmembrane segment
    • Will H, Hinzmann B. cDNA sequence and mFtNA tissue distribution of a novel human matrix metalloproteinase with a potential transmembrane segment. Eur J Biochem 1995; 231: 602 – 8.
    • (1995) Eur J Biochem , vol.231 , pp. 602-608
    • Will, H.1    Hinzmann, B.2
  • 12
    • 0030022539 scopus 로고    scopus 로고
    • Molecular cloning of a novel membrane-type matrix metallo-proteinase from a human breast carcinoma
    • Puente XS, Pendas AM, Llano E, Velasco G, Lopez-Otin C. Molecular cloning of a novel membrane-type matrix metallo-proteinase from a human breast carcinoma. Cancer Res 1996; 56: 944 – 9.
    • (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
  • 13
    • 0033605561 scopus 로고    scopus 로고
    • Identification and characterization of the fifth membrane-type matrix metalloproteinase MT5-MIMP
    • Pei D. Identification and characterization of the fifth membrane-type matrix metalloproteinase MT5-MIMP. J Biol Chem 1999; 274: 8925 – 32.
    • (1999) J Biol Chem , vol.274 , pp. 8925-8932
    • Pei, D.1
  • 14
    • 0033256294 scopus 로고    scopus 로고
    • Leukolysin/MMP25/MT6-MMP: a novel matrix metallo-proteinase specifically expressed in the leukocyte lineage
    • Pei D. Leukolysin/MMP25/MT6-MMP: a novel matrix metallo-proteinase specifically expressed in the leukocyte lineage. Cell Res 1999; 9: 291 – 303.
    • (1999) Cell Res , vol.9 , pp. 291-303
    • Pei, D.1
  • 15
    • 0033582513 scopus 로고    scopus 로고
    • Cloning and characterization of human MMP-23, a new matrix metalloproteinase predominantly expressed in repro-ductive tissues and lacking conserved domains in other family members
    • Velasco G, Pendas AM, Fueyo A, Knauper V, Murphy G, Lopez-Otin C. Cloning and characterization of human MMP-23, a new matrix metalloproteinase predominantly expressed in repro-ductive tissues and lacking conserved domains in other family members. J Biol Chem 1999; 274: 4570 – 6.
    • (1999) J Biol Chem , vol.274 , pp. 4570-4576
    • Velasco, G.1    Pendas, A.M.2    Fueyo, A.3    Knauper, V.4    Murphy, G.5    Lopez-Otin, C.6
  • 16
    • 0033607524 scopus 로고    scopus 로고
    • Membrane type 4 matrix metalloproteinase (MT4-MMP, MMP-17) is a glycosylphosphatidylinositol-anchored proteinase
    • Itoh Y, Kajita M, Kinoh H, Mori H, Okada A, Seiki M. Membrane type 4 matrix metalloproteinase (MT4-MMP, MMP-17) is a glycosylphosphatidylinositol-anchored proteinase. J Biol Chem 1999; 274: 34260 – 6.
    • (1999) J Biol Chem , vol.274 , pp. 34260-34266
    • Itoh, Y.1    Kajita, M.2    Kinoh, H.3    Mori, H.4    Okada, A.5    Seiki, M.6
  • 17
    • 0031041647 scopus 로고    scopus 로고
    • Identification and characterization of a novel human matrix metalloproteinase with unique structural characteristics, chromo-somal location, and tissue distribution
    • Pendas AM, Knauper V, Puente XS, Llano E, Mattei MG, Apte S, et al. Identification and characterization of a novel human matrix metalloproteinase with unique structural characteristics, chromo-somal location, and tissue distribution. J Biol Chem 1997; 272: 4281 – 6.
    • (1997) J Biol Chem , vol.272 , pp. 4281-4286
    • Pendas, A.M.1    Knauper, V.2    Puente, X.S.3    Llano, E.4    Mattei, M.G.5    Apte, S.6
  • 18
    • 0030032444 scopus 로고    scopus 로고
    • Cloning, expression, and type II collagenolytic activity of matrix metalloproteinase-13 from human osteoarthritic cartilage
    • Mitchell PG, Magna HA, Reeves LM, Lopresti-Morrow LL, Yocum SA, Rosner PJ, et al. Cloning, expression, and type II collagenolytic activity of matrix metalloproteinase-13 from human osteoarthritic cartilage. J Clin Invest 1996; 97: 761 – 8.
    • (1996) J Clin Invest , vol.97 , pp. 761-768
    • Mitchell, P.G.1    Magna, H.A.2    Reeves, L.M.3    Lopresti-Morrow, L.L.4    Yocum, S.A.5    Rosner, P.J.6
  • 20
    • 0030024311 scopus 로고    scopus 로고
    • Degra-dation of cartilage aggrecan by collagenase-3 (MMP-13)
    • Fosang AJ, Last K, Knauper V, Murphy G, Neame PJ. Degra-dation of cartilage aggrecan by collagenase-3 (MMP-13). FEBS Lett 1996; 380: 17 – 20.
    • (1996) FEBS Lett , vol.380 , pp. 17-20
    • Fosang, A.J.1    Last, K.2    Knauper, V.3    Murphy, G.4    Neame, P.J.5
  • 21
    • 0030898796 scopus 로고    scopus 로고
    • The role of the C-terminal domain of human collagenase-3 (MMP-13) in the activation of procollagenase-3, substrate specificity, and tissue inhibitor of metalloproteinase interaction
    • Knauper V, Cowell S, Smith B, Lopez-Otin C, O'Shea M, Morris H, et al. The role of the C-terminal domain of human collagenase-3 (MMP-13) in the activation of procollagenase-3, substrate specificity, and tissue inhibitor of metalloproteinase interaction. J Biol Chem 1997; 272: 7608 – 16.
    • (1997) J Biol Chem , vol.272 , pp. 7608-7616
    • Knauper, V.1    Cowell, S.2    Smith, B.3    Lopez-Otin, C.4    O'Shea, M.5    Morris, H.6
  • 24
    • 0025914976 scopus 로고
    • Substrate specificities and activation mechanisms of matrix metallopro-teinases
    • Nagase H, Ogata Y, Suzuki K, Enghild JJ, Salvesen G. Substrate specificities and activation mechanisms of matrix metallopro-teinases. Biochem Soc Trans 1991; 19: 715 – 8.
    • (1991) Biochem Soc Trans , vol.19 , pp. 715-718
    • Nagase, H.1    Ogata, Y.2    Suzuki, K.3    Enghild, J.J.4    Salvesen, G.5
  • 25
    • 0026701977 scopus 로고
    • The interglobular domain of cartilage aggrecan is cleaved by PUMP, gelatinases, and cathepsin B
    • Fosang AJ, Neame PJ, Last K, Hardingham TE, Murphy G, Hamilton JA. The interglobular domain of cartilage aggrecan is cleaved by PUMP, gelatinases, and cathepsin B. J Biol Chem 1992; 267: 19470 – 4.
    • (1992) J Biol Chem , vol.267 , pp. 19470-19474
    • Fosang, A.J.1    Neame, P.J.2    Last, K.3    Hardingham, T.E.4    Murphy, G.5    Hamilton, J.A.6
  • 26
    • 0027428710 scopus 로고
    • Matrix metalloproteinases cleave at two distinct sites on human cartilage link protein
    • Nguyen Q, Murphy G, Hughes CE, Mort JS, Roughley PJ. Matrix metalloproteinases cleave at two distinct sites on human cartilage link protein. Biochem J 1993; 295: 595 – 8.
    • (1993) Biochem J , vol.295 , pp. 595-598
    • Nguyen, Q.1    Murphy, G.2    Hughes, C.E.3    Mort, J.S.4    Roughley, P.J.5
  • 27
    • 0029006135 scopus 로고
    • Human stromelysins 1 and 2
    • Nagase H. Human stromelysins 1 and 2. Methods Enzymol 1995; 248: 449 – 70.
    • (1995) Methods Enzymol , vol.248 , pp. 449-470
    • Nagase, H.1
  • 28
    • 0025895193 scopus 로고
    • Matrix metallo-proteinase degradation of elastin, type IV collagen and proteoglycan. A quantitative comparison of the activities of 95 kDa and 72 kDa gelatinases, stromelysins-1 and -2 and punctuated metalloproteinase (PUMP)
    • Murphy G, Cockett MI, Ward RV, Docherty AJ. Matrix metallo-proteinase degradation of elastin, type IV collagen and proteoglycan. A quantitative comparison of the activities of 95 kDa and 72 kDa gelatinases, stromelysins-1 and -2 and punctuated metalloproteinase (PUMP). Biochem J 1991; 277: 277 – 9.
    • (1991) Biochem J , vol.277 , pp. 277-279
    • Murphy, G.1    Cockett, M.I.2    Ward, R.V.3    Docherty, A.J.4
  • 29
    • 0023024460 scopus 로고
    • A metalloproteinase from human rheumatoid synovial fibroblasts that digests connective tissue matrix components
    • Okada Y, Nagase H, Harris ED, Jr. A metalloproteinase from human rheumatoid synovial fibroblasts that digests connective tissue matrix components. Purification and characterization. J Biol Chem 1986; 261: 14245 – 55.
    • (1986) Purification and characterization. J Biol Chem , vol.261 , pp. 14245-14255
    • Okada, Y.1    Nagase, H.2    Harris, E.D.3
  • 30
    • 0025949206 scopus 로고
    • Sites of stromelysin cleavage in collagen types II, IX, X, and XI of cartilage
    • Wu JJ, Lark MW, Chun LE, Eyre DR. Sites of stromelysin cleavage in collagen types II, IX, X, and XI of cartilage. J Biol Chem 1991; 266: 5625 – 8.
    • (1991) J Biol Chem , vol.266 , pp. 5625-5628
    • Wu, J.J.1    Lark, M.W.2    Chun, L.E.3    Eyre, D.R.4
  • 31
    • 0030957218 scopus 로고    scopus 로고
    • Activation mechanisms of matrix metalloproteinases
    • Nagase H. Activation mechanisms of matrix metalloproteinases. Biol Chem 1997; 378: 151 – 60.
    • (1997) Biol Chem , vol.378 , pp. 151-160
    • Nagase, H.1
  • 32
    • 0031025218 scopus 로고    scopus 로고
    • Membrane type 1 matrix metalloproteinase digests interstitial collagens and other extracellular matrix macromolecules
    • Ohuchi E, Imai K, Fujii Y, Sato H, Seiki M, Okada Y. Membrane type 1 matrix metalloproteinase digests interstitial collagens and other extracellular matrix macromolecules. J Biol Chem 1997; 272: 2446 – 51.
    • (1997) J Biol Chem , vol.272 , pp. 2446-2451
    • Ohuchi, E.1    Imai, K.2    Fujii, Y.3    Sato, H.4    Seiki, M.5    Okada, Y.6
  • 33
    • 0029885707 scopus 로고    scopus 로고
    • Transmembrane-deletion mutants of the membrane-type matrix metalloproteinase-1 process progelatinase A and express intrinsic matrix-degrading activity
    • Pei D, Weiss SJ. Transmembrane-deletion mutants of the membrane-type matrix metalloproteinase-1 process progelatinase A and express intrinsic matrix-degrading activity. J Biol Chem 1996; 271: 9135 – 40.
    • (1996) J Biol Chem , vol.271 , pp. 9135-9140
    • Pei, D.1    Weiss, S.J.2
  • 34
    • 0032479462 scopus 로고    scopus 로고
    • Membrane-type 1 MMP (MMP-14) cleaves at three sites in the aggrecan inter- globular domain
    • Fosang AJ, Last K, Fujii Y, Seiki M, Okada Y. Membrane-type 1 MMP (MMP-14) cleaves at three sites in the aggrecan inter- globular domain. FEBS Lett 1998; 430: 186–90.55.
    • (1998) FEBS Lett , vol.430 , pp. 186-90.55
    • Fosang, A.J.1    Last, K.2    Fujii, Y.3    Seiki, M.4    Okada, Y.5
  • 35
    • 0033564010 scopus 로고    scopus 로고
    • Characterization of a truncated recombinant form of human 57 membrane type 3 matrix metalloproteinase
    • Shimada T, Nakamura H, Ohuchi E, Fujii Y, Murakami Y, Sato H, et al. Characterization of a truncated recombinant form of human 57. membrane type 3 matrix metalloproteinase. Eur J Biochem 1999; 262: 907 – 14.
    • (1999) Eur J Biochem , vol.262 , pp. 907-914
    • Shimada, T.1    Nakamura, H.2    Ohuchi, E.3    Fujii, Y.4    Murakami, Y.5    Sato, H.6
  • 36
    • 0032585730 scopus 로고    scopus 로고
    • Expression, purification and 58. characterization of recombinant mouse MT5-MIMP protein products
    • Wang X, Yi J, Lei J, Pei D. Expression, purification and 58. characterization of recombinant mouse MT5-MIMP protein products. FEBS Lett 1999; 462: 261 – 6.
    • (1999) FEBS Lett , vol.462 , pp. 261-266
    • Wang, X.1    Yi, J.2    Lei, J.3    Pei, D.4
  • 37
    • 0028913443 scopus 로고
    • Matrix metalloproteinase 7 (matrilysin) from human rectal carcinoma cells. Activation of the precursor, interaction with other matrix metalloproteinases and enzymic properties
    • Imai K, Yokohama Y, Nakanishi I, Ohuchi E, Fujii Y, Nakai N, et 59. al. Matrix metalloproteinase 7 (matrilysin) from human rectal carcinoma cells. Activation of the precursor, interaction with other matrix metalloproteinases and enzymic properties. J Biol Chem 1995; 270: 6691 – 7.
    • (1995) J Biol Chem , vol.270 , pp. 6691-6697
    • Imai, K.1    Yokohama, Y.2    Nakanishi, I.3    Ohuchi, E.4    Fujii, Y.5    Nakai, N.6
  • 38
    • 0027264485 scopus 로고
    • The 28-kDa N-terminal domain of mouse stromelysin-3 has the general properties of a weak metalloproteinase
    • Murphy G, Segain JP, O'Shea M, Cockett M, Ioannou C, Lefebvre 60. O, et al. The 28-kDa N-terminal domain of mouse stromelysin-3 has the general properties of a weak metalloproteinase. J Biol Chem 1993; 268: 15435–41.61.
    • (1993) J Biol Chem , vol.268 , pp. 15435-41.61
    • Murphy, G.1    Segain, J.P.2    O'Shea, M.3    Cockett, M.4    Ioannou, C.5    Lefebvre, O.6
  • 39
    • 0027515289 scopus 로고
    • Cloning and characterization of a unique elastolytic metalloproteinase produced by human alveolar macrophages
    • Shapiro SD, Kobayashi DK, Ley TJ. Cloning and characterization of a unique elastolytic metalloproteinase produced by human alveolar macrophages. J Biol Chem 1993; 268: 23824-9. 62.
    • (1993) J Biol Chem , vol.268 , Issue.23824-9 , pp. 62
    • Shapiro, S.D.1    Kobayashi, D.K.2    Ley, T.J.3
  • 41
    • 0030720933 scopus 로고    scopus 로고
    • Identification and structural and functional characterization of human enamelysin (MMP-20)
    • Llano E, Pendas AM, Knauper V, Sorsa T, Salo T, Salido E, et al. Identification and structural and functional characterization of human enamelysin (MMP-20). Biochemistry 1997; 36: 15101-8. 64.
    • (1997) Biochemistry , vol.36 , Issue.15101-8 , pp. 64
    • Llano, E.1    Pendas, A.M.2    Knauper, V.3    Sorsa, T.4    Salo, T.5    Salido, E.6
  • 42
    • 0032053550 scopus 로고    scopus 로고
    • Activation of the precursor of human stromelysin 2 and its interactions with other matrix metalloproteinases
    • Nakamura H, Fujii Y, Ohuchi E, Yamamoto E, Okada Y. Activation of the precursor of human stromelysin 2 and its interactions with other matrix metalloproteinases. Eur J Biochem 1998; 253: 67–75.65.
    • (1998) Eur J Biochem , vol.253 , pp. 67-75.65
    • Nakamura, H.1    Fujii, Y.2    Ohuchi, E.3    Yamamoto, E.4    Okada, Y.5
  • 43
    • 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 – 7.
    • (1995) Nature , vol.375 , pp. 244-247
    • Pei, D.1    Weiss, S.J.2
  • 44
    • 0030577022 scopus 로고    scopus 로고
    • Activation of a recombinant membrane type 1-matrix metalloproteinase 66. (MT1-MMP) by furin and its interaction with tissue inhibitor of metalloproteinases (TIMP)-2
    • Sato H, Kinoshita T, Takino T, Nakayama K, Seiki M. Activation of a recombinant membrane type 1-matrix metalloproteinase 66. (MT1-MMP) by furin and its interaction with tissue inhibitor of metalloproteinases (TIMP)-2. FEBS Lett 1996; 393: 101 – 4.
    • (1996) FEBS Lett , vol.393 , pp. 101-104
    • Sato, H.1    Kinoshita, T.2    Takino, T.3    Nakayama, K.4    Seiki, M.5
  • 45
    • 0032513136 scopus 로고    scopus 로고
    • Inhibition of matrix metalloproteinase 2 maturation and HT1080 invasiveness by a synthetic furin inhibitor
    • Maquoi E, Noel A, Frankenne F, Angliker H, Murphy G, Foidart JM. Inhibition of matrix metalloproteinase 2 maturation and HT1080 invasiveness by a synthetic furin inhibitor. FEBS Lett 67. 1998; 424: 262 – 6.
    • (1998) FEBS Lett , vol.424 , pp. 262-266
    • Maquoi, E.1    Noel, A.2    Frankenne, F.3    Angliker, H.4    Murphy, G.5    Foidart, J.M.6
  • 46
    • 0031985228 scopus 로고    scopus 로고
    • The TIMP2 membrane type 1 metallo-proteinase “receptor” regulates the concentration and efficient 68. activation of progelatinase A. A kinetic study
    • Butler GS, Butler MJ, Atkinson SJ, Will H, Tamura T, van Westrum SS, et al. The TIMP2 membrane type 1 metallo-proteinase “receptor” regulates the concentration and efficient 68. activation of progelatinase A. A kinetic study. J Biol Chem 1998; 273: 871 – 80.
    • (1998) J Biol Chem , vol.273 , pp. 871-880
    • Butler, G.S.1    Butler, M.J.2    Atkinson, S.J.3    Will, H.4    Tamura, T.5    van Westrum, S.S.6
  • 47
    • 0032568932 scopus 로고    scopus 로고
    • 69. TIMP-2 promotes activation of progelatinase A by membrane-type 1 matrix metalloproteinase immobilized on agarose beads
    • Kinoshita T, Sato H, Okada A, Ohuchi E, Imai K, Okada Y, et al. 69. TIMP-2 promotes activation of progelatinase A by membrane-type 1 matrix metalloproteinase immobilized on agarose beads. J Biol Chem 1998; 273: 16098 – 103.
    • (1998) J Biol Chem , vol.273 , pp. 16098-16103
    • Kinoshita, T.1    Sato, H.2    Okada, A.3    Ohuchi, E.4    Imai, K.5    Okada, Y.6
  • 48
    • 0029022713 scopus 로고
    • Tissue inhibitors of matrix metallo- endopeptidases
    • Murphy G, Willenbrock F. Tissue inhibitors of matrix metallo- endopeptidases. Methods Enzymol 1995; 248: 496-510. 70.
    • (1995) Methods Enzymol , vol.248 , Issue.496-510 , pp. 70
    • Murphy, G.1    Willenbrock, F.2
  • 49
    • 53249090335 scopus 로고    scopus 로고
    • Computational sequence analysis of the tissue inhibitor of metalloproteinase family
    • Douglas DA, Shi YE, Sang QA. Computational sequence analysis of the tissue inhibitor of metalloproteinase family. J Protein Chem 1997; 16: 237 – 55.
    • (1997) J Protein Chem , vol.16 , pp. 237-255
    • Douglas, D.A.1    Shi, Y.E.2    Sang, Q.A.3
  • 50
    • 0030717692 scopus 로고    scopus 로고
    • inhibitors of metalloproteinases, structure, regulation and biological functions. Eur J Cell Biol
    • Gomez DE, Alonso DF, Yoshiji H, Thorgeirsson UP. Tissue 71. inhibitors of metalloproteinases: structure, regulation and biological functions. Eur J Cell Biol 1997; 74: 111 – 22.
    • (1997) Tissue 71. , vol.74 , pp. 111-122
    • Gomez, D.E.1    Alonso, D.F.2    Yoshiji, H.3    Thorgeirsson, U.P.4
  • 51
    • 0030016342 scopus 로고    scopus 로고
    • The soluble catalytic domain of membrane type 1 matrix metalloproteinase 72. cleaves the propeptide of progelatinase A and initiates auto-proteolytic activation. Regulation by TIMP-2 and TIMP-3
    • Will H, Atkinson SJ, Butler GS, Smith B, Murphy G. The soluble catalytic domain of membrane type 1 matrix metalloproteinase 72. cleaves the propeptide of progelatinase A and initiates auto-proteolytic activation. Regulation by TIMP-2 and TIMP-3. J Biol Chem 1996; 271: 17119 – 23.
    • (1996) J Biol Chem , vol.271 , pp. 17119-17123
    • Will, H.1    Atkinson, S.J.2    Butler, G.S.3    Smith, B.4    Murphy, G.5
  • 52
    • 0033851494 scopus 로고    scopus 로고
    • Production of tissue inhibitor of metallopro- 73. teinases 3 is selectively enhanced by calcium pentosan polysulfate in human rheumatoid synovial fibroblasts
    • Takizawa M, Ohuchi E, Yamanaka H, Nakamura H, Ikeda E, Ghosh P, Okada Y. Production of tissue inhibitor of metallopro- 73. teinases 3 is selectively enhanced by calcium pentosan polysulfate in human rheumatoid synovial fibroblasts. Arthritis Rheum 2000; 43: 812 – 20.
    • (2000) Arthritis Rheum , vol.43 , pp. 812-820
    • Takizawa, M.1    Ohuchi, E.2    Yamanaka, H.3    Nakamura, H.4    Ikeda, E.5    Ghosh, P.6    Okada, Y.7
  • 54
    • 0031016568 scopus 로고    scopus 로고
    • Purification of ADAM 10 from bovine spleen as a TNFalpha convertase
    • Lunn CA, Fan X, Dalie B, Miller K, Zavodny PJ, Narula SK, et al. Purification of ADAM 10 from bovine spleen as a TNFalpha convertase. FEBS Lett 1997; 400: 333 – 5.
    • (1997) FEBS Lett , vol.400 , pp. 333-335
    • Lunn, C.A.1    Fan, X.2    Dalie, B.3    Miller, K.4    Zavodny, P.J.5    Narula, S.K.6
  • 55
    • 8044250278 scopus 로고    scopus 로고
    • Cloning of a disintegrin metalloproteinase that processes precursor tumour-necrosis factor-alpha
    • Moss ML, Jin SL, Milla ME, Bickett DM, Burkhart W, Carter HL, et al. Cloning of a disintegrin metalloproteinase that processes precursor tumour-necrosis factor-alpha. Nature 1997; 385: 733 – 6.
    • (1997) Nature , vol.385 , pp. 733-736
    • Moss, M.L.1    Jin, S.L.2    Milla, M.E.3    Bickett, D.M.4    Burkhart, W.5    Carter, H.L.6
  • 56
    • 8044257704 scopus 로고    scopus 로고
    • A metalloproteinase disintegrin that releases tumour-necrosis factor-alpha from cells
    • Black RA, Rauch CT, Kozlosky CJ, Peschon JJ, Slack JL, Wolfson MF, et al. A metalloproteinase disintegrin that releases tumour-necrosis factor-alpha from cells. Nature 1997; 385: 729 – 33.
    • (1997) Nature , vol.385 , pp. 729-733
    • Black, R.A.1    Rauch, C.T.2    Kozlosky, C.J.3    Peschon, J.J.4    Slack, J.L.5    Wolfson, M.F.6
  • 58
    • 0030959540 scopus 로고    scopus 로고
    • cDNA cloning and expression of bovine procollagen I N-proteinase: a new member of the superfamily of zinc-metalloproteinases with binding sites for cells and other matrix components
    • Colige A, Li SW, Sieron AL, Nusgens BV, Prockop DJ, Lapiere CM. cDNA cloning and expression of bovine procollagen I N-proteinase: a new member of the superfamily of zinc-metalloproteinases with binding sites for cells and other matrix components. Proc Natl Acad Sci USA 1997; 94: 2374 – 9.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 2374-2379
    • Colige, A.1    Li, S.W.2    Sieron, A.L.3    Nusgens, B.V.4    Prockop, D.J.5    Lapiere, C.M.6
  • 59
    • 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, Abbaszade I, Hollis JM, Liu R, et al. Purification and cloning of aggrecanase-1: a member of the ADAMTS family of proteins. Science 1999; 284: 1664 – 6.
    • (1999) Science , vol.284 , pp. 1664-1666
    • Tortorella, M.D.1    Burn, T.C.2    Pratta, M.A.3    Abbaszade, I.4    Hollis, J.M.5    Liu, R.6
  • 60
    • 0033551844 scopus 로고    scopus 로고
    • Cloning and characterization of ADAMTS11, an aggrecanase from the ADAMTS family
    • Abbaszade I, Liu RQ, Yang F, Rosenfeld SA, Ross OH, Link JR, et al. Cloning and characterization of ADAMTS11, an aggrecanase from the ADAMTS family. J Biol Chem 1999; 274: 23443 – 50.
    • (1999) J Biol Chem , vol.274 , pp. 23443-23450
    • Abbaszade, I.1    Liu, R.Q.2    Yang, F.3    Rosenfeld, S.A.4    Ross, O.H.5    Link, J.R.6
  • 61
    • 0033603356 scopus 로고    scopus 로고
    • ADAMTS-1 is an active metalloproteinase associated with the extracellular matrix
    • Kuno K, Terashima Y, Matsushima K. ADAMTS-1 is an active metalloproteinase associated with the extracellular matrix. J Biol Chem 1999; 274: 18821 – 6.
    • (1999) J Biol Chem , vol.274 , pp. 18821-18826
    • Kuno, K.1    Terashima, Y.2    Matsushima, K.3
  • 64
    • 0024473876 scopus 로고
    • Immunolocalization of matrix metalloproteinase 3 (stromelysin) in rheumatoid synovioblasts (B cells): correlation with rheumatoid arthritis
    • Okada Y, Takeuchi N, Tomita K, Nakanishi I, Nagase H. Immunolocalization of matrix metalloproteinase 3 (stromelysin) in rheumatoid synovioblasts (B cells): correlation with rheumatoid arthritis. Ann Rheum Dis 1989; 48: 645 – 53.
    • (1989) Ann Rheum Dis , vol.48 , pp. 645-653
    • Okada, Y.1    Takeuchi, N.2    Tomita, K.3    Nakanishi, I.4    Nagase, H.5
  • 65
    • 0025039296 scopus 로고
    • Immunohistochemical demonstration of collagenase and tissue inhibitor of metalloproteinases (TIMP) in synovial lining cells of rheumatoid synovium
    • Okada Y, Gonoji Y, Nakanishi I, Nagase H, Hayakawa T. Immunohistochemical demonstration of collagenase and tissue inhibitor of metalloproteinases (TIMP) in synovial lining cells of rheumatoid synovium. Virchows Arch B Cell Pathol 1990; 59: 305 – 12.
    • (1990) Virchows Arch B Cell Pathol , vol.59 , pp. 305-312
    • Okada, Y.1    Gonoji, Y.2    Nakanishi, I.3    Nagase, H.4    Hayakawa, T.5
  • 66
    • 0028854885 scopus 로고
    • Immuno-localisation studies on six matrix metalloproteinases and their inhibitors, TIMP-1 and TIMP-2, in synovia from patients with osteo- and rheumatoid arthritis
    • Hembry RM, Bagga MR, Reynolds JJ, Hamblen DL. Immuno-localisation studies on six matrix metalloproteinases and their inhibitors, TIMP-1 and TIMP-2, in synovia from patients with osteo- and rheumatoid arthritis. Ann Rheum Dis 1995; 54: 25 – 32.
    • (1995) Ann Rheum Dis , vol.54 , pp. 25-32
    • Hembry, R.M.1    Bagga, M.R.2    Reynolds, J.J.3    Hamblen, D.L.4
  • 67
    • 0029790101 scopus 로고    scopus 로고
    • Expression of matrix metalloproteinase 9 (96-kd gelatinase B) in human rheumatoid arthritis
    • Ahrens D, Koch AE, Pope RM, Stein-Picarella M, Niedbala MJ. Expression of matrix metalloproteinase 9 (96-kd gelatinase B) in human rheumatoid arthritis. Arthritis Rheum 1996; 39: 1576 – 87.
    • (1996) Arthritis Rheum , vol.39 , pp. 1576-1587
    • Ahrens, D.1    Koch, A.E.2    Pope, R.M.3    Stein-Picarella, M.4    Niedbala, M.J.5
  • 68
    • 0008741084 scopus 로고    scopus 로고
    • Matrix metalloproteinases and tissue inhibi-tors of meta-lloproteinases in synovial fluids from patients with rheumatoid arthritis or osteoarthritis
    • Yoshihara Y, Nakamura H, Obata K, Yamada H, Hayakawa T, Fujikawa K, Okada Y. Matrix metalloproteinases and tissue inhibi-tors of meta-lloproteinases in synovial fluids from patients with rheumatoid arthritis or osteoarthritis. Ann Rheum Dis 2000; 59: 455 – 61.
    • (2000) Ann Rheum Dis , vol.59 , pp. 455-461
    • Yoshihara, Y.1    Nakamura, H.2    Obata, K.3    Yamada, H.4    Hayakawa, T.5    Fujikawa, K.6    Okada, Y.7
  • 69
    • 0034076456 scopus 로고    scopus 로고
    • Expression and tissue localization of membrane-types 1, 2 and 3 matrix metalloproteinases in rheumatoid synovium
    • Yamanaka H, Makino K, Takizawa M, Nakamura H, Fujimoto N, Moriya H, Nemori R, et al. Expression and tissue localization of membrane-types 1, 2 and 3 matrix metalloproteinases in rheumatoid synovium. Lab Invest 2000; 80: 677 – 87.
    • (2000) Lab Invest , vol.80 , pp. 677-687
    • Yamanaka, H.1    Makino, K.2    Takizawa, M.3    Nakamura, H.4    Fujimoto, N.5    Moriya, H.6    Nemori, R.7
  • 70
    • 0002801861 scopus 로고
    • Mechanism of mineral solubilization and matrix degradation in osteoclastic bone resorption
    • In: Rifkin BR, Gay CV, editors. Boca Raton, CRC Press
    • Delaisse J, Vaes G. Mechanism of mineral solubilization and matrix degradation in osteoclastic bone resorption. In: Rifkin BR, Gay CV, editors. Biology and physiology of the osteodast. Boca Raton: CRC Press; 1992. pp 289 – 314.
    • (1992) Biology and physiology of the osteodast. , pp. 289-314
    • Delaisse, J.1    Vaes, G.2
  • 71
    • 0028957812 scopus 로고
    • Localization of matrix metalloproteinase 9 (92-kilodalton gelatinase/type IV collagenase - gelatinase B) in osteoclasts: implications for bone resorption
    • Okada Y, Naka K, Kawamura K, Matsumoto T, Nakanishi I, Fujimoto N, et al. Localization of matrix metalloproteinase 9 (92-kilodalton gelatinase/type IV collagenase - gelatinase B) in osteoclasts: implications for bone resorption. Lab Invest 1995; 72: 311 – 22.
    • (1995) Lab Invest , vol.72 , pp. 311-322
    • Okada, Y.1    Naka, K.2    Kawamura, K.3    Matsumoto, T.4    Nakanishi, I.5    Fujimoto, N.6
  • 72
    • 0030059536 scopus 로고    scopus 로고
    • Matrix metalloproteinase 9 (gelatinase B) is expressed in multinucleated giant cells of human giant cell tumor of bone and is associated with vascular invasion
    • Ueda Y, Imai K, Tsuchiya H, Fujimoto N, Nakanishi I, Katsuda S, et al. Matrix metalloproteinase 9 (gelatinase B) is expressed in multinucleated giant cells of human giant cell tumor of bone and is associated with vascular invasion. Am J Pathol 1996; 148: 611 – 22.
    • (1996) Am J Pathol , vol.148 , pp. 611-622
    • Ueda, Y.1    Imai, K.2    Tsuchiya, H.3    Fujimoto, N.4    Nakanishi, I.5    Katsuda, S.6
  • 73
    • 0026736030 scopus 로고
    • Localization of matrix metalloproteinase 3 (stromelysin) in osteoarthritic cartilage and synovium
    • Okada Y, Shinmei M, Tanaka O, Naka K, Kimura A, Nakanishi I, et al. Localization of matrix metalloproteinase 3 (stromelysin) in osteoarthritic cartilage and synovium. Lab Invest 1992; 66: 680 – 90.
    • (1992) Lab Invest , vol.66 , pp. 680-690
    • Okada, Y.1    Shinmei, M.2    Tanaka, O.3    Naka, K.4    Kimura, A.5    Nakanishi, I.6
  • 74
    • 0031883781 scopus 로고    scopus 로고
    • Expression of matrix metalloproteinase 7 (matrilysin) in human osteoarthritic cartilage
    • Ohta S, Imai K, Yamashita K, Matsumoto T, Azumano I, Okada Y. Expression of matrix metalloproteinase 7 (matrilysin) in human osteoarthritic cartilage. Lab Invest 1998; 78: 79 – 87.
    • (1998) Lab Invest , vol.78 , pp. 79-87
    • Ohta, S.1    Imai, K.2    Yamashita, K.3    Matsumoto, T.4    Azumano, I.5    Okada, Y.6
  • 76
    • 0029880393 scopus 로고    scopus 로고
    • The new collagenase, collagenase-3, is expressed and synthesized by human chondrocytes but not by synoviocytes. A role in osteoarthritis
    • Reboul P, Pelletier JP, Tardif G, Cloutier JM, Martel-Pelletier J. The new collagenase, collagenase-3, is expressed and synthesized by human chondrocytes but not by synoviocytes. A role in osteoarthritis. J Clin Invest 1996; 97: 2011 – 9.
    • (1996) J Clin Invest , vol.97 , pp. 2011-2019
    • Reboul, P.1    Pelletier, J.P.2    Tardif, G.3    Cloutier, J.M.4    Martel-Pelletier, J.5
  • 77
    • 0027316964 scopus 로고
    • Expression of 92-kD type IV collagenase/ gelatinase (gelatinase B) in osteoarthritic cartilage and its induction in normal human articular cartilage by interleukin 1
    • Mohtai M, Smith RL, Schurman DJ, Tsuji Y, Torti FM, Hutchinson NI, et al. Expression of 92-kD type IV collagenase/ gelatinase (gelatinase B) in osteoarthritic cartilage and its induction in normal human articular cartilage by interleukin 1. J Clin Invest 1993; 92: 179 – 85.
    • (1993) J Clin Invest , vol.92 , pp. 179-185
    • Mohtai, M.1    Smith, R.L.2    Schurman, D.J.3    Tsuji, Y.4    Torti, F.M.5    Hutchinson, N.I.6
  • 78
    • 0030875073 scopus 로고    scopus 로고
    • Expression of membrane-type 1 matrix metalloproteinase and ac-tivation of progelatinase A in human osteoarthritic cartilage
    • Imai K, Ohta S, Matsumoto T, Fujimoto N, Sato H, Seiki M, et al. Expression of membrane-type 1 matrix metalloproteinase and ac-tivation of progelatinase A in human osteoarthritic cartilage. Am J Pathol 1997; 151: 245 – 56.
    • (1997) Am J Pathol , vol.151 , pp. 245-256
    • Imai, K.1    Ohta, S.2    Matsumoto, T.3    Fujimoto, N.4    Sato, H.5    Seiki, M.6
  • 79
    • 0031566190 scopus 로고    scopus 로고
    • Expression of members of a novel mem-brane linked metalloproteinase family (ADAM) in human articular chondrocytes
    • McKie N, Edwards T, Dallas DJ, Houghton A, Stringer B, Graham R, et al. Expression of members of a novel mem-brane linked metalloproteinase family (ADAM) in human articular chondrocytes. Biochem Biophys Res Commun 1997; 230: 335 – 9.
    • (1997) Biochem Biophys Res Commun , vol.230 , pp. 335-339
    • McKie, N.1    Edwards, T.2    Dallas, D.J.3    Houghton, A.4    Stringer, B.5    Graham, R.6
  • 80
  • 81
    • 0029825963 scopus 로고    scopus 로고
    • Identification and characterization of a novel collagenase in Xenopus laevis: possible roles during frog development
    • Stolow MA, Bauzon DD, Li J, Sedgwick T, Liang VC, Sang QA, Shi YB. Identification and characterization of a novel collagenase in Xenopus laevis: possible roles during frog development. Mol Biol Cell 1996; 7: 1471 – 83.
    • (1996) Mol Biol Cell , vol.7 , pp. 1471-1483
    • Stolow, M.A.1    Bauzon, D.D.2    Li, J.3    Sedgwick, T.4    Liang, V.C.5    Sang, Q.A.6    Shi, Y.B.7
  • 82
    • 0030991956 scopus 로고    scopus 로고
    • A novel metalloproteinase gene (XMIMP) encoding vitronectin-like motifs is transiently ex-pressed in Xenopus laevis early embryo development
    • Yang M, Marray MT, Kurkinen M. A novel metalloproteinase gene (XMIMP) encoding vitronectin-like motifs is transiently ex-pressed in Xenopus laevis early embryo development. J Biol Chem 1997; 272: 13527 – 33.
    • (1997) J Biol Chem , vol.272 , pp. 13527-13533
    • Yang, M.1    Marray, M.T.2    Kurkinen, M.3
  • 83
    • 0032504177 scopus 로고    scopus 로고
    • Cloning and characterization of a novel matrix metalloproteinase (MMP), CMMP, from chicken embryo fibroblasts. CMMP, Xenopus XMIMP, and human MMP-19 have a conserved unique cyosteine in the catalytic domain
    • Yang M, Kurkinen M. Cloning and characterization of a novel matrix metalloproteinase (MMP), CMMP, from chicken embryo fibroblasts. CMMP, Xenopus XMIMP, and human MMP-19 have a conserved unique cyosteine in the catalytic domain. J Biol Chem 1998; 273: 17893 – 900.
    • (1998) J Biol Chem , vol.273 , pp. 17893-17900
    • Yang, M.1    Kurkinen, M.2


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