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Volumn 56, Issue 2, 1997, Pages 108-113

Temporal pattern of cysteine endopeptidase (cathepsin B) expression in cartilage and synovium from rabbit knees with experimental osteoarthritis: Gene expression in chondrocytes in response to interleukin-1 and matrix depletion

Author keywords

[No Author keywords available]

Indexed keywords

CATHEPSIN B; INTERLEUKIN 1BETA;

EID: 0030943690     PISSN: 00034967     EISSN: None     Source Type: Journal    
DOI: 10.1136/ard.56.2.108     Document Type: Article
Times cited : (36)

References (26)
  • 1
    • 0024712236 scopus 로고
    • Evidence for metalloproteinase and metalloproteinase inhibitor (TIMP) imbalance in human osteoarthritic cartilage
    • Dean DD, Martel-Pelletier J, Pelletier J-P, Howell DS, Woessner JJF. Evidence for metalloproteinase and metalloproteinase inhibitor (TIMP) imbalance in human osteoarthritic cartilage. J Clin Invest 1989;84:678-85.
    • (1989) J Clin Invest , vol.84 , pp. 678-685
    • Dean, D.D.1    Martel-Pelletier, J.2    Pelletier, J.-P.3    Howell, D.S.4    Woessner, J.J.F.5
  • 2
    • 0026701977 scopus 로고
    • The interglobular domain of cartilage aggrecan is cleaved by PUMP, gelatinase and cathepsin B
    • Fosang AJ, Neame PJ, Last K, Hardingham T , Murphy G. The interglobular domain of cartilage aggrecan is cleaved by PUMP, gelatinase 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.4    Murphy, G.5
  • 3
    • 0026575258 scopus 로고
    • Degradation of extracellular matrix proteins by human cathepsin B from normal and tumor tissues
    • Buck MR, Karustis DJ, Day NA, Honn KV, Sloane BF. Degradation of extracellular matrix proteins by human cathepsin B from normal and tumor tissues. Biochem J 1992;282:273-8.
    • (1992) Biochem J , vol.282 , pp. 273-278
    • Buck, M.R.1    Karustis, D.J.2    Day, N.A.3    Honn, K.V.4    Sloane, B.F.5
  • 5
    • 0025061478 scopus 로고
    • Susceptibility of the cartilage collagens types II, IX and XI to degradation by the cysteine proteinases, cathepsin B and L
    • Maciewicz RA, Wolton SF, Etherington DJ, Duance VC. Susceptibility of the cartilage collagens types II, IX and XI to degradation by the cysteine proteinases, cathepsin B and L. FEBS Lett 1990;269:189-93.
    • (1990) FEBS Lett , vol.269 , pp. 189-193
    • Maciewicz, R.A.1    Wolton, S.F.2    Etherington, D.J.3    Duance, V.C.4
  • 6
    • 0025821115 scopus 로고
    • Link protein as a monitor in situ of endogenous proteolysis in adult human articular cartilage
    • Nguyen Q, Liu J, Roughley PJ, Mort JS. Link protein as a monitor in situ of endogenous proteolysis in adult human articular cartilage. Biochem J 1991;278:143-7.
    • (1991) Biochem J , vol.278 , pp. 143-147
    • Nguyen, Q.1    Liu, J.2    Roughley, P.J.3    Mort, J.S.4
  • 7
    • 0025424354 scopus 로고
    • Cathepsin B and cysteine protease inhibitors in human osteoarthritis
    • Martel-Pelletier J, Cloutier JM, Pelletier J-P. Cathepsin B and cysteine protease inhibitors in human osteoarthritis. J Orthop Res 1990;8:336-44.
    • (1990) J Orthop Res , vol.8 , pp. 336-344
    • Martel-Pelletier, J.1    Cloutier, J.M.2    Pelletier, J.-P.3
  • 8
    • 0028907722 scopus 로고
    • Cathepsin B in osteoarthritis: Zonal variation of enzyme activity in human femoral head
    • Baici A, Horler D, Lang A, Merlin C, Kissling R. Cathepsin B in osteoarthritis: zonal variation of enzyme activity in human femoral head. Annals Rheum Dis 1995;54:281-8.
    • (1995) Annals Rheum Dis , vol.54 , pp. 281-288
    • Baici, A.1    Horler, D.2    Lang, A.3    Merlin, C.4    Kissling, R.5
  • 9
    • 0028901908 scopus 로고
    • Cathepsin B in osteoarthritis: Cytochemical and histochemical analysis of human femoral head cartilage
    • Baici A, Lang A, Horler D, Kissling R, Merlin C. Cathepsin B in osteoarthritis: cytochemical and histochemical analysis of human femoral head cartilage. Ann Rheum Dis 1995;54:289-97.
    • (1995) Ann Rheum Dis , vol.54 , pp. 289-297
    • Baici, A.1    Lang, A.2    Horler, D.3    Kissling, R.4    Merlin, C.5
  • 10
    • 0027438713 scopus 로고
    • Inhibition of cartilage proteoglycan release by a specific inactivator of cathepsin B and inhibitor of matrix metalloproteases
    • Buttle DJ, Handley CJ, Ilic MZ, Saklatvala J, Murata M, Barrett AJ. Inhibition of cartilage proteoglycan release by a specific inactivator of cathepsin B and inhibitor of matrix metalloproteases. Arthritis Rheum 1993;36:1709-17.
    • (1993) Arthritis Rheum , vol.36 , pp. 1709-1717
    • Buttle, D.J.1    Handley, C.J.2    Ilic, M.Z.3    Saklatvala, J.4    Murata, M.5    Barrett, A.J.6
  • 11
    • 0028055132 scopus 로고
    • Cysteine proteinase inhibitors decrease articular cartilage and bone destruction in chronic inflammatory arthritis
    • Esser RE, Angelo RA, Murphey MD, Watts LM, Thornburg LP, Palmer JT, et al. Cysteine proteinase inhibitors decrease articular cartilage and bone destruction in chronic inflammatory arthritis. Arthritis Rheum 1994; 37:236-47.
    • (1994) Arthritis Rheum , vol.37 , pp. 236-247
    • Esser, R.E.1    Angelo, R.A.2    Murphey, M.D.3    Watts, L.M.4    Thornburg, L.P.5    Palmer, J.T.6
  • 12
    • 0025606499 scopus 로고
    • Effect of interleukin-1 on the production of cathepsin B by rabbit articular chondrocytes
    • Baici A, Lang A. Effect of interleukin-1 on the production of cathepsin B by rabbit articular chondrocytes. FEBS Lett 1990;277:93-6.
    • (1990) FEBS Lett , vol.277 , pp. 93-96
    • Baici, A.1    Lang, A.2
  • 13
    • 0027295108 scopus 로고
    • Stimulation of the secretion of latent cysteine proteinase activity by tumor necrosis factor-α and interleukin-1
    • Huet G, Flipo RM, Colin C, Janin A, Hemon B, Hooghe M, et al. Stimulation of the secretion of latent cysteine proteinase activity by tumor necrosis factor-α and interleukin-1. Arthritis Rheum 1993;36:772-80.
    • (1993) Arthritis Rheum , vol.36 , pp. 772-780
    • Huet, G.1    Flipo, R.M.2    Colin, C.3    Janin, A.4    Hemon, B.5    Hooghe, M.6
  • 14
    • 0026712292 scopus 로고
    • Lysosomal cysteine endopeptidases mediate interleukin-1 stimulated cartilage proteoglycan degradation
    • Buttle DJ, Saklatvala J. Lysosomal cysteine endopeptidases mediate interleukin-1 stimulated cartilage proteoglycan degradation. Biochem J 1992;287:657-61.
    • (1992) Biochem J , vol.287 , pp. 657-661
    • Buttle, D.J.1    Saklatvala, J.2
  • 15
    • 0015619712 scopus 로고
    • Experimentally induced degenerative joint lesions following partial meniscectomy in the rabbit
    • Moskowitz RW, Davis W, Sammarco J, Martens M, Baker J, Mayer M, et al. Experimentally induced degenerative joint lesions following partial meniscectomy in the rabbit. Arthritis Rheum 1973;16:397-405.
    • (1973) Arthritis Rheum , vol.16 , pp. 397-405
    • Moskowitz, R.W.1    Davis, W.2    Sammarco, J.3    Martens, M.4    Baker, J.5    Mayer, M.6
  • 16
    • 0000249898 scopus 로고
    • Nucleotide and predicted amino acid sequences of cloned human and mouse preprocathepsin B cDNAs
    • Chan SJ, Segundo BS, McCormick MB, Steiner DF. Nucleotide and predicted amino acid sequences of cloned human and mouse preprocathepsin B cDNAs. Proc Natl Acad Sci USA 1986;83:7721-5.
    • (1986) Proc Natl Acad Sci USA , vol.83 , pp. 7721-7725
    • Chan, S.J.1    Segundo, B.S.2    McCormick, M.B.3    Steiner, D.F.4
  • 18
    • 0028061750 scopus 로고
    • Prostromelysin and procollagenase genes are differentially up-regulated in chondrocyts from the knees of rabbits with experimental osteoarthritis
    • Mehraban F, Kuo S-Y, Riera H, Chang C, Moskowitz RW. Prostromelysin and procollagenase genes are differentially up-regulated in chondrocyts from the knees of rabbits with experimental osteoarthritis. Arthritis Rheum 1994; 37:1189-97.
    • (1994) Arthritis Rheum , vol.37 , pp. 1189-1197
    • Mehraban, F.1    Kuo, S.-Y.2    Riera, H.3    Chang, C.4    Moskowitz, R.W.5
  • 19
    • 0027319177 scopus 로고
    • Characterization of the cathepsin B gene and multiple mRNAs in human tissues: Evidence for alternative splicing of cathepsin B pre-mRNA
    • Gong Q, Chan SJ, Bajkowski AS, Steiner DF, Frankfater A. Characterization of the cathepsin B gene and multiple mRNAs in human tissues: evidence for alternative splicing of cathepsin B pre-mRNA. DNA Cell Biol 1993;12:299-309.
    • (1993) DNA Cell Biol , vol.12 , pp. 299-309
    • Gong, Q.1    Chan, S.J.2    Bajkowski, A.S.3    Steiner, D.F.4    Frankfater, A.5
  • 20
    • 0026111656 scopus 로고
    • Role of metalloproteinases in human osteoarthritis
    • Woessner JF, Gunja-Smith Z. Role of metalloproteinases in human osteoarthritis. J Rheumatol (suppl) 1991;27:99-101.
    • (1991) J Rheumatol (Suppl) , vol.27 , pp. 99-101
    • Woessner, J.F.1    Gunja-Smith, Z.2
  • 21
  • 22
    • 0027442510 scopus 로고
    • Matrix metalloproteinase-3 (stromelysin-1). Identification as the cartilage acid metalloprotease and effect of pH on catalytic properties and calcium affinity
    • Wilhelm SM, Shao ZH, Housley TJ, Seperack PK, Baumann AP, Gunja Smith Z, et al. Matrix metalloproteinase-3 (stromelysin-1). Identification as the cartilage acid metalloprotease and effect of pH on catalytic properties and calcium affinity. J Biol Chem 1993; 268:21906-13.
    • (1993) J Biol Chem , vol.268 , pp. 21906-21913
    • Wilhelm, S.M.1    Shao, Z.H.2    Housley, T.J.3    Seperack, P.K.4    Baumann, A.P.5    Gunja Smith, Z.6
  • 23
    • 0027015335 scopus 로고
    • Physiological mechanisms of metalloproteinase activation
    • Murphy G, Ward R, Gavrilovic J, Atkinson S. Physiological mechanisms of metalloproteinase activation. Matrix 1992; suppl 1:224-30.
    • (1992) Matrix , Issue.1 SUPPL. , pp. 224-230
    • Murphy, G.1    Ward, R.2    Gavrilovic, J.3    Atkinson, S.4
  • 24
    • 0028939165 scopus 로고
    • Synthesis and secretion of procathepsin B and cystatin C by human bronchial epithelial cells in vitro: Modulation of cathepsin B activity by neutrophil elastase
    • Burnett D, Abrahamson M, Devalia JL, Sapsford RJ, Davies RJ, Buttle DJ. Synthesis and secretion of procathepsin B and cystatin C by human bronchial epithelial cells in vitro: modulation of cathepsin B activity by neutrophil elastase. Arch Biochem Biophys 1995;317:305-10.
    • (1995) Arch Biochem Biophys , vol.317 , pp. 305-310
    • Burnett, D.1    Abrahamson, M.2    Devalia, J.L.3    Sapsford, R.J.4    Davies, R.J.5    Buttle, D.J.6
  • 25
    • 0028048344 scopus 로고
    • Cathepsin B in tumors, normal tissue and isolated cells from the human lung
    • Werle B, Ebert W, Klein W, Spiess E. Cathepsin B in tumors, normal tissue and isolated cells from the human lung. Anticancer Res 1994;14:1169-76.
    • (1994) Anticancer Res , vol.14 , pp. 1169-1176
    • Werle, B.1    Ebert, W.2    Klein, W.3    Spiess, E.4
  • 26
    • 0023801964 scopus 로고
    • Cathepsin B as a marker of the dedifferentiated chondrocyte phenotype
    • Baici A, Lang A, Horler D, Knopfel M. Cathepsin B as a marker of the dedifferentiated chondrocyte phenotype. Ann Rheum Dis 1988;47:684-91.
    • (1988) Ann Rheum Dis , vol.47 , pp. 684-691
    • Baici, A.1    Lang, A.2    Horler, D.3    Knopfel, M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.