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Volumn 6, Issue 3, 1998, Pages 214-228

Cytokine-induced cartilage proteoglycan degradation is mediated by aggrecanase

Author keywords

Aggrecanase; Cartilage; Cytokines; Matrix metalloproteinase; Proteoglycan degradation

Indexed keywords

AGGRECAN; AGGRECANASE; DEXAMETHASONE; DOXYCYCLINE; INDOMETACIN; INTERLEUKIN 1; MONOCLONAL ANTIBODY; MONOCLONAL ANTIBODY BC 3; NAPROXEN; TENIDAP; TUMOR NECROSIS FACTOR; UNCLASSIFIED DRUG;

EID: 0032076280     PISSN: 10634584     EISSN: None     Source Type: Journal    
DOI: 10.1053/joca.1998.0114     Document Type: Article
Times cited : (130)

References (53)
  • 1
    • 0014770490 scopus 로고
    • Biochemical and metabolic abnormalities inarticular cartilage from osteo-arthritic human hips
    • 1. Mankin HJ, Lippiello L. Biochemical and metabolic abnormalities inarticular cartilage from osteo-arthritic human hips. J Bone Joint Surg[Am] 1970;52:424-34.
    • (1970) J Bone Joint Surg[Am] , vol.52 , pp. 424-434
    • Mankin, H.J.1    Lippiello, L.2
  • 2
    • 0025743297 scopus 로고
    • Analysis of the catabolism ofaggrecan in cartilage expiants by quantitation of peptides from the three globular domains
    • 2. Sandy JD, Boynton RE, Flannery CR. Analysis of the catabolism ofaggrecan in cartilage expiants by quantitation of peptides from the three globular domains. J Biol Chem 1991;266:8198-205.
    • (1991) J Biol Chem , vol.266 , pp. 8198-8205
    • Sandy, J.D.1    Boynton, R.E.2    Flannery, C.R.3
  • 3
    • 0026701977 scopus 로고
    • The interglobular domain of cartilage aggrecan is cleaved by PUMP, gelatinases, and cathepsin B
    • 3. Fosang AJ, Neame PJ, Last K, Hardingham TE, Murphy G, Hamilton JA. The interglobular domain of cartilage aggrecan is cleaved by PUMP, gelatinases, and cathepsin B. J Biol Chem 1992;267:19470-4.
    • (1992) J Biol Chem , vol.267 , pp. 19470-19474
    • Fosang, A.J.1    Neame, P.J.2    Last, K.3    Hardingham, T.E.4    Murphy, G.5    Hamilton, J.A.6
  • 4
    • 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
    • 4. 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; 267:1008-14.
    • (1992) J Biol Chem , vol.267 , pp. 1008-1014
    • Flannery, C.R.1    Lark, M.W.2    Sandy, J.D.3
  • 5
    • 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 Glu373-Ala374 bond of the interglobular domain
    • 5. 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 Glu373-Ala374 bond of the interglobular domain. J Clin Invest 1992;89:1512-6.
    • (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
  • 6
    • 0027445981 scopus 로고
    • The structure of aggrecan fragments in human synovial fluid. Evidence that aggrecanase mediates cartilage degradation in inflammatory joint disease, joint injury, andosteoarthritis
    • 6. 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, andosteoarthritis. Arthritis Rheum 1993;36:1214-22.
    • (1993) Arthritis Rheum , vol.36 , pp. 1214-1222
    • Lohmander, L.S.1    Neame, P.J.2    Sandy, J.D.3
  • 7
    • 0025776382 scopus 로고
    • Catabolism of aggrecan in cartilage expiants. Identification of a major cleavage site within the interglobular domain
    • 7. Sandy JD, Neame PJ, Boynton RE, Flannery CR. Catabolism of aggrecan in cartilage expiants. Identification of a major cleavage site within the interglobular domain. J Biol Chem 1991;266: 8683-5.
    • (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
  • 8
    • 0026771893 scopus 로고
    • N-terminal sequence of proteoglycan fragments isolated from medium of interleukin-1-treated articular-cartilage cultures. Putative site(s) of enzymatic cleavage
    • 8. 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 enzymatic cleavage. Biochem J 1992; 284(Pt 2): 589-93.
    • (1992) Biochem J , vol.284 , Issue.PT 2 , pp. 589-593
    • Loulakis, P.1    Shrikhande, A.2    Davis, G.3    Maniglia, C.A.4
  • 10
    • 0028815147 scopus 로고
    • Cell-mediated catabolism of aggrecan. Evidence that cleavage at the 'aggrecanase' site (Glu373-Ala374) is a primary event in proteolysis of the interglobular domain
    • 10. Lark MW, Gordy JT, Weidner JR, Ayala J, Kimura JH, Williams HR et al. Cell-mediated catabolism of aggrecan. Evidence that cleavage at the 'aggrecanase' site (Glu373-Ala374) is a primary event in proteolysis of the interglobular domain. J Biol Chem 1995;270:2550-6.
    • (1995) J Biol Chem , vol.270 , pp. 2550-2556
    • Lark, M.W.1    Gordy, J.T.2    Weidner, J.R.3    Ayala, J.4    Kimura, J.H.5    Williams, H.R.6
  • 11
    • 0027369012 scopus 로고
    • Fibroblast and neutrephil collagenases cleave at two sites in the cartilage aggrecan interglobular domain
    • 11. Fosang AJ, Last K, Knauper V, Neame PJ, Murphy G, Hardingham TE et al. Fibroblast and neutrephil collagenases cleave at two sites in the cartilage aggrecan interglobular domain. Biochem J 1993;295:273-6.
    • (1993) Biochem J , vol.295 , pp. 273-276
    • Fosang, A.J.1    Last, K.2    Knauper, V.3    Neame, P.J.4    Murphy, G.5    Hardingham, T.E.6
  • 12
    • 0030024311 scopus 로고    scopus 로고
    • Degradation of cartilage aggrecan by collagenase-3 (MMP-13)
    • 12. Fosang AJ, Last K, Knauper V, Murphy G, Neame PJ. Degradation of cartilage aggrecan by collagenase-3 (MMP-13). FEBS Lett 1996;380: 17-20.
    • (1996) FEBS Lett , vol.380 , pp. 17-20
    • Fosang, A.J.1    Last, K.2    Knauper, V.3    Murphy, G.4    Neame, P.J.5
  • 13
    • 0000428894 scopus 로고
    • Aggrecan catabolism in cartilage: Studies on the nature of a novel proteinase (aggrecanase) which cleaves the Glu373-Ala374 bond of the interglobular domain
    • 13. Flannery CR, Sandy JD. Aggrecan catabolism in cartilage: studies on the nature of a novel proteinase (aggrecanase) which cleaves the Glu373-Ala374 bond of the interglobular domain. Trans Orthop Res Soc 1993;18:190.
    • (1993) Trans Orthop Res Soc , vol.18 , pp. 190
    • Flannery, C.R.1    Sandy, J.D.2
  • 14
    • 0028127495 scopus 로고
    • Neutrophil collagenase (MMP-8) cleaves at the aggrecanase site E373-A374 in the interglobular domain of cartilage aggrecan
    • 14. Fosang AJ, Last K, Neame PJ, Murphy G, Knauper V, Tschesche H et al. Neutrophil collagenase (MMP-8) cleaves at the aggrecanase site E373-A374 in the interglobular domain of cartilage aggrecan. Biochem J 1994;304:347-51.
    • (1994) Biochem J , vol.304 , pp. 347-351
    • Fosang, A.J.1    Last, K.2    Neame, P.J.3    Murphy, G.4    Knauper, V.5    Tschesche, H.6
  • 15
    • 0030910398 scopus 로고    scopus 로고
    • Cleavage of native cartilage aggrecan by neutrophil collagenase (MMP-8) is distinct from endogenous cleavage by aggrecanase
    • 15. Arner EC, Decicco CP, Cherney R, Tortorella MD. Cleavage of native cartilage aggrecan by neutrophil collagenase (MMP-8) is distinct from endogenous cleavage by aggrecanase. J Biol Chem 1997;272:9294-9.
    • (1997) J Biol Chem , vol.272 , pp. 9294-9299
    • Arner, E.C.1    Decicco, C.P.2    Cherney, R.3    Tortorella, M.D.4
  • 16
    • 0030033710 scopus 로고    scopus 로고
    • Chondrocyte matrix metalloproteinase-8: Up-regulation ofneutrophil collagenase by interleukin-1 beta in human cartilage from knee and ankle joints
    • 16. Chubinskaya S, Huch K, Mikecz K, Cs-Szabo G, Hasty KA, Kuettner KE, Cole AA. Chondrocyte matrix metalloproteinase-8: up-regulation ofneutrophil collagenase by interleukin-1 beta in human cartilage from knee and ankle joints. Lab Invest 1996;74:232-40.
    • (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
  • 17
    • 0028919163 scopus 로고
    • Monoclonal antibodies that specifically recognize neoepitope sequences generated by 'aggrecanase' and matrix metalloproteinase cleavage of aggrecan: Application to catabolism in situ and in vitro
    • 17. Hughes CE, Caterson B, Fosang AJ, Roughley PJ, Mort JS. Monoclonal antibodies that specifically recognize neoepitope sequences generated by 'aggrecanase' and matrix metalloproteinase cleavage of aggrecan: application to catabolism in situ and in vitro. Biochem J 1995;305:799-804.
    • (1995) Biochem J , vol.305 , pp. 799-804
    • Hughes, C.E.1    Caterson, B.2    Fosang, A.J.3    Roughley, P.J.4    Mort, J.S.5
  • 18
    • 0023354578 scopus 로고
    • High-level expression in Escherichia coli of a soluble and fully active recombinant interleukin-1 beta
    • 18. Huang JJ, Newton RC, Pezzella K, Covington M, Tamblyn T, Rutlege SJ et al. High-level expression in Escherichia coli of a soluble and fully active recombinant interleukin-1 beta. Mol Biol Med 1987;4:169-81.
    • (1987) Mol Biol Med , vol.4 , pp. 169-181
    • Huang, J.J.1    Newton, R.C.2    Pezzella, K.3    Covington, M.4    Tamblyn, T.5    Rutlege, S.J.6
  • 19
    • 1842406549 scopus 로고    scopus 로고
    • Utiliation of a recombinant substrate (rAgg1) to study the biochemical properties of 'aggrecanase' in cell culture systems
    • 19. Hughes CE, Buttner FH, Eidenmuller B, Caterson B, Bartnik. Utiliation of a recombinant substrate (rAgg1) to study the biochemical properties of 'aggrecanase' in cell culture systems. J Biol Chem 1997;272:20269-72.
    • (1997) J Biol Chem , vol.272 , pp. 20269-20272
    • Hughes, C.E.1    Buttner, F.H.2    Eidenmuller, B.3    Caterson, B.4    Bartnik5
  • 22
    • 0018759373 scopus 로고
    • A tissue-culture model of cartilage breakdown in rheumatoid arthritis. Quantitative aspects of proteoglycan release
    • 22. Steinberg J, Sledge CB, Noble J, Stirrat CR. A tissue-culture model of cartilage breakdown in rheumatoid arthritis. Quantitative aspects of proteoglycan release. Biochem J 1979; 180:403-12.
    • (1979) Biochem J , vol.180 , pp. 403-412
    • Steinberg, J.1    Sledge, C.B.2    Noble, J.3    Stirrat, C.R.4
  • 23
    • 0025836186 scopus 로고
    • Modulation of interleukin-1-induced alterations in cartilage proteoglycan metabolism by activation of protein kinase C
    • 23. Arner EC, Pratta MA. Modulation of interleukin-1-induced alterations in cartilage proteoglycan metabolism by activation of protein kinase C. Arthritis Rheum 1991;34:1006-13.
    • (1991) Arthritis Rheum , vol.34 , pp. 1006-1013
    • Arner, E.C.1    Pratta, M.A.2
  • 24
    • 0014669991 scopus 로고
    • Proteinpolysaccharide complex from bovine nasal cartilage. The function of glycoprotein in the formation of aggregates
    • 24. Hascall VC, Sajdera SW. Proteinpolysaccharide complex from bovine nasal cartilage. The function of glycoprotein in the formation of aggregates. J Biol Chem 1969;244:2384-96.
    • (1969) J Biol Chem , vol.244 , pp. 2384-2396
    • Hascall, V.C.1    Sajdera, S.W.2
  • 25
    • 0019914963 scopus 로고
    • A direct spectrophotometric microassay for sulfated glycosaminoglycans in cartilage cultures
    • 25. Farndale RW, Sayers CA, Barrett AJ. A direct spectrophotometric microassay for sulfated glycosaminoglycans in cartilage cultures. Connect Tissue Res 1982;9:247-8.
    • (1982) Connect Tissue Res , vol.9 , pp. 247-248
    • Farndale, R.W.1    Sayers, C.A.2    Barrett, A.J.3
  • 26
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • 26. Laemmli UK. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970;227:680-5.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 27
    • 0026714961 scopus 로고
    • Monoclonal antibodies recognizing pro tease-generated neoepitopes from cartilage proteoglycan degradation. Application to studies of human link protein cleavage by stromelysin
    • 27. Hughes CE, Caterson B, White RJ, Roughley PJ, Mort JS. Monoclonal antibodies recognizing pro tease-generated neoepitopes from cartilage proteoglycan degradation. Application to studies of human link protein cleavage by stromelysin. J Biol Chem 1992;267:16011-4.
    • (1992) J Biol Chem , vol.267 , pp. 16011-16014
    • Hughes, C.E.1    Caterson, B.2    White, R.J.3    Roughley, P.J.4    Mort, J.S.5
  • 28
    • 0024523257 scopus 로고
    • Independent effects of interleukin-1 on proteoglycan breakdown, proteoglycan synthesis, and prostaglandin E2 release from cartilage in organ culture
    • 28. Arner EC, Pratta MA. Independent effects of interleukin-1 on proteoglycan breakdown, proteoglycan synthesis, and prostaglandin E2 release from cartilage in organ culture. Arthritis Rheum 1989;32:288-97.
    • (1989) Arthritis Rheum , vol.32 , pp. 288-297
    • Arner, E.C.1    Pratta, M.A.2
  • 30
    • 0029843761 scopus 로고    scopus 로고
    • Isothiazolones intefere with normal matrix metalloproteinase activation and inhibit cartilage proteoglycan degradation
    • 30. Arner EC, Pratta MA, Freimark B, Lischwe M, Trzaskos JM, Magolda RL, Wright SW. Isothiazolones intefere with normal matrix metalloproteinase activation and inhibit cartilage proteoglycan degradation. Biochem J 1996;318: 417-24.
    • (1996) Biochem J , vol.318 , pp. 417-424
    • Arner, E.C.1    Pratta, M.A.2    Freimark, B.3    Lischwe, M.4    Trzaskos, J.M.5    Magolda, R.L.6    Wright, S.W.7
  • 31
    • 18744437369 scopus 로고    scopus 로고
    • Aggrecan degradation in human cartilage: Evidence for both matrix metalloproteinase and aggrecanase activity in normal, osteoarthritic and rheumatoid joints
    • 31. Lark, MW, Bayne EK, Flanagan J, Harper CF, Hoerner LA, Hutchinson NI et al. Aggrecan degradation in human cartilage: evidence for both matrix metalloproteinase and aggrecanase activity in normal, osteoarthritic and rheumatoid joints. J Clin Invest 1997; 100:93-106.
    • (1997) J Clin Invest , vol.100 , pp. 93-106
    • Lark, M.W.1    Bayne, E.K.2    Flanagan, J.3    Harper, C.F.4    Hoerner, L.A.5    Hutchinson, N.I.6
  • 32
    • 0026771893 scopus 로고
    • N-terminal sequence of proteoglycan fragments isolated from medium of interleukin-1-treated articular-cartilage cultures: Putative site(s) of enzymatic cleavage
    • 32. Loulakis P, Shrikhande A, Davis G, Maniglia. N-terminal sequence of proteoglycan fragments isolated from medium of interleukin-1-treated articular-cartilage cultures: putative site(s) of enzymatic cleavage. Biochem J 1992;284:589-93.
    • (1992) Biochem J , vol.284 , pp. 589-593
    • Loulakis, P.1    Shrikhande, A.2    Davis, G.3    Maniglia4
  • 33
    • 0025149044 scopus 로고
    • Effect of naproxen sodium on the net synthesis of glycosaminoglycans and protein by normal canine articular cartilage in vitro
    • 33. Brandt KD, Albrecht M. Effect of naproxen sodium on the net synthesis of glycosaminoglycans and protein by normal canine articular cartilage in vitro. J Pharm Pharmacol 1990;42: 738-40.
    • (1990) J Pharm Pharmacol , vol.42 , pp. 738-740
    • Brandt, K.D.1    Albrecht, M.2
  • 34
    • 0010384748 scopus 로고
    • The effects of the active metabolite of nabumetone (6MNA) on the synthesis of normal canine articular cartilage in vitro: Comparison with other non-steroidal anti-inflamatory drugs (NSAIDS)
    • 34. Gentry C. The effects of the active metabolite of nabumetone (6MNA) on the synthesis of normal canine articular cartilage in vitro: comparison with other non-steroidal anti-inflamatory drugs (NSAIDS). Br J Rheumatol 1992;31(Suppl. 2):168.
    • (1992) Br J Rheumatol , vol.31 , Issue.SUPPL. 2 , pp. 168
    • Gentry, C.1
  • 36
    • 0026596047 scopus 로고
    • Inhibition of interleukin 1 induced chondrocyte protease activity by a corticosteroid and a nonsteroidal anti-inflammatory drug
    • 36. Lane NE, Williams RJ III, Schurman DJ, Smith RL. Inhibition of interleukin 1 induced chondrocyte protease activity by a corticosteroid and a nonsteroidal anti-inflammatory drug. J Rheumatol 1992;19:135-9.
    • (1992) J Rheumatol , vol.19 , pp. 135-139
    • Lane, N.E.1    Williams R.J. III2    Schurman, D.J.3    Smith, R.L.4
  • 37
    • 0026037110 scopus 로고
    • The interactions of cytokines, NSAIDs and prostaglandins in cartilage destruction and repair
    • 37. Dingle JT, Shield MJ. The interactions of cytokines, NSAIDs and prostaglandins in cartilage destruction and repair. Adv Prostaglandin Thromboxane Leukot Res 1991;21B:955-66.
    • (1991) Adv Prostaglandin Thromboxane Leukot Res , vol.21 B , pp. 955-966
    • Dingle, J.T.1    Shield, M.J.2
  • 38
    • 0027250987 scopus 로고
    • Anti-inflammatory drugs and their effects on cartilage synthesis and renal function
    • 38. Shield MJ. Anti-inflammatory drugs and their effects on cartilage synthesis and renal function. Eur J Rheumatol Inflamm 1993;13:7-16.
    • (1993) Eur J Rheumatol Inflamm , vol.13 , pp. 7-16
    • Shield, M.J.1
  • 39
    • 0028657567 scopus 로고
    • Pharmacologic influence on the activity of stromelysin from bovine articular cartilage
    • 39. Steinmeyer J, Daufeldt S, Kalbhen DA. Pharmacologic influence on the activity of stromelysin from bovine articular cartilage. Ann NY Acad Sci 1994;732:482-3.
    • (1994) Ann NY Acad Sci , vol.732 , pp. 482-483
    • Steinmeyer, J.1    Daufeldt, S.2    Kalbhen, D.A.3
  • 40
    • 0027401754 scopus 로고
    • The effect of naproxen and interleukin-1 on proteoglycan catabolism and on neutral metalloproteinase activity in normal articular cartilage in vitro
    • 40. Glazer PA, Rosenwasser MP, Ratcliffe A. The effect of naproxen and interleukin-1 on proteoglycan catabolism and on neutral metalloproteinase activity in normal articular cartilage in vitro. J Clin Pharmacol 1993;33:109-14.
    • (1993) J Clin Pharmacol , vol.33 , pp. 109-114
    • Glazer, P.A.1    Rosenwasser, M.P.2    Ratcliffe, A.3
  • 41
    • 0027556626 scopus 로고
    • In vivo effects of naproxen on composition, proteoglycan metabolism, and matrix metalloproteinase activities in canine articular cartilage
    • 41. Ratcliffe A, Azzo W, Saed-Nejad F, Lane N, Rosenwasser MP, Mow VC. In vivo effects of naproxen on composition, proteoglycan metabolism, and matrix metalloproteinase activities in canine articular cartilage. J Orthop Res 1993;11:163-71.
    • (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
  • 42
    • 0029168059 scopus 로고
    • The levels of collagenase, tissue inhibitor of metalloproteinases-1 (TIMP-1), collagenase-TIMP-1 complexes and glycosaminoglycan (GAG) in sequential samples of synovial fluid aspirated from patients with osteoarthritis
    • 42. Cawston TE, Curry V, Ramsey S, Clark IM, Kyle VA, Adebajo A, Silverman B et al. The levels of collagenase, tissue inhibitor of metalloproteinases-1 (TIMP-1), collagenase-TIMP-1 complexes and glycosaminoglycan (GAG) in sequential samples of synovial fluid aspirated from patients with osteoarthritis. Clin Exp Rheumatol 1995;13:431-7.
    • (1995) Clin Exp Rheumatol , vol.13 , pp. 431-437
    • Cawston, T.E.1    Curry, V.2    Ramsey, S.3    Clark, I.M.4    Kyle, V.A.5    Adebajo, A.6    Silverman, B.7
  • 46
    • 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
    • 46. Fernandes JC, Caron JP, Martel-Pelletier J, Jovanovic D, Mineau F, Tardif G et al. Effects of tenidap on the progression of osteoarthritic lesions in a canine experimental model. Suppression of metalloprotease and interleukin-1 activity. Arthritis Rheum 1997;40:284-94.
    • (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
  • 47
    • 0028351976 scopus 로고
    • Effects of certain antiarthritic agents on the synthesis of type II collagen and glycosaminoglycans in rat chondrosarcoma cultures
    • 47. Srinivas GR, Chichester CO, Barrach HJ, Matoney AL. Effects of certain antiarthritic agents on the synthesis of type II collagen and glycosaminoglycans in rat chondrosarcoma cultures. Agents Actions 1994;41:193-9.
    • (1994) Agents Actions , vol.41 , pp. 193-199
    • Srinivas, G.R.1    Chichester, C.O.2    Barrach, H.J.3    Matoney, A.L.4
  • 48
    • 0025184963 scopus 로고
    • Tetracyclines, derivatives as potential inhibitors of connective tissue degradation
    • 48. Greenwald RA. Tetracyclines, derivatives as potential inhibitors of connective tissue degradation. Drug News & Perspect 1990;3:161-6.
    • (1990) Drug News & Perspect , vol.3 , pp. 161-166
    • Greenwald, R.A.1
  • 50
    • 0000552419 scopus 로고
    • Inhibition of neutral metalloproteinase activities in epiphyseal and articular cartilages by tetracyclines both in vivo and in vitro
    • 50. Arsenis C, Greenwald RA, Moak SA, Laskin RS. Inhibition of neutral metalloproteinase activities in epiphyseal and articular cartilages by tetracyclines both in vivo and in vitro. Trans Orthop Res Soc 1990;15:268.
    • (1990) Trans Orthop Res Soc , vol.15 , pp. 268
    • Arsenis, C.1    Greenwald, R.A.2    Moak, S.A.3    Laskin, R.S.4
  • 52
  • 53
    • 8044250278 scopus 로고    scopus 로고
    • Cloning of a disintegrin metalloproteinase that processes precursor tumour-necrosis factor-a
    • 53. Moss ML, Jin S-L C, Millia ME, Burkhart W, Carter HL, Chen W-J et al. Cloning of a disintegrin metalloproteinase that processes precursor tumour-necrosis factor-a. Nature 1997;385:733-6.
    • (1997) Nature , vol.385 , pp. 733-736
    • Moss, M.L.1    Jin, S.-L.C.2    Millia, M.E.3    Burkhart, W.4    Carter, H.L.5    Chen, W.-J.6


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