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Volumn 11, Issue SUPPL. 3, 2006, Pages 3081-3095

The role of collagenolytic matrix metalloproteinases in the loss of articular cartilage in osteoarthritis

Author keywords

Cartilage; Collagenase; Matrix Metalloproteinases; Osteoarthritis; Review

Indexed keywords


EID: 33744496575     PISSN: 27686701     EISSN: 27686698     Source Type: Journal    
DOI: 10.2741/2034     Document Type: Review
Times cited : (68)

References (121)
  • 1
    • 0035660111 scopus 로고    scopus 로고
    • A degeneration-based hypothesis for interpreting fibrillar changes in the osteoarthritic cartilage matrix
    • Broom, N., M. H. Chen & A. Hardy: A degeneration-based hypothesis for interpreting fibrillar changes in the osteoarthritic cartilage matrix. J Anat, 199, 683-98 (2001)
    • (2001) J Anat , vol.199 , pp. 683-698
    • Broom, N.1    Chen, M.H.2    Hardy, A.3
  • 2
    • 5444243560 scopus 로고    scopus 로고
    • Collagens and cartilage matrix homeostasis
    • Eyre, D. R.: Collagens and cartilage matrix homeostasis. Clin Orthop Rel Res, 427, S118-22 (2004)
    • (2004) Clin Orthop Rel Res , vol.427
    • Eyre, D.R.1
  • 3
    • 0024513679 scopus 로고
    • Cartilage collagens. What is their function, and are they involved in articular disease?
    • Mayne, R.: Cartilage collagens. What is their function, and are they involved in articular disease? Arthritis Rheum, 32, 241-6 (1989)
    • (1989) Arthritis Rheum , vol.32 , pp. 241-246
    • Mayne, R.1
  • 4
    • 0024152091 scopus 로고
    • New collagens, new concepts
    • Burgeson, R. E.: New collagens, new concepts. Annu Rev Cell Biol, 4, 551-77 (1988)
    • (1988) Annu Rev Cell Biol , vol.4 , pp. 551-577
    • Burgeson, R.E.1
  • 5
    • 0023655670 scopus 로고
    • Type XI collagen is a heterotrimer with the composition (1 alpha, 2 alpha, 3 alpha) retaining non-triple-helical domains
    • Morris, N. P. & H. P. Bachinger: Type XI collagen is a heterotrimer with the composition (1 alpha, 2 alpha, 3 alpha) retaining non-triple-helical domains. J Biol Chem, 262, 11345-50 (1987)
    • (1987) J Biol Chem , vol.262 , pp. 11345-11350
    • Morris, N.P.1    Bachinger, H.P.2
  • 7
    • 0023864492 scopus 로고
    • Cartilage type IX collagen-proteoglycan contains a large amino-terminal globular domain encoded by multiple exons
    • Vasios, G., I. Nishimura, H. Konomi, M. van der Rest, Y. Ninomiya & B. R. Olsen: Cartilage type IX collagen-proteoglycan contains a large amino-terminal globular domain encoded by multiple exons. J Biol Chem, 263, 2324-9 (1988)
    • (1988) J Biol Chem , vol.263 , pp. 2324-2329
    • Vasios, G.1    Nishimura, I.2    Konomi, H.3    Van Der Rest, M.4    Ninomiya, Y.5    Olsen, B.R.6
  • 8
    • 1842856924 scopus 로고    scopus 로고
    • Recent developments in cartilage research: Matrix biology of the collagen II/IX/XI heterofibril network
    • Eyre, D. R., J. J. Wu, R. J. Fernandes, T. A. Pietka & M. A. Weis: Recent developments in cartilage research: matrix biology of the collagen II/IX/XI heterofibril network. Biochem Soc Trans, 30, 893-9 (2002)
    • (2002) Biochem Soc Trans , vol.30 , pp. 893-899
    • Eyre, D.R.1    Wu, J.J.2    Fernandes, R.J.3    Pietka, T.A.4    Weis, M.A.5
  • 9
    • 1642494706 scopus 로고    scopus 로고
    • Covalent cross-linking of the NC1 domain of collagen type IX to collagen type II in cartilage
    • Eyre, D. R., T. Pietka, M. A. Weis & J.-J. Wu: Covalent cross-linking of the NC1 domain of collagen type IX to collagen type II in cartilage. J Biol Chem, 279, 2568-74 (2004)
    • (2004) J Biol Chem , vol.279 , pp. 2568-2574
    • Eyre, D.R.1    Pietka, T.2    Weis, M.A.3    Wu, J.-J.4
  • 10
    • 0032549578 scopus 로고    scopus 로고
    • Differences between the thermal stabilities of the three triple-helical domains of type IX collagen
    • Miles, C. A., L. Knott, I. G. Sumner & A. J. Bailey: Differences between the thermal stabilities of the three triple-helical domains of type IX collagen. J Mol Biol, 277, 135-44 (1998)
    • (1998) J Mol Biol , vol.277 , pp. 135-144
    • Miles, C.A.1    Knott, L.2    Sumner, I.G.3    Bailey, A.J.4
  • 11
    • 0022837416 scopus 로고
    • Peptide-specific antibodies identify the alpha 2 chain as the proteoglycan subunit of type IX collagen
    • Konomi, H., J. M. Seyer, Y. Ninomiya & B. R. Olsen: Peptide-specific antibodies identify the alpha 2 chain as the proteoglycan subunit of type IX collagen. J Biol Chem, 261, 6742-6 (1986)
    • (1986) J Biol Chem , vol.261 , pp. 6742-6746
    • Konomi, H.1    Seyer, J.M.2    Ninomiya, Y.3    Olsen, B.R.4
  • 12
    • 0031951265 scopus 로고    scopus 로고
    • The cartilage collagens: A review of their structure, organization, and role in the pathogenesis of experimental arthritis in animals and in human rheumatic disease
    • Cremer, M. A., E. F. Rosloniec & A. H. Kang: The cartilage collagens: a review of their structure, organization, and role in the pathogenesis of experimental arthritis in animals and in human rheumatic disease. J Mol Med, 76, 275-88 (1998)
    • (1998) J Mol Med , vol.76 , pp. 275-288
    • Cremer, M.A.1    Rosloniec, E.F.2    Kang, A.H.3
  • 15
    • 0031801895 scopus 로고    scopus 로고
    • Severe disturbance of the distribution and expression of type VI collagen chains in osteoarthritic articular cartilage
    • Hambach, L., D. Neureiter, G. Zeiler, T. Kirchner & T. Aigner: Severe disturbance of the distribution and expression of type VI collagen chains in osteoarthritic articular cartilage. Arthritis Rheum, 41, 986-96 (1998)
    • (1998) Arthritis Rheum , vol.41 , pp. 986-996
    • Hambach, L.1    Neureiter, D.2    Zeiler, G.3    Kirchner, T.4    Aigner, T.5
  • 16
    • 0027240447 scopus 로고
    • Catabolism of intact type VI collagen microfibrils: Susceptibility to degradation by serine proteinases
    • Kielty, C. M., M. Lees, C. A. Shuttleworth & D. Woolley: Catabolism of intact type VI collagen microfibrils: susceptibility to degradation by serine proteinases. Biochem Biophys Res Comm, 191, 1230-6 (1993)
    • (1993) Biochem Biophys Res Comm , vol.191 , pp. 1230-1236
    • Kielty, C.M.1    Lees, M.2    Shuttleworth, C.A.3    Woolley, D.4
  • 17
    • 0037693895 scopus 로고    scopus 로고
    • Matrix metalloproteinases and tissue inhibitors of metalloproteinases: Structure, function, and biochemistry
    • Visse, R. & H. Nagase: Matrix metalloproteinases and tissue inhibitors of metalloproteinases: structure, function, and biochemistry. Circ Res, 92, 827-39 (2003)
    • (2003) Circ Res , vol.92 , pp. 827-839
    • Visse, R.1    Nagase, H.2
  • 19
    • 0036822797 scopus 로고    scopus 로고
    • Relative messenger RNA expression profiling of collagenases and aggrecanases in human articular chondrocytes in vivo and in vitro
    • Bau, B., P. M. Gebhard, J. Haag, T. Knorr, E. Bartnik & T. Aigner: Relative messenger RNA expression profiling of collagenases and aggrecanases in human articular chondrocytes in vivo and in vitro. Arthritis Rheum, 46, 2648-57 (2002)
    • (2002) Arthritis Rheum , vol.46 , pp. 2648-2657
    • Bau, B.1    Gebhard, P.M.2    Haag, J.3    Knorr, T.4    Bartnik, E.5    Aigner, T.6
  • 21
    • 0035799580 scopus 로고    scopus 로고
    • Matrix metalloproteinase-1, - 3, -13 and aggrecanase-1 and -2 are differentially expressed in experimental osteoarthritis
    • Bluteau, G., T. Conrozier, P. Mathieu, E. Vignon, D. Herbage & F. Mallein-Gerin: Matrix metalloproteinase-1, - 3, -13 and aggrecanase-1 and -2 are differentially expressed in experimental osteoarthritis. Biochim Biophys Acta, 1526, 147-58 (2001)
    • (2001) Biochim Biophys Acta , vol.1526 , pp. 147-158
    • Bluteau, G.1    Conrozier, T.2    Mathieu, P.3    Vignon, E.4    Herbage, D.5    Mallein-Gerin, F.6
  • 22
    • 0031025218 scopus 로고    scopus 로고
    • Membrane type 1 matrix metalloproteinase digests interstitial collagens and other extracellular matrix macromolecules
    • Ohuchi, E., K. Imai, Y. Fujii, H. Sato, M. Seiki & Y. Okada: Membrane type 1 matrix metalloproteinase digests interstitial collagens and other extracellular matrix macromolecules. J Biol Chem, 272, 2446-51 (1997)
    • (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
  • 23
    • 0036516460 scopus 로고    scopus 로고
    • Matrix metalloproteinases: A tail of a frog that became a prince
    • Brinckerhoff, C. E. & L. M. Matrisian: Matrix metalloproteinases: a tail of a frog that became a prince. Nat Rev Mol Cell Biol, 3, 207-14 (2002)
    • (2002) Nat Rev Mol Cell Biol , vol.3 , pp. 207-214
    • Brinckerhoff, C.E.1    Matrisian, L.M.2
  • 24
    • 0025611427 scopus 로고
    • Type IV collagenases in tumor invasion and metastasis
    • Stetler-Stevenson, W. G.: Type IV collagenases in tumor invasion and metastasis. Cancer Metastasis Rev, 9, 289-303 (1990)
    • (1990) Cancer Metastasis Rev , vol.9 , pp. 289-303
    • Stetler-Stevenson, W.G.1
  • 27
    • 0028947020 scopus 로고
    • Matrix metalloproteinase-2 is an interstitial collagenase. Inhibitor-free enzyme catalyzes the cleavage of collagen fibrils and soluble native type I collagen generating the specific 3/4-and 1/4-length fragments
    • Aimes, R. T. & J. P. Quigley: Matrix metalloproteinase-2 is an interstitial collagenase. Inhibitor-free enzyme catalyzes the cleavage of collagen fibrils and soluble native type I collagen generating the specific 3/4-and 1/4-length fragments. J Biol Chem, 270, 5872-6 (1995)
    • (1995) J Biol Chem , vol.270 , pp. 5872-5876
    • Aimes, R.T.1    Quigley, J.P.2
  • 28
    • 13044296013 scopus 로고    scopus 로고
    • New collagenolytic enzymes/cascade identified at the pannus-hard tissue junction in rheumatoid arthritis: Destruction from above
    • Konttinen, Y. T., A. Ceponis, M. Takagi, M. Ainola, T. Sorsa, M. Sutinen, T. Salo, J. Ma, S. Santavirta & M. Seiki: New collagenolytic enzymes/cascade identified at the pannus-hard tissue junction in rheumatoid arthritis: destruction from above. Matrix Biol, 17, 585-601 (1998)
    • (1998) Matrix Biol , vol.17 , pp. 585-601
    • Konttinen, Y.T.1    Ceponis, A.2    Takagi, M.3    Ainola, M.4    Sorsa, T.5    Sutinen, M.6    Salo, T.7    Ma, J.8    Santavirta, S.9    Seiki, M.10
  • 29
    • 0033607524 scopus 로고    scopus 로고
    • Membrane type 4 matrix metalloproteinase (MT4-MMP, MMP-17) is a glycosylphosphatidylinositol-anchored proteinase
    • Itoh, Y., M. Kajita, H. Kinoh, H. Mori, A. Okada & M. Seiki: Membrane type 4 matrix metalloproteinase (MT4-MMP, MMP-17) is a glycosylphosphatidylinositol-anchored proteinase. J Biol Chem, 274, 34260-6 (1999)
    • (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
  • 30
    • 0035854654 scopus 로고    scopus 로고
    • Mutation analysis of membrane type-1 matrix metalloproteinase (MT1-MMP). The role of the cytoplasmic tail Cys (574), the active site Glu (240), and furin cleavage motifs in oligomerization, processing, and self-proteolysis of MT1-MMP expressed in breast carcinoma cells
    • Rozanov, D. V., E. I. Deryugina, B. I. Ratnikov, E. Z. Monosov, G. N. Marchenko, J. P. Quigley & A. Y. Strongin: Mutation analysis of membrane type-1 matrix metalloproteinase (MT1-MMP). The role of the cytoplasmic tail Cys (574), the active site Glu (240), and furin cleavage motifs in oligomerization, processing, and self-proteolysis of MT1-MMP expressed in breast carcinoma cells. J Biol Chem, 276, 25705-14 (2001)
    • (2001) J Biol Chem , vol.276 , pp. 25705-25714
    • Rozanov, D.V.1    Deryugina, E.I.2    Ratnikov, B.I.3    Monosov, E.Z.4    Marchenko, G.N.5    Quigley, J.P.6    Strongin, A.Y.7
  • 31
    • 0035030872 scopus 로고    scopus 로고
    • A synthetic triterpenoid selectively inhibits the induction of matrix metalloproteinases 1 and 13 by inflammatory cytokines
    • Mix, K. S., J. A. Mengshol, U. Benbow, M. P. Vincenti, M. B. Sporn & C. E. Brinckerhoff: A synthetic triterpenoid selectively inhibits the induction of matrix metalloproteinases 1 and 13 by inflammatory cytokines. Arthritis Rheum, 44, 1096-104 (2001)
    • (2001) Arthritis Rheum , vol.44 , pp. 1096-1104
    • Mix, K.S.1    Mengshol, J.A.2    Benbow, U.3    Vincenti, M.P.4    Sporn, M.B.5    Brinckerhoff, C.E.6
  • 32
    • 0345643514 scopus 로고    scopus 로고
    • Regulation of matrix metalloproteinase expression in tumor invasion
    • Westermarck, J. & V. M. Kahari: Regulation of matrix metalloproteinase expression in tumor invasion. FASEB J, 13, 781-92 (1999)
    • (1999) FASEB J , vol.13 , pp. 781-792
    • Westermarck, J.1    Kahari, V.M.2
  • 33
    • 0033624445 scopus 로고    scopus 로고
    • Matrix metalloproteinases: Molecular aspects of their roles in tumour invasion and metastasis
    • Curran, S. & G. I. Murray: Matrix metalloproteinases: molecular aspects of their roles in tumour invasion and metastasis. Eur J Cancer, 36, 1621-30 (2000)
    • (2000) Eur J Cancer , vol.36 , pp. 1621-1630
    • Curran, S.1    Murray, G.I.2
  • 34
    • 0029860549 scopus 로고    scopus 로고
    • Inhibition of rabbit collagenase (matrix metalloproteinase-1; MMP-1) transcription by retinoid receptors: Evidence for binding of RARs/RXRs to the -77 AP-1 site through interactions with c-Jun
    • Schroen, D. J. & C. E. Brinckerhoff: Inhibition of rabbit collagenase (matrix metalloproteinase-1; MMP-1) transcription by retinoid receptors: evidence for binding of RARs/RXRs to the -77 AP-1 site through interactions with c-Jun. J Cell Physiol, 169, 320-32 (1996)
    • (1996) J Cell Physiol , vol.169 , pp. 320-332
    • Schroen, D.J.1    Brinckerhoff, C.E.2
  • 35
    • 0027013810 scopus 로고
    • Positive and negative regulation of collagenase gene expression
    • Jonat, C., B. Stein, H. Ponta, P. Herrlich & H. J. Rahmsdorf: Positive and negative regulation of collagenase gene expression. Matrix Suppl, 1, 145-55 (1992)
    • (1992) Matrix Suppl , vol.1 , pp. 145-155
    • Jonat, C.1    Stein, B.2    Ponta, H.3    Herrlich, P.4    Rahmsdorf, H.J.5
  • 36
    • 0034943365 scopus 로고    scopus 로고
    • Transforming growth factor-beta induced collagenase-3 production in human osteoarthritic chondrocytes is triggered by Smad proteins: Cooperation between activator protein-1 and PEA-3 binding sites
    • Tardif, G., P. Reboul, M. Dupuis, C. Geng, N. Duval, J. P. Pelletier & J. Martel-Pelletier: Transforming growth factor-beta induced collagenase-3 production in human osteoarthritic chondrocytes is triggered by Smad proteins: cooperation between activator protein-1 and PEA-3 binding sites. J Rheum, 28, 1631-9 (2001)
    • (2001) J Rheum , vol.28 , pp. 1631-1639
    • Tardif, G.1    Reboul, P.2    Dupuis, M.3    Geng, C.4    Duval, N.5    Pelletier, J.P.6    Martel-Pelletier, J.7
  • 37
    • 0032908329 scopus 로고    scopus 로고
    • Differential patterns of response to doxycycline and transforming growth factor beta1 in the down-regulation of collagenases in osteoarthritic and normal human chondrocytes
    • Shlopov, B. V., G. N. Smith, Jr., A. A. Cole & K. A. Hasty: Differential patterns of response to doxycycline and transforming growth factor beta1 in the down-regulation of collagenases in osteoarthritic and normal human chondrocytes. Arthritis Rheum, 42, 719-27 (1999)
    • (1999) Arthritis Rheum , vol.42 , pp. 719-727
    • Shlopov, B.V.1    Smith Jr., G.N.2    Cole, A.A.3    Hasty, K.A.4
  • 38
    • 3142690433 scopus 로고    scopus 로고
    • Elevation of activated protein C in synovial joints in rheumatoid arthritis and its correlation with matrix metalloproteinase 2
    • Buisson-Legendre, N., S. Smith, L. March & C. Jackson: Elevation of activated protein C in synovial joints in rheumatoid arthritis and its correlation with matrix metalloproteinase 2. Arthritis Rheum, 50, 2151-6 (2004)
    • (2004) Arthritis Rheum , vol.50 , pp. 2151-2156
    • Buisson-Legendre, N.1    Smith, S.2    March, L.3    Jackson, C.4
  • 39
    • 0032981665 scopus 로고    scopus 로고
    • Cyclic mechanical stress induces extracellular matrix degradation in cultured chondrocytes via gene expression of matrix metalloproteinases and interleukin-1
    • Fujisawa, T., T. Hattori, K. Takahashi, T. Kuboki, A. Yamashita & M. Takigawa: Cyclic mechanical stress induces extracellular matrix degradation in cultured chondrocytes via gene expression of matrix metalloproteinases and interleukin-1. J Biochem, 125, 966-75 (1999)
    • (1999) J Biochem , vol.125 , pp. 966-975
    • Fujisawa, T.1    Hattori, T.2    Takahashi, K.3    Kuboki, T.4    Yamashita, A.5    Takigawa, M.6
  • 40
    • 0033798228 scopus 로고    scopus 로고
    • The effects of high magnitude cyclic tensile load on cartilage matrix metabolism in cultured chondrocytes
    • Honda, K., S. Ohno, K. Tanimoto, C. Ijuin, N. Tanaka, T. Doi, Y. Kato & K. Tanne: The effects of high magnitude cyclic tensile load on cartilage matrix metabolism in cultured chondrocytes. Eur J Cell Biol, 79, 601-9 (2000)
    • (2000) Eur J Cell Biol , vol.79 , pp. 601-609
    • Honda, K.1    Ohno, S.2    Tanimoto, K.3    Ijuin, C.4    Tanaka, N.5    Doi, T.6    Kato, Y.7    Tanne, K.8
  • 41
    • 0036252213 scopus 로고    scopus 로고
    • Reduction of cytokine-induced expression and activity of MMP-1 and MMP-13 by mechanical strain in MH7A rheumatoid synovial cells
    • Sun, H. B. & H. Yokota: Reduction of cytokine-induced expression and activity of MMP-1 and MMP-13 by mechanical strain in MH7A rheumatoid synovial cells. Matrix Biol, 21, 263-70 (2002)
    • (2002) Matrix Biol , vol.21 , pp. 263-270
    • Sun, H.B.1    Yokota, H.2
  • 42
    • 0030932125 scopus 로고    scopus 로고
    • The AP-1 site and MMP gene regulation: What is all flie fuss about?
    • Benbow, U. & C. E. Brinckerhoff: The AP-1 site and MMP gene regulation: what is all flie fuss about? Matrix Biol, 15, 519-26 (1997)
    • (1997) Matrix Biol , vol.15 , pp. 519-526
    • Benbow, U.1    Brinckerhoff, C.E.2
  • 43
    • 0035227794 scopus 로고    scopus 로고
    • The matrix metalloproteinase (MMP) and tissue inhibitor of metalloproteinase (TIMP) genes. Transcriptional and posttranscriptional regulation, signal transduction and cell-type-specific expression
    • Vincenti, M. P.: The matrix metalloproteinase (MMP) and tissue inhibitor of metalloproteinase (TIMP) genes. Transcriptional and posttranscriptional regulation, signal transduction and cell-type-specific expression. Meth Molec Biol, 151, 121-48 (2001)
    • (2001) Meth Molec Biol , vol.151 , pp. 121-148
    • Vincenti, M.P.1
  • 44
    • 0033851463 scopus 로고    scopus 로고
    • Interleukin-1 induction of collagenase 3 (matrix metalloproteinase 13) gene expression in chondrocytes requires p38, c-Jun N-terminal kinase, and nuclear factor kappaB: Differential regulation of collagenase 1 and collagenase 3
    • Mengshol, J. A., M. P. Vincenti, C. I. Coon, A. Barchowsky & C. E. Brinckerhoff: Interleukin-1 induction of collagenase 3 (matrix metalloproteinase 13) gene expression in chondrocytes requires p38, c-Jun N-terminal kinase, and nuclear factor kappaB: differential regulation of collagenase 1 and collagenase 3. Arthritis Rheum, 43, 801-11 (2000)
    • (2000) Arthritis Rheum , vol.43 , pp. 801-811
    • Mengshol, J.A.1    Vincenti, M.P.2    Coon, C.I.3    Barchowsky, A.4    Brinckerhoff, C.E.5
  • 45
    • 0036159161 scopus 로고    scopus 로고
    • Matrix metalloproteinases as therapeutic targets in arthritic diseases: Bull's-eye or missing the mark?
    • Mengshol, J. A., K. S. Mix & C. E. Brinckerhoff: Matrix metalloproteinases as therapeutic targets in arthritic diseases: bull's-eye or missing the mark? Arthritis Rheum, 46, 13-20 (2002)
    • (2002) Arthritis Rheum , vol.46 , pp. 13-20
    • Mengshol, J.A.1    Mix, K.S.2    Brinckerhoff, C.E.3
  • 46
    • 0033973613 scopus 로고    scopus 로고
    • Structural analysis and promoter characterization of the human membrane-type matrix metalloproteinase-1 (MT1-MMP) gene
    • Lohi, J., K. Lehti, H. Valtanen, W. C. Parks & J. Keski-Oja: Structural analysis and promoter characterization of the human membrane-type matrix metalloproteinase-1 (MT1-MMP) gene. Gene, 242, 75-86 (2000)
    • (2000) Gene , vol.242 , pp. 75-86
    • Lohi, J.1    Lehti, K.2    Valtanen, H.3    Parks, W.C.4    Keski-Oja, J.5
  • 47
    • 0026079362 scopus 로고
    • Cleavage of type XI collagen fibers by gelatinase and by extracts of osteoarthritic canine cartilage
    • Smith, G. N., Jr., K. A. Hasty, L. P. Yu, Jr., K. S. Lamberson, E. A. Mickler & K. D. Brandt: Cleavage of type XI collagen fibers by gelatinase and by extracts of osteoarthritic canine cartilage. Matrix, 11, 36-42 (1991)
    • (1991) Matrix , vol.11 , pp. 36-42
    • Smith Jr., G.N.1    Hasty, K.A.2    Yu Jr., L.P.3    Lamberson, K.S.4    Mickler, E.A.5    Brandt, K.D.6
  • 48
    • 0036800192 scopus 로고    scopus 로고
    • Metalloproteinase inhibitors: Biological actions and therapeutic opportunities
    • Baker, A. H., D. R. Edwards & G. Murphy: Metalloproteinase inhibitors: biological actions and therapeutic opportunities. J Cell Sci, 115, 3719-27 (2002)
    • (2002) J Cell Sci , vol.115 , pp. 3719-3727
    • Baker, A.H.1    Edwards, D.R.2    Murphy, G.3
  • 50
    • 14144251229 scopus 로고    scopus 로고
    • Expression and localisation of the new metalloproteinase inhibitor RECK (reversion inducing cysteine-rich protein with Kazal motifs) in inflamed synovial membranes of patients with rheumatoid arthritis
    • van Lent, P. L., P. N. Span, A. W. Sloetjes, T. R. Radstake, A. W. van Lieshout, J. J. Heuvel, C. G. Sweep & W. B. van den Berg: Expression and localisation of the new metalloproteinase inhibitor RECK (reversion inducing cysteine-rich protein with Kazal motifs) in inflamed synovial membranes of patients with rheumatoid arthritis. Ann Rheumatic Dis, 64, 368-74 (2005)
    • (2005) Ann Rheumatic Dis , vol.64 , pp. 368-374
    • Van Lent, P.L.1    Span, P.N.2    Sloetjes, A.W.3    Radstake, T.R.4    Van Lieshout, A.W.5    Heuvel, J.J.6    Sweep, C.G.7    Van Den Berg, W.B.8
  • 51
    • 7744235531 scopus 로고    scopus 로고
    • Testican-1, an inhibitor of pro-MMP-2 activation, is expressed in cartilage
    • Hausser, H. J., R. Decking & R. E. Brenner: Testican-1, an inhibitor of pro-MMP-2 activation, is expressed in cartilage. Osteoarthritis Cartilage, 12, 870-7 (2004)
    • (2004) Osteoarthritis Cartilage , vol.12 , pp. 870-877
    • Hausser, H.J.1    Decking, R.2    Brenner, R.E.3
  • 52
    • 0026476388 scopus 로고
    • Characterization of a human seminal plasma glycosaminoglycan-bearing polypeptide
    • Bonnet, F., J. P. Perin, P. Maillet, P. Jolles & P. M. Alliel: Characterization of a human seminal plasma glycosaminoglycan-bearing polypeptide. Biochem J, 288, 565-9 (1992)
    • (1992) Biochem J , vol.288 , pp. 565-569
    • Bonnet, F.1    Perin, J.P.2    Maillet, P.3    Jolles, P.4    Alliel, P.M.5
  • 53
    • 0035893764 scopus 로고    scopus 로고
    • Suppression of membrane-type 1 matrix metalloproteinase (MMP)-mediated MMP-2 activation and tumor invasion by testican 3 and its splicing variant gene product, N-Tes
    • Nakada, M., A. Yamada, T. Takino, H. Miyamori, T. Takahashi, J. Yamashita & H. Sato: Suppression of membrane-type 1 matrix metalloproteinase (MMP)-mediated MMP-2 activation and tumor invasion by testican 3 and its splicing variant gene product, N-Tes. Cancer Res, 61, 8896-902 (2001)
    • (2001) Cancer Res , vol.61 , pp. 8896-8902
    • Nakada, M.1    Yamada, A.2    Takino, T.3    Miyamori, H.4    Takahashi, T.5    Yamashita, J.6    Sato, H.7
  • 54
    • 0025025442 scopus 로고
    • The cysteine switch: A principle of regulation of metalloproteinase activity with potential applicability to the entire matrix metalloproteinase gene family
    • Van Wart, H. E. & H. Birkedal-Hansen: The cysteine switch: a principle of regulation of metalloproteinase activity with potential applicability to the entire matrix metalloproteinase gene family. Proc Natl Acad Sci USA, 87, 5578-82 (1990)
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 5578-5582
    • Van Wart, H.E.1    Birkedal-Hansen, H.2
  • 55
    • 0024337641 scopus 로고
    • Prophylactic treatment of canine osteoarthritis with glycosaminoglycan polysulfuric acid ester
    • Altman, R. D., D. D. Dean, O. E. Muniz & D. S. Howell: Prophylactic treatment of canine osteoarthritis with glycosaminoglycan polysulfuric acid ester. Arthritis Rheum, 32, 759-66 (1989)
    • (1989) Arthritis Rheum , vol.32 , pp. 759-766
    • Altman, R.D.1    Dean, D.D.2    Muniz, O.E.3    Howell, D.S.4
  • 56
    • 0025295127 scopus 로고
    • Secreted proteases. Regulation of their activity and their possible role in metastasis
    • Goldberg, G. I., S. M. Frisch, C. He, S. M. Wilhelm, R. Reich & I. E. Collier: Secreted proteases. Regulation of their activity and their possible role in metastasis. Ann N Y Acad Sci, 580, 375-84 (1990)
    • (1990) Ann N Y Acad Sci , vol.580 , pp. 375-384
    • Goldberg, G.I.1    Frisch, S.M.2    He, C.3    Wilhelm, S.M.4    Reich, R.5    Collier, I.E.6
  • 57
    • 0027015335 scopus 로고
    • Physiological mechanisms for metalloproteinase activation
    • Murphy, G., R. Ward, J. Gavrilovic & S. Atkinson: Physiological mechanisms for metalloproteinase activation. Matrix Suppl, 1, 224-30 (1992)
    • (1992) Matrix Suppl , vol.1 , pp. 224-230
    • Murphy, G.1    Ward, R.2    Gavrilovic, J.3    Atkinson, S.4
  • 58
    • 0030325052 scopus 로고    scopus 로고
    • Molecular regulation of cellular invasion-role of gelatinase A and TIMP-2
    • Yu, A. E., R. E. Hewitt, D. E. Kleiner & W. G. Stetler-Stevenson: Molecular regulation of cellular invasion-role of gelatinase A and TIMP-2. Biochem Cell Biol, 74, 823-31 (1996)
    • (1996) Biochem Cell Biol , vol.74 , pp. 823-831
    • Yu, A.E.1    Hewitt, R.E.2    Kleiner, D.E.3    Stetler-Stevenson, W.G.4
  • 60
    • 0032522576 scopus 로고    scopus 로고
    • Induction of matrix metalloproteinase activation cascades based on membrane-type 1 matrix metalloproteinase: Associated activation of gelatinase A, gelatinase B and collagenase 3
    • Cowell, S., V. Knauper, M. L. Stewart, M. P. D'Ortho, H. Stanton, R. M. Hembry, C. Lopez-Otin, J. J. Reynolds & G. Murphy: Induction of matrix metalloproteinase activation cascades based on membrane-type 1 matrix metalloproteinase: associated activation of gelatinase A, gelatinase B and collagenase 3. Biochem J, 331, 453-8 (1998)
    • (1998) Biochem J , vol.331 , pp. 453-458
    • Cowell, S.1    Knauper, V.2    Stewart, M.L.3    D'Ortho, M.P.4    Stanton, H.5    Hembry, R.M.6    Lopez-Otin, C.7    Reynolds, J.J.8    Murphy, G.9
  • 61
    • 10544246489 scopus 로고    scopus 로고
    • Reactive oxygen species produced by macrophage-derived foam cells regulate the activity of vascular matrix metalloproteinases in vitro. Implications for atherosclerotic plaque stability
    • Rajagopalan, S., X. P. Meng, S. Ramasamy, D. G. Harrison & Z. S. Galis: Reactive oxygen species produced by macrophage-derived foam cells regulate the activity of vascular matrix metalloproteinases in vitro. Implications for atherosclerotic plaque stability. J Clin Invest, 98, 2572-9 (1996)
    • (1996) J Clin Invest , vol.98 , pp. 2572-2579
    • Rajagopalan, S.1    Meng, X.P.2    Ramasamy, S.3    Harrison, D.G.4    Galis, Z.S.5
  • 63
    • 0035464376 scopus 로고    scopus 로고
    • Activation of procollagenases is a key control point in cartilage collagen degradation: Interaction of serine and metalloproteinase pathways
    • Milner, J. M, S. F. Elliott & T. E. Cawston: Activation of procollagenases is a key control point in cartilage collagen degradation: interaction of serine and metalloproteinase pathways. Arthritis Rheum, 44, 2084-96 (2001)
    • (2001) Arthritis Rheum , vol.44 , pp. 2084-2096
    • Milner, J.M.1    Elliott, S.F.2    Cawston, T.E.3
  • 64
    • 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., C. Miyaura, M. Inada, T. Tamura, A. Ito, H. Nagase, K. Kamoi & T. Suda: 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, 139, 1338-45 (1998)
    • (1998) Endocrinology , vol.139 , pp. 1338-1345
    • Kusano, K.1    Miyaura, C.2    Inada, M.3    Tamura, T.4    Ito, A.5    Nagase, H.6    Kamoi, K.7    Suda, T.8
  • 65
    • 0032902109 scopus 로고    scopus 로고
    • Thrombin rapidly and efficiently activates gelatinase A in human microvascular endothelial cells via a mechanism independent of active MT1 matrix metalloproteinase
    • Nguyen, M., J. Arkell & C. J. Jackson: Thrombin rapidly and efficiently activates gelatinase A in human microvascular endothelial cells via a mechanism independent of active MT1 matrix metalloproteinase. Lab Invest, 79, 467-75 (1999)
    • (1999) Lab Invest , vol.79 , pp. 467-475
    • Nguyen, M.1    Arkell, J.2    Jackson, C.J.3
  • 70
    • 0019792987 scopus 로고
    • Production of collagenase and inhibitor (TIMP) by normal, rheumatoid and osteoarthritic synovium in vitro: Effects of hydrocortisone and indomethacin
    • McGuire, M. B., G. Murphy, J. J. Reynolds & R. G. Russell: Production of collagenase and inhibitor (TIMP) by normal, rheumatoid and osteoarthritic synovium in vitro: effects of hydrocortisone and indomethacin. Clin Sci, 61, 703-10 (1981)
    • (1981) Clin Sci , vol.61 , pp. 703-710
    • McGuire, M.B.1    Murphy, G.2    Reynolds, J.J.3    Russell, R.G.4
  • 71
    • 0028069617 scopus 로고
    • Characteristics of 92 kDa type IV collagenase/gelatinase produced by granulocytic leukemia cells: Structure, expression of cDNA in E. coli and enzymic properties
    • Pourmotabbed, T., T. L. Solomon, K. A. Hasty & C. L. Mainardi: Characteristics of 92 kDa type IV collagenase/gelatinase produced by granulocytic leukemia cells: structure, expression of cDNA in E. coli and enzymic properties. Biochim Biophysic Acta, 1204, 97-107 (1994)
    • (1994) Biochim Biophysic Acta , vol.1204 , pp. 97-107
    • Pourmotabbed, T.1    Solomon, T.L.2    Hasty, K.A.3    Mainardi, C.L.4
  • 72
    • 0021732056 scopus 로고
    • Purification of a type V collagen degrading metalloproteinase from rabbit alveolar macrophages
    • Mainardi, C. L., M. S. Hibbs, K. A. Hasty & J. M. Seyer: Purification of a type V collagen degrading metalloproteinase from rabbit alveolar macrophages. Coll Rel Res, 4, 479-92 (1984)
    • (1984) Coll Rel Res , vol.4 , pp. 479-492
    • Mainardi, C.L.1    Hibbs, M.S.2    Hasty, K.A.3    Seyer, J.M.4
  • 73
    • 0025606526 scopus 로고
    • Type XI collagen-degrading activity in human osteoarthritic cartilage
    • Yu, L. P., Jr., G. N. Smith, Jr., K. D. Brandt & W. Capello: Type XI collagen-degrading activity in human osteoarthritic cartilage. Arthritis Rheum, 33, 1626-33 (1990)
    • (1990) Arthritis Rheum , vol.33 , pp. 1626-1633
    • Yu Jr., L.P.1    Smith Jr., G.N.2    Brandt, K.D.3    Capello, W.4
  • 74
    • 0024561514 scopus 로고
    • Degradation of type IX collagen by matrix metalloproteinase 3 (stromelysin) from human rheumatoid synovial cells
    • Okada, Y., H. Konomi, T. Yada, K. Kimata & H. Nagase: Degradation of type IX collagen by matrix metalloproteinase 3 (stromelysin) from human rheumatoid synovial cells. FEBS Letters, 244, 473-6 (1989)
    • (1989) FEBS Letters , vol.244 , pp. 473-476
    • Okada, Y.1    Konomi, H.2    Yada, T.3    Kimata, K.4    Nagase, H.5
  • 75
    • 0031937738 scopus 로고    scopus 로고
    • Collagen IX: Evidence for a structural association between NC4 domains in cartilage and a novel cleavage site in the alpha 1 (IX) chain
    • Douglas, S. P., J. M. Jenkins & K. E. Kadler: Collagen IX: evidence for a structural association between NC4 domains in cartilage and a novel cleavage site in the alpha 1 (IX) chain. Matrix Biol, 16, 497-505 (1998)
    • (1998) Matrix Biol , vol.16 , pp. 497-505
    • Douglas, S.P.1    Jenkins, J.M.2    Kadler, K.E.3
  • 77
    • 0018222563 scopus 로고
    • Correlation between articular cartilage collagenase activity and osteoarthritis
    • Ehrlich, M. G., P. A. Houle, G. Vigliani & H. J. Mankin: Correlation between articular cartilage collagenase activity and osteoarthritis. Arthritis Rheum, 21, 761-6 (1978)
    • (1978) Arthritis Rheum , vol.21 , pp. 761-766
    • Ehrlich, M.G.1    Houle, P.A.2    Vigliani, G.3    Mankin, H.J.4
  • 78
    • 0023882210 scopus 로고
    • In vitro effects of tiaprofenic acid, sodium salicylate and hydrocortisone on human osteoarthritic cartilage degradation and synovial collagenase synthesis
    • Pelletier, J. P. & J. Martel-Pelletier: In vitro effects of tiaprofenic acid, sodium salicylate and hydrocortisone on human osteoarthritic cartilage degradation and synovial collagenase synthesis. Drugs, 35 Suppl 1, 42-5 (1988)
    • (1988) Drugs , vol.35 , Issue.SUPPL. 1 , pp. 42-45
    • Pelletier, J.P.1    Martel-Pelletier, J.2
  • 79
    • 0027443334 scopus 로고
    • Effects of nimesulide and naproxen on the degradation and metalloprotease synthesis of human osteoarthritic cartilage
    • Pelletier, J. P. & J. Martel-Pelletier: Effects of nimesulide and naproxen on the degradation and metalloprotease synthesis of human osteoarthritic cartilage. Drugs, 46 Suppl 1, 34-9 (1993)
    • (1993) Drugs , vol.46 , Issue.SUPPL. 1 , pp. 34-39
    • Pelletier, J.P.1    Martel-Pelletier, J.2
  • 80
    • 0028322352 scopus 로고
    • Molecular cloning and expression of collagenase-3, a novel human matrix metalloproteinase produced by breast carcinomas
    • Freije, J. M., I. Diez-Itza, M. Balbin, L. M. Sanchez, R. Blasco, J. Tolivia & C. Lopez-Otin: Molecular cloning and expression of collagenase-3, a novel human matrix metalloproteinase produced by breast carcinomas. J Biol Chem, 269, 16766-73 (1994)
    • (1994) J Biol Chem , vol.269 , pp. 16766-16773
    • Freije, J.M.1    Diez-Itza, I.2    Balbin, M.3    Sanchez, L.M.4    Blasco, R.5    Tolivia, J.6    Lopez-Otin, C.7
  • 81
    • 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., J. P. Pelletier, G. Tardif, J. M. Cloutier & J. Martel-Pelletier: The new collagenase, collagenase-3, is expressed and synthesized by human chondrocytes but not by synoviocytes. A role in osteoarthritis. J Clin Invest, 97, 2011-9 (1996)
    • (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
  • 83
    • 0026804664 scopus 로고
    • Reduction of the severity of canine osteoarthritis by prophylactic treatment with oral doxycycline
    • see comment
    • Yu, L. P., Jr., G. N. Smith, Jr., K. D. Brandt, S. L. Myers, B. L. O'Connor & D. A. Brandt: Reduction of the severity of canine osteoarthritis by prophylactic treatment with oral doxycycline. [see comment]. Arthritis Rheum, 35, 1150-9 (1992)
    • (1992) Arthritis Rheum , vol.35 , pp. 1150-1159
    • Yu Jr., L.P.1    Smith Jr., G.N.2    Brandt, K.D.3    Myers, S.L.4    O'Connor, B.L.5    Brandt, D.A.6
  • 86
    • 0026708439 scopus 로고
    • Preferential mRNA expression of prostromelysin relative to procollagenase and in situ localization in human articular cartilage
    • Nguyen, Q., J. S. Mort & P. J. Roughley: Preferential mRNA expression of prostromelysin relative to procollagenase and in situ localization in human articular cartilage. J Clin Invest, 89, 1189-97 (1992)
    • (1992) J Clin Invest , vol.89 , pp. 1189-1197
    • Nguyen, Q.1    Mort, J.S.2    Roughley, P.J.3
  • 87
    • 0024470051 scopus 로고
    • Chondrocyte activation by interleukin-1:6 analysis of the synergistic properties of fibroblast growth factor and phorbol myristate acetate
    • Bandara, G., C. W. Lin, H. I. Georgescu, D. Mendelow & C. H. Evans: Chondrocyte activation by interleukin-1:6 analysis of the synergistic properties of fibroblast growth factor and phorbol myristate acetate. Arch Biochem Biophys, 274, 539-47 (1989)
    • (1989) Arch Biochem Biophys , vol.274 , pp. 539-547
    • Bandara, G.1    Lin, C.W.2    Georgescu, H.I.3    Mendelow, D.4    Evans, C.H.5
  • 89
    • 0030033710 scopus 로고    scopus 로고
    • Chondrocyte matrix metalloproteinase-8: Up-regulation of neutrophil collagenase by interleukin-1 beta in human cartilage from knee and ankle joints
    • Chubinskaya, S., K. Huch, K. Mikecz, G. Cs-Szabo, K. A. Hasty, K. E. Kuettner & A. A. Cole: Chondrocyte matrix metalloproteinase-8: up-regulation of neutrophil collagenase by interleukin-1 beta in human cartilage from knee and ankle joints. Lab Invest, 74, 232-40 (1996)
    • (1996) Lab Invest , vol.74 , pp. 232-240
    • Chubinskaya, S.1    Huch, K.2    Mikecz, K.3    Cs-Szabo, G.4    Hasty, K.A.5    Kuettner, K.E.6    Cole, A.A.7
  • 90
    • 0030875073 scopus 로고    scopus 로고
    • Expression of membrane-type 1 matrix metalloproteinase and activation of progelatinase a in human osteoarthritic cartilage
    • Imai, K., S. Ohta, T. Matsumoto, N. Fujimoto, H. Sato, M. Seiki & Y. Okada: Expression of membrane-type 1 matrix metalloproteinase and activation of progelatinase A in human osteoarthritic cartilage. Am J Pathol, 151, 245-56 (1997)
    • (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    Okada, Y.7
  • 94
    • 18244427699 scopus 로고    scopus 로고
    • Selective enhancement of collagenase-mediated cleavage of resident type II collagen in cultured osteoarthritic cartilage and arrest with a synthetic inhibitor that spares collagenase 1 (matrix metalloproteinase 1)
    • Dahlberg, L., R. C. Billinghurst, P. Manner, F. Nelson, G. Webb, M. Ionescu, A. Reiner, M. Tanzer, D. Zukor, J. Chen, H. E. van Wart & A. R. Poole: Selective enhancement of collagenase-mediated cleavage of resident type II collagen in cultured osteoarthritic cartilage and arrest with a synthetic inhibitor that spares collagenase 1 (matrix metalloproteinase 1). Arthritis Rheum, 43, 673-82 (2000)
    • (2000) Arthritis Rheum , vol.43 , pp. 673-682
    • Dahlberg, L.1    Billinghurst, R.C.2    Manner, P.3    Nelson, F.4    Webb, G.5    Ionescu, M.6    Reiner, A.7    Tanzer, M.8    Zukor, D.9    Chen, J.10    Van Wart, H.E.11    Poole, A.R.12
  • 95
    • 0028839263 scopus 로고
    • Damage to type II collagen in aging and osteoarthritis starts at the articular surface, originates around chondrocytes, and extends into the cartilage with progressive degeneration
    • Hollander, A. P., I. Pidoux, A. Reiner, C. Rorabeck, R. Bourne & A. R. Poole: Damage to type II collagen in aging and osteoarthritis starts at the articular surface, originates around chondrocytes, and extends into the cartilage with progressive degeneration. J Clin Invest, 96, 2859-69 (1995)
    • (1995) J Clin Invest , vol.96 , pp. 2859-2869
    • Hollander, A.P.1    Pidoux, I.2    Reiner, A.3    Rorabeck, C.4    Bourne, R.5    Poole, A.R.6
  • 97
    • 0028328915 scopus 로고
    • Increased damage to type II collagen in osteoarthritic articular cartilage detected by a new immunoassay
    • Hollander, A. P., T. F. Heathfield, C. Webber, Y. Iwata, R. Bourne, C. Rorabeck & A. R. Poole: Increased damage to type II collagen in osteoarthritic articular cartilage detected by a new immunoassay. J Clin Invest, 93, 1722-32 (1994)
    • (1994) J Clin Invest , vol.93 , pp. 1722-1732
    • Hollander, A.P.1    Heathfield, T.F.2    Webber, C.3    Iwata, Y.4    Bourne, R.5    Rorabeck, C.6    Poole, A.R.7
  • 98
    • 0031958104 scopus 로고    scopus 로고
    • Collagenase 1 and collagenase 3 expression in a guinea pig model of osteoarthritis
    • see comment
    • Huebner, J. L., I. G. Otterness, E. M. Freund, B. Caterson & V. B. Kraus: Collagenase 1 and collagenase 3 expression in a guinea pig model of osteoarthritis. [see comment]. Arthritis Rheum, 41, 877-90 (1998)
    • (1998) Arthritis Rheum , vol.41 , pp. 877-890
    • Huebner, J.L.1    Otterness, I.G.2    Freund, E.M.3    Caterson, B.4    Kraus, V.B.5
  • 99
    • 0036671512 scopus 로고    scopus 로고
    • Elevation of a collagenase generated type II collagen neoepitope and proteoglycan epitopes in synovial fluid following induction of joint instability in the dog
    • Chu, Q., M. Lopez, K. Hayashi, M. Ionescu, R. C. Billinghurst, K. A. Johnson, A. R. Poole & M. D. Markel: Elevation of a collagenase generated type II collagen neoepitope and proteoglycan epitopes in synovial fluid following induction of joint instability in the dog. Osteoarthritis Cartilage, 10, 662-9 (2002)
    • (2002) Osteoarthritis Cartilage , vol.10 , pp. 662-669
    • Chu, Q.1    Lopez, M.2    Hayashi, K.3    Ionescu, M.4    Billinghurst, R.C.5    Johnson, K.A.6    Poole, A.R.7    Markel, M.D.8
  • 100
    • 0033001430 scopus 로고    scopus 로고
    • In situ zymographic localisation of type II collagen degrading activity in osteoarthritic human articular cartilage
    • Freemont, A. J., R. J. Byers, Y. O. Taiwo & J. A. Hoyland: In situ zymographic localisation of type II collagen degrading activity in osteoarthritic human articular cartilage. Ann Rheum Dis, 58, 357-65 (1999)
    • (1999) Ann Rheum Dis , vol.58 , pp. 357-365
    • Freemont, A.J.1    Byers, R.J.2    Taiwo, Y.O.3    Hoyland, J.A.4
  • 102
    • 0346658320 scopus 로고    scopus 로고
    • Gene deletion of either interleukin-1beta, interleukin-1 beta-converting enzyme, inducible nitric oxide synthase, or stromelysin 1 accelerates the development of knee osteoarthritis in mice after surgical transection of the medial collateral ligament and partial medial meniscectomy
    • see comment
    • Clements, K. M., J. S. Price, M. G. Chambers, D. M. Visco, A. R. Poole & R. M. Mason: Gene deletion of either interleukin-1beta, interleukin-1 beta-converting enzyme, inducible nitric oxide synthase, or stromelysin 1 accelerates the development of knee osteoarthritis in mice after surgical transection of the medial collateral ligament and partial medial meniscectomy. [see comment]. Arthritis Rheum, 48, 3452-63 (2003)
    • (2003) Arthritis Rheum , vol.48 , pp. 3452-3463
    • Clements, K.M.1    Price, J.S.2    Chambers, M.G.3    Visco, D.M.4    Poole, A.R.5    Mason, R.M.6
  • 103
    • 0030839472 scopus 로고    scopus 로고
    • Matrix metalloproteinase inhibition as a novel anticancer strategy: A review with special focus on batimastat and marimastat
    • Rasmussen, H. S. & P. P. McCann: Matrix metalloproteinase inhibition as a novel anticancer strategy: a review with special focus on batimastat and marimastat. Pharmacol Ther, 75, 69-75 (1997)
    • (1997) Pharmacol Ther , vol.75 , pp. 69-75
    • Rasmussen, H.S.1    McCann, P.P.2
  • 105
    • 0031654554 scopus 로고    scopus 로고
    • Ro 32-3555, an orally active collagenase selective inhibitor, prevents structural damage in the STR/ORT mouse model of osteoarthritis
    • Brewster, M., E. J. Lewis, K. L. Wilson, A. K. Greenham & K. M. Bottomley: Ro 32-3555, an orally active collagenase selective inhibitor, prevents structural damage in the STR/ORT mouse model of osteoarthritis. Arthritis Rheum, 41, 1639-44 (1998)
    • (1998) Arthritis Rheum , vol.41 , pp. 1639-1644
    • Brewster, M.1    Lewis, E.J.2    Wilson, K.L.3    Greenham, A.K.4    Bottomley, K.M.5
  • 106
    • 0036793151 scopus 로고    scopus 로고
    • Induction of osteoarthritis in the rat by surgical tear of the meniscus: Inhibition of joint damage by a matrix metalloproteinase inhibitor
    • erratum appears in Osteoarthritis Cartilage 2002 Nov; 10 (1):905
    • Janusz, M. J., A. M. Bendele, K. K. Brown, Y. O. Taiwo, L. Hsieh & S. A. Heitmeyer: Induction of osteoarthritis in the rat by surgical tear of the meniscus: Inhibition of joint damage by a matrix metalloproteinase inhibitor. [erratum appears in Osteoarthritis Cartilage 2002 Nov; 10 (1):905]. Osteoarthritis Cartilage, 10, 785-91 (2002)
    • (2002) Osteoarthritis Cartilage , vol.10 , pp. 785-791
    • Janusz, M.J.1    Bendele, A.M.2    Brown, K.K.3    Taiwo, Y.O.4    Hsieh, L.5    Heitmeyer, S.A.6
  • 107
    • 0034770450 scopus 로고    scopus 로고
    • Matrix metalloproteinase inhibitors in rheumatic diseases
    • Close, D. R.: Matrix metalloproteinase inhibitors in rheumatic diseases. Ann Rheum Dis, 60 Suppl 3, iii62-7 (2001)
    • (2001) Ann Rheum Dis , vol.60 , Issue.SUPPL. 3
    • Close, D.R.1
  • 109
    • 0027556626 scopus 로고
    • In vivo effects of naproxen on composition, proteoglycan metabolism, and matrix metalloproteinase activities in canine articular cartilage
    • Ratcliffe, A., W. Azzo, F. Saed-Nejad, N. Lane, M. P. Rosenwasser & V. C. Mow: In vivo effects of naproxen on composition, proteoglycan metabolism, and matrix metalloproteinase activities in canine articular cartilage. J Orthop Res, 11, 163-71 (1993)
    • (1993) J Orthop Res , vol.11 , pp. 163-171
    • Ratcliffe, A.1    Azzo, W.2    Saed-Nejad, F.3    Lane, N.4    Rosenwasser, M.P.5    Mow, V.C.6
  • 110
    • 0031058583 scopus 로고    scopus 로고
    • Effects of tenidap on the progression of osteoarthritic lesions in a canine experimental model. Suppression of metalloprotease and interleukin-1 activity
    • Fernandes, J. C., J. P. Caron, J. Martel-Pelletier, D. Jovanovic, F. Mineau, G. Tardif, I. G. Otterness & J. P. Pelletier: Effects of tenidap on the progression of osteoarthritic lesions in a canine experimental model. Suppression of metalloprotease and interleukin-1 activity. Arthritis Rheum, 40, 284-94 (1997)
    • (1997) Arthritis Rheum , vol.40 , pp. 284-294
    • Fernandes, J.C.1    Caron, J.P.2    Martel-Pelletier, J.3    Jovanovic, D.4    Mineau, F.5    Tardif, G.6    Otterness, I.G.7    Pelletier, J.P.8
  • 111
    • 0027167892 scopus 로고
    • Reduced expression of glucocorticoid receptor levels in human osteoarthritic chondrocytes. Role in the suppression of metalloprotease synthesis
    • DiBattista, J. A., J. Martel-Pelletier, T. Antakly, G. Tardif, J. M. Cloutier & J. P. Pelletier: Reduced expression of glucocorticoid receptor levels in human osteoarthritic chondrocytes. Role in the suppression of metalloprotease synthesis. J Clin Endocrinol Metab, 76, 1128-34 (1993)
    • (1993) J Clin Endocrinol Metab , vol.76 , pp. 1128-1134
    • DiBattista, J.A.1    Martel-Pelletier, J.2    Antakly, T.3    Tardif, G.4    Cloutier, J.M.5    Pelletier, J.P.6
  • 112
    • 0025727968 scopus 로고
    • Cytokines, prostaglandin E2, phospholipase A and metalloproteases in synovial fluid in osteoarthritis
    • Balblanc, J. C., E. Vignon, P. Mathieu, P. Broquet, T. Conrozier & M. Richard: [Cytokines, prostaglandin E2, phospholipase A and metalloproteases in synovial fluid in osteoarthritis]. Rev Rhum Mal Osteoartic, 58, 343-7 (1991)
    • (1991) Rev Rhum Mal Osteoartic , vol.58 , pp. 343-347
    • Balblanc, J.C.1    Vignon, E.2    Mathieu, P.3    Broquet, P.4    Conrozier, T.5    Richard, M.6
  • 113
    • 0025364083 scopus 로고
    • Cartilage degradative enzymes in human osteoarthritis: Effect of a nonsteroidal antiinflammatory drug administered orally
    • Vignon, E., P. Mathieu, P. Broquet, P. Louisot & M. Richard: Cartilage degradative enzymes in human osteoarthritis: effect of a nonsteroidal antiinflammatory drug administered orally. Seminars in Arthritis Rheum, 19, 26-9 (1990)
    • (1990) Seminars in Arthritis Rheum , vol.19 , pp. 26-29
    • Vignon, E.1    Mathieu, P.2    Broquet, P.3    Louisot, P.4    Richard, M.5
  • 114
    • 1542286076 scopus 로고    scopus 로고
    • The inhibition of subchondral bone resorption in the early phase of experimental dog osteoarthritis by licofelone is associated with a reduction in the synthesis of MMP-13 and cathepsin K
    • Pelletier, J. P., C. Boileau, J. Brunet, M. Boily, D. Lajeunesse, P. Reboul, S. Laufer & J. Martel-Pelletier: The inhibition of subchondral bone resorption in the early phase of experimental dog osteoarthritis by licofelone is associated with a reduction in the synthesis of MMP-13 and cathepsin K. Bone, 34, 527-38 (2004)
    • (2004) Bone , vol.34 , pp. 527-538
    • Pelletier, J.P.1    Boileau, C.2    Brunet, J.3    Boily, M.4    Lajeunesse, D.5    Reboul, P.6    Laufer, S.7    Martel-Pelletier, J.8
  • 115
    • 0030426902 scopus 로고    scopus 로고
    • Pharmacological profile of SB 203580, a selective inhibitor of cytokine suppressive binding protein/p38 kinase, in animal models of arthritis, bone resorption, endotoxin shock and immune function
    • Badger, A. M., J. N. Bradbeer, B. Votta, J. C. Lee, J. L. Adams & D. E. Griswold: Pharmacological profile of SB 203580, a selective inhibitor of cytokine suppressive binding protein/p38 kinase, in animal models of arthritis, bone resorption, endotoxin shock and immune function. J Pharmacol Exp Ther, 279, 1453-61 (1996)
    • (1996) J Pharmacol Exp Ther , vol.279 , pp. 1453-1461
    • Badger, A.M.1    Bradbeer, J.N.2    Votta, B.3    Lee, J.C.4    Adams, J.L.5    Griswold, D.E.6
  • 116
    • 0033405584 scopus 로고    scopus 로고
    • Selective inhibition of inducible nitric oxide synthase in experimental osteoarthritis is associated with reduction in tissue levels of catabolic factors
    • Pelletier, J. P., V. Lascau-Coman, D. Jovanovic, J. C. Fernandes, P. Manning, J. R. Connor, M. G. Currie & J. Martel- Pelletier: Selective inhibition of inducible nitric oxide synthase in experimental osteoarthritis is associated with reduction in tissue levels of catabolic factors. J Rheum, 26, 2002-14 (1999)
    • (1999) J Rheum , vol.26 , pp. 2002-2014
    • Pelletier, J.P.1    Lascau-Coman, V.2    Jovanovic, D.3    Fernandes, J.C.4    Manning, P.5    Connor, J.R.6    Currie, M.G.7    Martel-Pelletier, J.8
  • 118
    • 0033917674 scopus 로고    scopus 로고
    • Distinct roles for the NF-kappaB1 (p50) and c-Rel transcription factors in inflammatory arthritis
    • Campbell, I. K., S. Gerondakis, K. O'Donnell & I. P. Wicks: Distinct roles for the NF-kappaB1 (p50) and c-Rel transcription factors in inflammatory arthritis. J Clin Invest, 105, 1799-806 (2000)
    • (2000) J Clin Invest , vol.105 , pp. 1799-1806
    • Campbell, I.K.1    Gerondakis, S.2    O'Donnell, K.3    Wicks, I.P.4
  • 119
    • 2642649541 scopus 로고    scopus 로고
    • Oral administration of doxycycline reduces collagenase and gelatinase activities in extracts of human osteoarthritic cartilage
    • Smith, G. N., Jr., L. P. Yu, Jr., K. D. Brandt & W. N. Capello: Oral administration of doxycycline reduces collagenase and gelatinase activities in extracts of human osteoarthritic cartilage. J Rheum, 25, 532-5 (1998)
    • (1998) J Rheum , vol.25 , pp. 532-535
    • Smith Jr., G.N.1    Yu Jr., L.P.2    Brandt, K.D.3    Capello, W.N.4
  • 121
    • 0038639763 scopus 로고    scopus 로고
    • Aggrecanases and cartilage matrix degradation
    • Nagase, H. & M. Kashiwagi: Aggrecanases and cartilage matrix degradation. Arthritis Res Ther, 5, 94-103 (2003)
    • (2003) Arthritis Res Ther , vol.5 , pp. 94-103
    • Nagase, H.1    Kashiwagi, M.2


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