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Volumn 5, Issue 2, 2003, Pages 94-103

Aggrecanases and cartilage matrix degradation

Author keywords

ADAMTS; Chondrocytes; Matrix metalloproteinases; Osteoarthritis

Indexed keywords

AGGRECAN; AGGRECANASE; ALANINE; CYCLOSPORIN A; GLUTAMIC ACID; HYDROXAMIC ACID DERIVATIVE; MATRIX METALLOPROTEINASE; MATRIX METALLOPROTEINASE INHIBITOR; OMEGA 3 FATTY ACID;

EID: 0038639763     PISSN: 14786354     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Review
Times cited : (355)

References (108)
  • 1
    • 24244435230 scopus 로고    scopus 로고
    • Matrix glycoprotein, proteoglycans, and cartilage
    • Edited by S. Ruddy, Harris ED Jr, Sledge CB. Philadelphia: WB Saunders Company
    • Hinegård D, Lorenzo P, Sanxe T: Matrix glycoprotein, proteoglycans, and cartilage. In Kelly's Textbook of Rheumatology. Edited by S. Ruddy, Harris ED Jr, Sledge CB. Philadelphia: WB Saunders Company; 2001:41-53.
    • (2001) Kelly's Textbook of Rheumatology , pp. 41-53
    • Hinegård, D.1    Lorenzo, P.2    Sanxe, T.3
  • 2
    • 0001841578 scopus 로고
    • Role of physical and medical aspects in degradating the matrix
    • Edited by Woessner JF Jr, Howell DS. New York: Marcel Dekker
    • Evans CH, Brown TD: Role of physical and medical aspects in degradating the matrix. In Joint Cartilage Degradation: Basic and Clinical Aspects. Edited by Woessner JF Jr, Howell DS. New York: Marcel Dekker; 1993:187-208.
    • (1993) Joint Cartilage Degradation: Basic and Clinical Aspects , pp. 187-208
    • Evans, C.H.1    Brown, T.D.2
  • 3
    • 0022642817 scopus 로고
    • Oxygen radicals as effectors of cartilage destruction. Direct degradative effect on matrix components and indirect action via activation of latent collagenase from polymorphonuclear leukocytes
    • Burkhardt H, Schwingel M, Menninger H, Macartney HW, Tschesche H: Oxygen radicals as effectors of cartilage destruction. Direct degradative effect on matrix components and indirect action via activation of latent collagenase from polymorphonuclear leukocytes. Arthritis Rheum 1986, 29:379-387.
    • (1986) Arthritis Rheum. , vol.29 , pp. 379-387
    • Burkhardt, H.1    Schwingel, M.2    Menninger, H.3    Macartney, H.W.4    Tschesche, H.5
  • 4
    • 0001889762 scopus 로고    scopus 로고
    • Proteinase and matrix degradation
    • Edited by Ruddy S, Harris ED Jr, Sledge CB. Philadelphia: WB Saunders Company
    • Okada Y: Proteinase and matrix degradation. In Kelly's Textbook of Rheumatology. Edited by Ruddy S, Harris ED Jr, Sledge CB. Philadelphia: WB Saunders Company; 2001:55-72.
    • (2001) Kelly's Textbook of Rheumatology , pp. 55-72
    • Okada, Y.1
  • 5
    • 0035076487 scopus 로고    scopus 로고
    • Matrix metalloproteinase and proinflammatory cytokine production by chondrocytes of human osteoarthritic cartilage: Associations with degenerative changes
    • Tetlow LC, Adlam DJ, Woolley DE: Matrix metalloproteinase and proinflammatory cytokine production by chondrocytes of human osteoarthritic cartilage: associations with degenerative changes. Arthritis Rheum 2001, 44:585-594.
    • (2001) Arthritis Rheum. , vol.44 , pp. 585-594
    • Tetlow, L.C.1    Adlam, D.J.2    Woolley, D.E.3
  • 8
    • 0035174308 scopus 로고    scopus 로고
    • Articular cartilage and changes in arthritis: Matrix degradation
    • Mort JS, Billington CJ: Articular cartilage and changes in arthritis: matrix degradation. Arthritis Res 2001, 3:337-341.
    • (2001) Arthritis Res. , vol.3 , pp. 337-341
    • Mort, J.S.1    Billington, C.J.2
  • 9
    • 0035056067 scopus 로고    scopus 로고
    • Aggrecanase in cartilage matrix breakdown
    • Nagase H: Aggrecanase in cartilage matrix breakdown. Connective Tissue 2001, 33:27-32.
    • (2001) Connective Tissue , vol.33 , pp. 27-32
    • Nagase, H.1
  • 10
    • 0036605643 scopus 로고    scopus 로고
    • Aggrecanase-mediated cartilage degradation
    • Arner EC: Aggrecanase-mediated cartilage degradation. Curr Opin Pharmacol 2002, 2:322-329.
    • (2002) Curr. Opin. Pharmacol. , vol.2 , pp. 322-329
    • Arner, E.C.1
  • 13
    • 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, 267:19470-19474.
    • (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
  • 14
    • 0026504563 scopus 로고
    • Identification of a stromelysin cleavage site within the interglobular domain of human aggrecan. Evidence for proteolysis at this site in vivo in human articular cartilage
    • Flannery CR, Lark MW, Sandy JD: Identification of a stromelysin cleavage site within the interglobular domain of human aggrecan. Evidence for proteolysis at this site in vivo in human articular cartilage. J Biol Chem 1992, 267:1008-1014.
    • (1992) J. Biol. Chem. , vol.267 , pp. 1008-1014
    • Flannery, C.R.1    Lark, M.W.2    Sandy, J.D.3
  • 15
    • 0025776382 scopus 로고
    • Catabolism of aggrecan in cartilage explants. Identification of a major cleavage site within the interglobular domain
    • Sandy JD, Neame PJ, Boynton RE, Flannery CR: Catabolism of aggrecan in cartilage explants. Identification of a major cleavage site within the interglobular domain. J Biol Chem 1991, 266:8683-8685.
    • (1991) J. Biol. Chem. , vol.266 , pp. 8683-8685
    • Sandy, J.D.1    Neame, P.J.2    Boynton, R.E.3    Flannery, C.R.4
  • 17
    • 0026771893 scopus 로고
    • N-terminal sequence of proteoglycan fragments isolated from medium of interleukin-1-treated articular-cartilage cultures. Putative site(s) of enzymic cleavage
    • Loulakis P, Shrikhande A, Davis G, Maniglia CA: N-terminal sequence of proteoglycan fragments isolated from medium of interleukin-1-treated articular-cartilage cultures. Putative site(s) of enzymic cleavage. Biochem J 1992, 284:589-593.
    • (1992) Biochem. J. , vol.284 , pp. 589-593
    • Loulakis, P.1    Shrikhande, A.2    Davis, G.3    Maniglia, C.A.4
  • 18
    • 0026682509 scopus 로고
    • The structure of aggrecan fragments in human synovial fluid. Evidence for the involvement in osteoarthritis of a novel proteinase which cleaves the Glu 373-Ala 374 bond of the interglobular domain
    • Sandy JD, Flannery CR, Neame PJ, Lohmander LS: The structure of aggrecan fragments in human synovial fluid. Evidence for the involvement in osteoarthritis of a novel proteinase which cleaves the Glu 373-Ala 374 bond of the interglobular domain. J Clin Invest 1992, 89:1512-1516.
    • (1992) J. Clin. Invest. , vol.89 , pp. 1512-1516
    • Sandy, J.D.1    Flannery, C.R.2    Neame, P.J.3    Lohmander, L.S.4
  • 19
    • 0027445981 scopus 로고
    • The structure of aggrecan fragments in human synovial fluid. Evidence that aggrecanase mediates cartilage degradation in inflammatory joint disease, joint injury, and osteoarthritis
    • Lohmander LS, Neame PJ, Sandy JD: The structure of aggrecan fragments in human synovial fluid. Evidence that aggrecanase mediates cartilage degradation in inflammatory joint disease, joint injury, and osteoarthritis. Arthritis Rheum 1993, 36:1214-1222.
    • (1993) Arthritis Rheum. , vol.36 , pp. 1214-1222
    • Lohmander, L.S.1    Neame, P.J.2    Sandy, J.D.3
  • 22
    • 0035129903 scopus 로고    scopus 로고
    • ADAMTS: A novel family of extracellular matrix proteases
    • Tang BL: ADAMTS: a novel family of extracellular matrix proteases. Int J Biochem Cell Biol 2001, 33:33-44.
    • (2001) Int. J. Biochem. Cell Biol. , vol.33 , pp. 33-44
    • Tang, B.L.1
  • 23
    • 0037160539 scopus 로고    scopus 로고
    • Cloning, expression analysis, and structural characterization of seven novel human ADAMTSs, a family of metalloproteinases with disintegrin and thrombospondin-1 domains
    • Cal S, Obaya AJ, Llamazares M, Garabaya C, Quesada. V, Lóez-Otín C: Cloning, expression analysis, and structural characterization of seven novel human ADAMTSs, a family of metalloproteinases with disintegrin and thrombospondin-1 domains. Gene 2002, 283:49-62.
    • (2002) Gene , vol.283 , pp. 49-62
    • Cal, S.1    Obaya, A.J.2    Llamazares, M.3    Garabaya, C.4    Quesada, V.5    Lóez-Otín, C.6
  • 28
    • 0037547454 scopus 로고    scopus 로고
    • http://www.gene.ucl.ac.uk/nomenclature/genefamily/metallo.html
  • 29
    • 0037885266 scopus 로고    scopus 로고
    • http://www.gene.ucl.ac.uk/nomenclature/genefamily/adamts.html
  • 30
    • 0026510747 scopus 로고
    • A potential fusion peptide and an integrin ligand domain in a protein active in sperm-egg fusion
    • Blobel CP, Wolfsberg TG, Turck CW, Myles DG, Primakoff P, White JM: A potential fusion peptide and an integrin ligand domain in a protein active in sperm-egg fusion. Nature 1992, 356:248-252.
    • (1992) Nature , vol.356 , pp. 248-252
    • Blobel, C.P.1    Wolfsberg, T.G.2    Turck, C.W.3    Myles, D.G.4    Primakoff, P.5    White, J.M.6
  • 33
    • 0343196671 scopus 로고    scopus 로고
    • Kuzbanian controls proteolytic processing of Notch and mediates lateral inhibition during Drosophila and vertebrate neurogenesis
    • Pan D, Rubin GM: Kuzbanian controls proteolytic processing of Notch and mediates lateral inhibition during Drosophila and vertebrate neurogenesis. Cell 1997, 90:271-280.
    • (1997) Cell , vol.90 , pp. 271-280
    • Pan, D.1    Rubin, G.M.2
  • 37
    • 0033214761 scopus 로고    scopus 로고
    • Expression of lacunin, a large multidomain extracellular matrix protein, accompanies morphogenesis of epithelial monolayers in Manduca sexta
    • Nardi JB, Martos R, Walden KK, Lampe DJ, Robertson HM: Expression of lacunin, a large multidomain extracellular matrix protein, accompanies morphogenesis of epithelial monolayers in Manduca sexta. Insect Biochem Mol Biol 1999, 29:883-897.
    • (1999) Insect Biochem. Mol. Biol. , vol.29 , pp. 883-897
    • Nardi, J.B.1    Martos, R.2    Walden, K.K.3    Lampe, D.J.4    Robertson, H.M.5
  • 38
    • 0027190974 scopus 로고
    • The CUB domain. A widespread module in developmentally regulated proteins
    • Bork P, Beckmann G: The CUB domain. A widespread module in developmentally regulated proteins. J Mol Biol 1993, 231:539-545.
    • (1993) J. Mol. Biol. , vol.231 , pp. 539-545
    • Bork, P.1    Beckmann, G.2
  • 39
    • 0029067409 scopus 로고
    • Characterization and partial amino acid sequencing of a 107-kDa procollagen I N-proteinase purified by affinity chromatography on immobilized type XIV collagen
    • Colige A, Beschin A, Samyn B, Goebels Y, van Beeumen J, Nusgens BV, Lapière CM: Characterization and partial amino acid sequencing of a 107-kDa procollagen I N-proteinase purified by affinity chromatography on immobilized type XIV collagen. J Biol Chem 1995, 270:16724-16730.
    • (1995) J. Biol. Chem. , vol.270 , pp. 16724-16730
    • Colige, A.1    Beschin, A.2    Samyn, B.3    Goebels, Y.4    van Beeumen, J.5    Nusgens, B.V.6    Lapière, C.M.7
  • 44
    • 0032569840 scopus 로고    scopus 로고
    • Antibodies to von Willebrand factor-cleaving protease in acute thrombotic thrombocytopenic purpura
    • Tsai HM, Lian EC: Antibodies to von Willebrand factor-cleaving protease in acute thrombotic thrombocytopenic purpura. N Engl J Med 1998, 339:1585-1594.
    • (1998) N. Engl. J. Med. , vol.339 , pp. 1585-1594
    • Tsai, H.M.1    Lian, E.C.2
  • 45
    • 0038757017 scopus 로고    scopus 로고
    • METH-1, a human ortholog of ADAMTS-1, and METH-2 are members of a new family of proteins with angio-inhibitory activity
    • Vazquez F, Hastings G, Ortega MA, Lane TF, Oikemus S, Lombardo M, Iruela-Arispe ML: METH-1, a human ortholog of ADAMTS-1, and METH-2 are members of a new family of proteins with angio-inhibitory activity. J Biol Chem 1999, 274: 23349-23357.
    • (1999) J. Biol. Chem. , vol.274 , pp. 23349-23357
    • Vazquez, F.1    Hastings, G.2    Ortega, M.A.3    Lane, T.F.4    Oikemus, S.5    Lombardo, M.6    Iruela-Arispe, M.L.7
  • 47
    • 0036775227 scopus 로고    scopus 로고
    • Characterization of human aggrecanase 2 (ADAM-TS5): Substrate specificity studies and comparison with aggrecanase 1 (ADAM-TS4)
    • Tortorella MD, Liu RQ, Burn T, Newton RC, Arner E: Characterization of human aggrecanase 2 (ADAM-TS5): substrate specificity studies and comparison with aggrecanase 1 (ADAM-TS4). Matrix Biol 2002, 21:499-511.
    • (2002) Matrix Biol. , vol.21 , pp. 499-511
    • Tortorella, M.D.1    Liu, R.Q.2    Burn, T.3    Newton, R.C.4    Arner, E.5
  • 51
    • 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, 274:18821-18826.
    • (1999) J. Biol. Chem. , vol.274 , pp. 18821-18826
    • Kuno, K.1    Terashima, Y.2    Matsushima, K.3
  • 52
    • 0034725657 scopus 로고    scopus 로고
    • Brain-enriched hyaluronan binding (BEHAB)/brevican cleavage in a glioma cell line is mediated by a disintegrin and metalloproteinase with thrombospondin motifs (ADAMTS) family member
    • Matthews RT, Gary SC, Zerillo C, Pratta M, Solomon K, Arner EC, Hockfield S: Brain-enriched hyaluronan binding (BEHAB)/brevican cleavage in a glioma cell line is mediated by a disintegrin and metalloproteinase with thrombospondin motifs (ADAMTS) family member. J Biol Chem 2000, 275:22695-22703.
    • (2000) J. Biol. Chem. , vol.275 , pp. 22695-22703
    • Matthews, R.T.1    Gary, S.C.2    Zerillo, C.3    Pratta, M.4    Solomon, K.5    Arner, E.C.6    Hockfield, S.7
  • 54
    • 0034682773 scopus 로고    scopus 로고
    • The thrombospondin motif of aggrecanase-1 (ADAMTS-4) is critical for aggrecan substrate recognition and cleavage
    • Tortorella M, Pratta M, Liu RQ, Abbaszade I, Ross H, Burn T, Arner E: The thrombospondin motif of aggrecanase-1 (ADAMTS-4) is critical for aggrecan substrate recognition and cleavage. J Biol Chem 2000, 275:25791-25797.
    • (2000) J. Biol. Chem. , vol.275 , pp. 25791-25797
    • Tortorella, M.1    Pratta, M.2    Liu, R.Q.3    Abbaszade, I.4    Ross, H.5    Burn, T.6    Arner, E.7
  • 55
    • 0034671485 scopus 로고    scopus 로고
    • Age-related changes in aggrecan glycosylation affect cleavage by aggrecanase
    • Pratta MA, Tortorella MD, Arner EC: Age-related changes in aggrecan glycosylation affect cleavage by aggrecanase. J Biol Chem 2000, 275:39096-39102.
    • (2000) J. Biol. Chem. , vol.275 , pp. 39096-39102
    • Pratta, M.A.1    Tortorella, M.D.2    Arner, E.C.3
  • 56
    • 0033794135 scopus 로고    scopus 로고
    • Truncation of the amino-terminus of the recombinant aggrecan rAgg1 mut leads to reduced cleavage at the aggrecanase site. Efficient aggrecanase catabolism may depend on multiple substrate interactions
    • Hörber C, Buttner FH, Kern C, Schmiedeknecht G, Bartnik E: Truncation of the amino-terminus of the recombinant aggrecan rAgg1 mut leads to reduced cleavage at the aggrecanase site. Efficient aggrecanase catabolism may depend on multiple substrate interactions. Matrix Biol 2000, 19:533-543.
    • (2000) Matrix Biol. , vol.19 , pp. 533-543
    • Hörber, C.1    Buttner, F.H.2    Kern, C.3    Schmiedeknecht, G.4    Bartnik, E.5
  • 57
    • 0034693167 scopus 로고    scopus 로고
    • Mutations in the interglobular domain of aggrecan alter matrix metalloproteinase and aggrecanase cleavage patterns. Evidence that matrix metalloproteinase cleavage interferes with aggrecanase activity
    • Mercuri FA, Maciewicz RA, Tart J, Last K, Fosang AJ: Mutations in the interglobular domain of aggrecan alter matrix metalloproteinase and aggrecanase cleavage patterns. Evidence that matrix metalloproteinase cleavage interferes with aggrecanase activity. J Biol Chem 2000, 275:33038-33045.
    • (2000) J. Biol. Chem. , vol.275 , pp. 33038-33045
    • Mercuri, F.A.1    Maciewicz, R.A.2    Tart, J.3    Last, K.4    Fosang, A.J.5
  • 60
    • 0033525533 scopus 로고    scopus 로고
    • Generation and characterization of aggrecanase. A soluble, cartilage-derived aggrecan-degrading activity
    • Arner EC, Pratta MA, Trzaskos JM, Decicco CP, Tortorella MD: Generation and characterization of aggrecanase. A soluble, cartilage-derived aggrecan-degrading activity. J Biol Chem 1999, 274:6594-6601.
    • (1999) J. Biol. Chem. , vol.274 , pp. 6594-6601
    • Arner, E.C.1    Pratta, M.A.2    Trzaskos, J.M.3    Decicco, C.P.4    Tortorella, M.D.5
  • 61
    • 0035918309 scopus 로고    scopus 로고
    • TIMP-3 is a potent inhibitor of aggrecanase 1 (ADAM-TS4) and aggrecanase 2 (ADAM-TS5)
    • Kashiwagi M, Tortorella M, Nagase H, Brew K: TIMP-3 is a potent inhibitor of aggrecanase 1 (ADAM-TS4) and aggrecanase 2 (ADAM-TS5). J Biol Chem 2001, 276:12501-12504.
    • (2001) J. Biol. Chem. , vol.276 , pp. 12501-12504
    • Kashiwagi, M.1    Tortorella, M.2    Nagase, H.3    Brew, K.4
  • 62
    • 0035853456 scopus 로고    scopus 로고
    • Inhibition of ADAMTS4 (aggrecanase-1) by tissue inhibitors of metalloproteinases (TIMP-1, 2, 3 and 4)
    • Hashimoto G, Aoki T, Nakamura H, Tanzawa K, Okada Y: Inhibition of ADAMTS4 (aggrecanase-1) by tissue inhibitors of metalloproteinases (TIMP-1, 2, 3 and 4). FEBS Lett 2001, 494: 192-195.
    • (2001) FEBS Lett. , vol.494 , pp. 192-195
    • Hashimoto, G.1    Aoki, T.2    Nakamura, H.3    Tanzawa, K.4    Okada, Y.5
  • 66
    • 0034613296 scopus 로고    scopus 로고
    • TIMP-3 binds to sulfated glycosaminoglycans of the extracellular matrix
    • Yu WH, Yu S, Meng Q, Brew K, Woessner JF Jr: TIMP-3 binds to sulfated glycosaminoglycans of the extracellular matrix. J Biol Chem 2000, 275:31226-31232.
    • (2000) J. Biol. Chem. , vol.275 , pp. 31226-31232
    • Yu, W.H.1    Yu, S.2    Meng, Q.3    Brew, K.4    Woessner J.F., Jr.5
  • 67
    • 0027932836 scopus 로고
    • Gene encoding a novel murine tissue inhibitor of metalloproteinases (TIMP), TIMP-3, is expressed in developing mouse epithelia, cartilage, and muscle, and is located on mouse chromosome 10
    • Apte SS, Hayashi K, Seldin MF, Mattei MG, Hayashi M, Olsen BR: Gene encoding a novel murine tissue inhibitor of metalloproteinases (TIMP), TIMP-3, is expressed in developing mouse epithelia, cartilage, and muscle, and is located on mouse chromosome 10. Dev Dyn 1994, 200:177-197.
    • (1994) Dev. Dyn. , vol.200 , pp. 177-197
    • Apte, S.S.1    Hayashi, K.2    Seldin, M.F.3    Mattei, M.G.4    Hayashi, M.5    Olsen, B.R.6
  • 69
    • 0032531277 scopus 로고    scopus 로고
    • Up-regulation of tissue inhibitor of metalloproteinases-3 gene expression by TGF-beta in articular chondrocytes is mediated by serine/threonine and tyrosine kinases
    • Su S, DiBattista JA, Sun Y, Li WQ, Zafarullah M: Up-regulation of tissue inhibitor of metalloproteinases-3 gene expression by TGF-beta in articular chondrocytes is mediated by serine/threonine and tyrosine kinases. J Cell Biochem 1998, 70:517-527.
    • (1998) J. Cell Biochem. , vol.70 , pp. 517-527
    • Su, S.1    DiBattista, J.A.2    Sun, Y.3    Li, W.Q.4    Zafarullah, M.5
  • 70
    • 0001155860 scopus 로고    scopus 로고
    • Oncostatin M up-regulates tissue inhibitor of metalloproteinases-3 gene expression in articular chondrocytes via de novo transcription, protein synthesis, and tyrosine kinase- and mitogen-activated protein kinase-dependent mechanisms
    • Li WQ, Zafarullah M: Oncostatin M up-regulates tissue inhibitor of metalloproteinases-3 gene expression in articular chondrocytes via de novo transcription, protein synthesis, and tyrosine kinase- and mitogen-activated protein kinase-dependent mechanisms. J Immunol 1998, 161:5000-5007.
    • (1998) J. Immunol. , vol.161 , pp. 5000-5007
    • Li, W.Q.1    Zafarullah, M.2
  • 71
    • 0033851494 scopus 로고    scopus 로고
    • Production of tissue inhibitor of metalloproteinases 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 metalloproteinases 3 is selectively enhanced by calcium pentosan polysulfate in human rheumatoid synovial fibroblasts. Arthritis Rheum 2000, 43:812-820.
    • (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
  • 72
    • 0033784028 scopus 로고    scopus 로고
    • Calcium pentosan polysulfate inhibits the catabolism of aggrecan in articular cartilage explant cultures
    • Munteanu SE, Ilic MZ, Handley CJ: Calcium pentosan polysulfate inhibits the catabolism of aggrecan in articular cartilage explant cultures. Arthritis Rheum 2000, 43:2211-2218.
    • (2000) Arthritis Rheum. , vol.43 , pp. 2211-2218
    • Munteanu, S.E.1    Ilic, M.Z.2    Handley, C.J.3
  • 73
    • 0036701822 scopus 로고    scopus 로고
    • Highly sulfated glycosaminoglycans inhibit aggrecanase degradation of aggrecan by bovine articular cartilage explant cultures
    • Munteanu SE, Ilic MZ, Handley CJ: Highly sulfated glycosaminoglycans inhibit aggrecanase degradation of aggrecan by bovine articular cartilage explant cultures. Matrix Biol 2002, 21:429-440.
    • (2002) Matrix Biol. , vol.21 , pp. 429-440
    • Munteanu, S.E.1    Ilic, M.Z.2    Handley, C.J.3
  • 79
    • 0037093523 scopus 로고    scopus 로고
    • The 45 kDa collagen-binding fragment of fibronectin induces matrix metalloproteinase-13 synthesis by chondrocytes and aggrecan degradation by aggrecanases
    • Stanton H, Ung L, Fosang AJ: The 45 kDa collagen-binding fragment of fibronectin induces matrix metalloproteinase-13 synthesis by chondrocytes and aggrecan degradation by aggrecanases. Biochem J 2002, 364:181-190.
    • (2002) Biochem. J. , vol.364 , pp. 181-190
    • Stanton, H.1    Ung, L.2    Fosang, A.J.3
  • 80
    • 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, Gebhard PM, Haag J, Knorr T, Bartnik E, Aigner T: Relative messenger RNA expression profiling of collagenases and aggrecanases in human articular chondrocytes in vivo and in vitro. Arthritis Rheum 2002, 46:2648-2657.
    • (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
  • 82
    • 0034840936 scopus 로고    scopus 로고
    • The role of ADAM-TS4 (aggrecanase-1) and ADAM-TS5 (aggrecanase-2) in a model of cartilage degradation
    • Tortorella MD, Malfait AM, Deccico C, Arner E: The role of ADAM-TS4 (aggrecanase-1) and ADAM-TS5 (aggrecanase-2) in a model of cartilage degradation. Osteoarthritis Cartilage 2001, 9:539-552.
    • (2001) Osteoarthritis Cartilage , vol.9 , pp. 539-552
    • Tortorella, M.D.1    Malfait, A.M.2    Deccico, C.3    Arner, E.4
  • 84
    • 0036222734 scopus 로고    scopus 로고
    • The modulation of matrix metalloproteinase and ADAM gene expression in human chondrocytes by interleukin-1 and oncostatin M: A time-course study using real-time quantitative reverse transcription-polymerase chain reaction
    • Koshy PJ, Lundy CJ, Rowan AD, Porter S, Edwards DR, Hogan A, Clark IM, Cawston TE: The modulation of matrix metalloproteinase and ADAM gene expression in human chondrocytes by interleukin-1 and oncostatin M: a time-course study using real-time quantitative reverse transcription-polymerase chain reaction. Arthritis Rheum 2002, 46:961-967.
    • (2002) Arthritis Rheum. , vol.46 , pp. 961-967
    • Koshy, P.J.1    Lundy, C.J.2    Rowan, A.D.3    Porter, S.4    Edwards, D.R.5    Hogan, A.6    Clark, I.M.7    Cawston, T.E.8
  • 88
    • 0029852094 scopus 로고    scopus 로고
    • Aggrecan is degraded by matrix metalloproteinases in human arthritis. Evidence that matrix metalloproteinase and aggrecanase activities can be independent
    • Fosang AJ, Last K, Maciewicz RA: Aggrecan is degraded by matrix metalloproteinases in human arthritis. Evidence that matrix metalloproteinase and aggrecanase activities can be independent. J Clin Invest 1996, 98:2292-2299.
    • (1996) J. Clin. Invest. , vol.98 , pp. 2292-2299
    • Fosang, A.J.1    Last, K.2    Maciewicz, R.A.3
  • 89
    • 0033571592 scopus 로고    scopus 로고
    • Aggrecanase versus matrix metalloproteinases in the catabolism of the interglobular domain of aggrecan in vitro
    • Little CB, Flannery CR, Hughes CE, Mort JS, Roughley PJ, Dent C, Caterson B: Aggrecanase versus matrix metalloproteinases in the catabolism of the interglobular domain of aggrecan in vitro. Biochem J 1999, 344:61-68.
    • (1999) Biochem. J. , vol.344 , pp. 61-68
    • Little, C.B.1    Flannery, C.R.2    Hughes, C.E.3    Mort, J.S.4    Roughley, P.J.5    Dent, C.6    Caterson, B.7
  • 91
    • 0034693231 scopus 로고    scopus 로고
    • Generation and novel distribution of matrix metalloproteinase-derived aggrecan fragments in porcine cartilage explants
    • Fosang AJ, Last K, Stanton H, Weeks DB, Campbell IK, Hardingham TE, Hembry RM: Generation and novel distribution of matrix metalloproteinase-derived aggrecan fragments in porcine cartilage explants. J Biol Chem 2000, 275:33027-33037.
    • (2000) J. Biol. Chem. , vol.275 , pp. 33027-33037
    • Fosang, A.J.1    Last, K.2    Stanton, H.3    Weeks, D.B.4    Campbell, I.K.5    Hardingham, T.E.6    Hembry, R.M.7
  • 92
    • 0036701567 scopus 로고    scopus 로고
    • Matrix metalloproteinases are active following guanidine hydrochloride extraction of cartilage: Generation of DIPEN neoepitope during dialysis
    • Stanton H, Fosang AJ: Matrix metalloproteinases are active following guanidine hydrochloride extraction of cartilage: generation of DIPEN neoepitope during dialysis. Matrix Biol 2002, 21:425-428.
    • (2002) Matrix Biol. , vol.21 , pp. 425-428
    • Stanton, H.1    Fosang, A.J.2
  • 93
    • 0036499471 scopus 로고    scopus 로고
    • The mechanism of aggrecan release from cartilage differs with tissue origin and the agent used to stimulate catabolism
    • Sztrolovics R, White RJ, Roughley PJ, Mort JS: The mechanism of aggrecan release from cartilage differs with tissue origin and the agent used to stimulate catabolism. Biochem J 2002, 362:465-472.
    • (2002) Biochem. J. , vol.362 , pp. 465-472
    • Sztrolovics, R.1    White, R.J.2    Roughley, P.J.3    Mort, J.S.4
  • 94
    • 0034866208 scopus 로고    scopus 로고
    • Enzymes active in the areas undergoing cartilage resorption during the development of the secondary ossification center in the tibiae of rats ages 0-21 days: I. Two groups of proteinases cleave the core protein of aggrecan
    • Lee ER, Lamplugh L, Davoli MA, Beauchemin A, Chan K, Mort JS, Leblond CP: Enzymes active in the areas undergoing cartilage resorption during the development of the secondary ossification center in the tibiae of rats ages 0-21 days: I. Two groups of proteinases cleave the core protein of aggrecan. Dev Dyn 2001, 222:52-70.
    • (2001) Dev. Dyn. , vol.222 , pp. 52-70
    • Lee, E.R.1    Lamplugh, L.2    Davoli, M.A.3    Beauchemin, A.4    Chan, K.5    Mort, J.S.6    Leblond, C.P.7
  • 96
    • 0035884605 scopus 로고    scopus 로고
    • Analysis of aggrecan in human knee cartilage and synovial fluid indicates that aggrecanase (ADAMTS) activity is responsible for the catabolic turnover and loss of whole aggrecan whereas other protease activity is required for C-terminal processing in vivo
    • Sandy JD, Verscharen C: Analysis of aggrecan in human knee cartilage and synovial fluid indicates that aggrecanase (ADAMTS) activity is responsible for the catabolic turnover and loss of whole aggrecan whereas other protease activity is required for C-terminal processing in vivo. Biochem J 2001, 358:615-626.
    • (2001) Biochem. J. , vol.358 , pp. 615-626
    • Sandy, J.D.1    Verscharen, C.2
  • 97
    • 0033000529 scopus 로고    scopus 로고
    • Kinetics of aggrecanase- and metalloproteinase-induced neoepitopes in various stages of cartilage destruction in murine arthritis
    • van Meurs JB, van Lent PL, Holthuysen AE, Singer II, Bayne EK, van den Berg WB: Kinetics of aggrecanase- and metalloproteinase-induced neoepitopes in various stages of cartilage destruction in murine arthritis. Arthritis Rheum 1999, 42:1128-1139.
    • (1999) Arthritis Rheum. , vol.42 , pp. 1128-1139
    • van Meurs, J.B.1    van Lent, P.L.2    Holthuysen, A.E.3    Singer, I.I.4    Bayne, E.K.5    van den Berg, W.B.6
  • 98
  • 100
    • 0032211766 scopus 로고    scopus 로고
    • Cathepsin B: An alternative protease for the generation of an aggrecan 'metalloproteinase' cleavage neoepitope
    • Mort JS, Magny MC, Lee ER: Cathepsin B: an alternative protease for the generation of an aggrecan 'metalloproteinase' cleavage neoepitope. Biochem J 1998, 335:491-494.
    • (1998) Biochem. J. , vol.335 , pp. 491-494
    • Mort, J.S.1    Magny, M.C.2    Lee, E.R.3
  • 102
    • 0034971357 scopus 로고    scopus 로고
    • Matrix metalloproteinases and aggrecanases cleave aggrecan in different zones of normal cartilage but colocalize in the development of osteoarthritic lesions in STR/ort mice
    • Chambers MG, Cox L, Chong L, Suri N, Cover P, Bayliss MT, Mason RM: Matrix metalloproteinases and aggrecanases cleave aggrecan in different zones of normal cartilage but colocalize in the development of osteoarthritic lesions in STR/ort mice. Arthritis Rheum 2001, 44:1455-1465.
    • (2001) Arthritis Rheum. , vol.44 , pp. 1455-1465
    • Chambers, M.G.1    Cox, L.2    Chong, L.3    Suri, N.4    Cover, P.5    Bayliss, M.T.6    Mason, R.M.7
  • 103
    • 0035906242 scopus 로고    scopus 로고
    • A disintegrin and metalloprotease with thrombospondin type1 motifs (ADAMTS-1) and IL-1 receptor type 1 mRNAs are simultaneously induced in nerve injured motor neurons
    • Sasaki M, Seo-Kiryu S, Kato R, Kita S, Kiyama H: A disintegrin and metalloprotease with thrombospondin type1 motifs (ADAMTS-1) and IL-1 receptor type 1 mRNAs are simultaneously induced in nerve injured motor neurons. Brain Res Mol Brain Res 2001, 89:158-163.
    • (2001) Brain Res. Mol. Brain Res. , vol.89 , pp. 158-163
    • Sasaki, M.1    Seo-Kiryu, S.2    Kato, R.3    Kita, S.4    Kiyama, H.5
  • 105
    • 0035400082 scopus 로고    scopus 로고
    • Intact aggrecan and fragments generated by both aggrecanse and metalloproteinase-like activities are present in the developing and adult rat spinal cord and their relative abundance is altered by injury
    • Lemons ML, Sandy JD, Anderson DK, Howland DR: Intact aggrecan and fragments generated by both aggrecanse and metalloproteinase-like activities are present in the developing and adult rat spinal cord and their relative abundance is altered by injury. J Neurosci 2001, 21:4772-4781.
    • (2001) J. Neurosci. , vol.21 , pp. 4772-4781
    • Lemons, M.L.1    Sandy, J.D.2    Anderson, D.K.3    Howland, D.R.4
  • 106
    • 0034637052 scopus 로고    scopus 로고
    • ADAMTS-4 (a disintegrin and metalloproteinase with thrombospondin motifs) is transcriptionally induced in beta-amyloid treated rat astrocytes
    • Satoh K, Suzuki N, Yokota H: ADAMTS-4 (a disintegrin and metalloproteinase with thrombospondin motifs) is transcriptionally induced in beta-amyloid treated rat astrocytes. Neurosci Lett 2000, 289:177-180.
    • (2000) Neurosci. Lett. , vol.289 , pp. 177-180
    • Satoh, K.1    Suzuki, N.2    Yokota, H.3
  • 108
    • 0033848451 scopus 로고    scopus 로고
    • The relative importance of cysteine peptidases in osteoarthritis
    • Lang A, Horler D, Baici A: The relative importance of cysteine peptidases in osteoarthritis. J Rheumatol 2000, 27:1970-1979.
    • (2000) J. Rheumatol. , vol.27 , pp. 1970-1979
    • Lang, A.1    Horler, D.2    Baici, A.3


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