메뉴 건너뛰기




Volumn 11, Issue 9, 2003, Pages 625-635

The effects of TIMP-1 and -2 on canine chondrocytes cultured in three-dimensional agarose culture system

Author keywords

Chondrocytes; Interleukin 1 ; Osteoarthritis; Tissue inhibitor of metalloproteinases

Indexed keywords

AGAROSE; GLYCOSAMINOGLYCAN; INTERLEUKIN 1BETA; STROMELYSIN; TISSUE INHIBITOR OF METALLOPROTEINASE 1; TISSUE INHIBITOR OF METALLOPROTEINASE 2;

EID: 0041885332     PISSN: 10634584     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1063-4584(03)00116-X     Document Type: Article
Times cited : (20)

References (58)
  • 1
    • 0029766216 scopus 로고    scopus 로고
    • Metalloproteinase inhibitors and the prevention of connective tissue breakdown
    • Cawston TE. Metalloproteinase inhibitors and the prevention of connective tissue breakdown. Pharmacol Ther 1996;70:163-82.
    • (1996) Pharmacol. Ther. , vol.70 , pp. 163-182
    • Cawston, T.E.1
  • 4
    • 0026111656 scopus 로고
    • Role of metalloproteinases in human osteoarthritis
    • Woessner JF Jr, Gunja-Smith Z. Role of metalloproteinases in human osteoarthritis. J Rheumatol 1991; 27(Suppl):99-101.
    • (1991) J. Rheumatol. , vol.27 , Issue.SUPPL. , pp. 99-101
    • Woessner J.F., Jr.1    Gunja-Smith, Z.2
  • 6
    • 0025152013 scopus 로고
    • Imbalance between the mechanisms of activation and inhibition of metalloproteases in the early lesions of experimental osteoarthritis
    • Pelletier JP, Mineau F, Faure MP, Martel-Pelletier J. Imbalance between the mechanisms of activation and inhibition of metalloproteases in the early lesions of experimental osteoarthritis. Arthritis Rheum 1990; 33:1466-76.
    • (1990) Arthritis Rheum. , vol.33 , pp. 1466-1476
    • Pelletier, J.P.1    Mineau, F.2    Faure, M.P.3    Martel-Pelletier, J.4
  • 7
    • 0027997899 scopus 로고
    • Using inhibitors of metalloproteinases to treat arthritis. Easier said than done?
    • Vincenti MP, Clark IM, Brinckerhoff CE. Using inhibitors of metalloproteinases to treat arthritis. Easier said than done? Arthritis Rheum 1994;37:1115-26.
    • (1994) Arthritis Rheum. , vol.37 , pp. 1115-1126
    • Vincenti, M.P.1    Clark, I.M.2    Brinckerhoff, C.E.3
  • 8
    • 0031853221 scopus 로고    scopus 로고
    • Prevention of cartilage breakdown by matrix metalloproteinase inhibition-a realistic therapeutic target?
    • Cawston TE, Rowan A. Prevention of cartilage breakdown by matrix metalloproteinase inhibition-a realistic therapeutic target? Br J Rheumatol 1998; 37:353-6.
    • (1998) Br. J. Rheumatol. , vol.37 , pp. 353-356
    • Cawston, T.E.1    Rowan, A.2
  • 9
    • 0032515157 scopus 로고    scopus 로고
    • Differential expression of aggrecanase and matrix metalloproteinase activity in chondrocytes isolated from bovine and porcine articular cartilage
    • Hughes CE, Little CB, Buttner FH, Bartnik E, Caterson B. Differential expression of aggrecanase and matrix metalloproteinase activity in chondrocytes isolated from bovine and porcine articular cartilage. J Biol Chem 1998;273:30576-82.
    • (1998) J. Biol. Chem. , vol.273 , pp. 30576-30582
    • Hughes, C.E.1    Little, C.B.2    Buttner, F.H.3    Bartnik, E.4    Caterson, B.5
  • 10
    • 0021081088 scopus 로고
    • The effects of razoxane (ICRF 159) on the production of collagenase and inhibitor (TIMP) by stimulated rabbit articular chondrocytes
    • Duncan SJ, Reynolds JJ. The effects of razoxane (ICRF 159) on the production of collagenase and inhibitor (TIMP) by stimulated rabbit articular chondrocytes. Biochem Pharmacol 1983;32:3853-8.
    • (1983) Biochem. Pharmacol. , vol.32 , pp. 3853-3858
    • Duncan, S.J.1    Reynolds, J.J.2
  • 11
    • 0032983177 scopus 로고    scopus 로고
    • Esculetin (dihydroxycoumarin) inhibits the production of matrix metalloproteinases in cartilage explants, and oral administration of its pro-drug, CPA-926, suppresses cartilage destruction in rabbit experimental osteoarthritis
    • Yamada H, Watanabe K, Saito T, Hayashi H, Niitani Y, Kikuchi T, et al. Esculetin (dihydroxycoumarin) inhibits the production of matrix metalloproteinases in cartilage explants, and oral administration of its pro-drug, CPA-926, suppresses cartilage destruction in rabbit experimental osteoarthritis. J Rheumatol 1999; 26:654-62.
    • (1999) J. Rheumatol. , vol.26 , pp. 654-662
    • Yamada, H.1    Watanabe, K.2    Saito, T.3    Hayashi, H.4    Niitani, Y.5    Kikuchi, T.6
  • 12
    • 0031571627 scopus 로고    scopus 로고
    • Inhibition of cartilage degradation and changes in physical properties induced by IL-1β and retinoic acid using matrix metalloproteinase inhibitors
    • Bonassar LJ, Sandy JD, Lark MW, Plaas AH, Frank EH, Grodzinsky AJ. Inhibition of cartilage degradation and changes in physical properties induced by IL-1β and retinoic acid using matrix metalloproteinase inhibitors. Arch Biochem Biophys 1997; 344:404-12.
    • (1997) Arch. Biochem. Biophys. , vol.344 , pp. 404-412
    • Bonassar, L.J.1    Sandy, J.D.2    Lark, M.W.3    Plaas, A.H.4    Frank, E.H.5    Grodzinsky, A.J.6
  • 13
  • 15
    • 0028334568 scopus 로고
    • The prevention of collagen breakdown in bovine nasal cartilage by TIMP, TIMP-2 and a low molecular weight synthetic inhibitor
    • Ellis AJ, Curry VA, Powell EK, Cawston TE. The prevention of collagen breakdown in bovine nasal cartilage by TIMP, TIMP-2 and a low molecular weight synthetic inhibitor. Biochem Biophys Res Commun 1994;201:94-101.
    • (1994) Biochem. Biophys. Res. Commun. , vol.201 , pp. 94-101
    • Ellis, A.J.1    Curry, V.A.2    Powell, E.K.3    Cawston, T.E.4
  • 16
    • 0026643124 scopus 로고
    • Tetracyclines suppress matrix metalloproteinase activity in adjuvant arthritis and in combination with flurbiprofen, ameliorate bone damage
    • Greenwald RA, Moak SA, Ramamurthy NS, Golub LM. Tetracyclines suppress matrix metalloproteinase activity in adjuvant arthritis and in combination with flurbiprofen, ameliorate bone damage. J Rheumatol 1992;19:927-38.
    • (1992) J. Rheumatol. , vol.19 , pp. 927-938
    • Greenwald, R.A.1    Moak, S.A.2    Ramamurthy, N.S.3    Golub, L.M.4
  • 17
    • 0031114849 scopus 로고    scopus 로고
    • Three-dimensional culture of canine articular chondrocytes on multiple transplantable substrates
    • Cook JL, Kreeger JM, Payne JT, Tomlinson JL. Three-dimensional culture of canine articular chondrocytes on multiple transplantable substrates. Am J Vet Res 1997;58:419-24.
    • (1997) Am. J. Vet. Res. , vol.58 , pp. 419-424
    • Cook, J.L.1    Kreeger, J.M.2    Payne, J.T.3    Tomlinson, J.L.4
  • 18
    • 0032725863 scopus 로고    scopus 로고
    • In vitro effects of glucosamine and acetylsalicylate on canine chondrocytes in three-dimensional culture
    • Anderson CC, Cook JL, Kreeger JM, Tomlinson JL, Wagner-Mann CC. In vitro effects of glucosamine and acetylsalicylate on canine chondrocytes in three-dimensional culture. Am J Vet Res 1999;60:1546-51.
    • (1999) Am. J. Vet. Res. , vol.60 , pp. 1546-1551
    • Anderson, C.C.1    Cook, J.L.2    Kreeger, J.M.3    Tomlinson, J.L.4    Wagner-Mann, C.C.5
  • 19
    • 0034220509 scopus 로고    scopus 로고
    • Effects of human recombinant interleukin-1β on canine articular chondrocytes in three-dimensional culture
    • Cook JL, Anderson CC, Kreeger JM, Tomlinson JL. Effects of human recombinant interleukin-1β on canine articular chondrocytes in three-dimensional culture. Am J Vet Res 2000;61:766-70.
    • (2000) Am. J. Vet. Res. , vol.61 , pp. 766-770
    • Cook, J.L.1    Anderson, C.C.2    Kreeger, J.M.3    Tomlinson, J.L.4
  • 20
    • 0035377561 scopus 로고    scopus 로고
    • Biochemical characterization of cartilage affected by osteochondritis dissecans in the humeral head of dogs
    • Tomlinson JL, Cook JL, Kuroki K, Kreeger JM, Anderson MA. Biochemical characterization of cartilage affected by osteochondritis dissecans in the humeral head of dogs. Am J Vet Res 2001; 62:876-81.
    • (2001) Am. J. Vet. Res. , vol.62 , pp. 876-881
    • Tomlinson, J.L.1    Cook, J.L.2    Kuroki, K.3    Kreeger, J.M.4    Anderson, M.A.5
  • 21
    • 0036736192 scopus 로고    scopus 로고
    • Immunohistochemical analysis of matrix metalloproteinase-1, -3, and -13 in naturally occurring cartilaginous tumors of dogs
    • Kuroki K, Kreeger JM, Cook JL, Tomlinson JL, Johnson GC, Pace LW, et al. Immunohistochemical analysis of matrix metalloproteinase-1, -3, and -13 in naturally occurring cartilaginous tumors of dogs. Am J Vet Res 2002;63:1285-91.
    • (2002) Am. J. Vet. Res. , vol.63 , pp. 1285-1291
    • Kuroki, K.1    Kreeger, J.M.2    Cook, J.L.3    Tomlinson, J.L.4    Johnson, G.C.5    Pace, L.W.6
  • 22
    • 0031928795 scopus 로고    scopus 로고
    • Collagenase-1 and collagenase-3 synthesis in normal and early experimental osteoarthritic canine cartilage: An immunohistochemical study
    • Fernandes JC, Martel-Pelletier J, Lascau-Coman V, Moldovan F, Jovanovic D, Raynauld JP, et al. Collagenase-1 and collagenase-3 synthesis in normal and early experimental osteoarthritic canine cartilage: an immunohistochemical study. J Rheumatol 1998;25:1585-94.
    • (1998) J. Rheumatol. , vol.25 , pp. 1585-1594
    • Fernandes, J.C.1    Martel-Pelletier, J.2    Lascau-Coman, V.3    Moldovan, F.4    Jovanovic, D.5    Raynauld, J.P.6
  • 23
    • 0022552896 scopus 로고
    • Improved quantitation and discrimination of sulphated glycosaminoglycans by use of dimethylmethylene blue
    • Farndale RW, Buttle DJ, Barrett AJ. Improved quantitation and discrimination of sulphated glycosaminoglycans by use of dimethylmethylene blue. Biochim Biophys Acta 1986;883:173-7.
    • (1986) Biochim. Biophys. Acta , vol.883 , pp. 173-177
    • Farndale, R.W.1    Buttle, D.J.2    Barrett, A.J.3
  • 24
    • 0028322045 scopus 로고
    • Adaptation of the diphenylamine (DPA) assay to a 96-well plate tissue culture format and comparison with the MTT assay
    • Natarajan N, Shambaugh GE 3rd, Elseth KM, Haines GK, Radosevich JA. Adaptation of the diphenylamine (DPA) assay to a 96-well plate tissue culture format and comparison with the MTT assay. Biotechniques 1994;17:167-71.
    • (1994) Biotechniques , vol.17 , pp. 167-171
    • Natarajan, N.1    Shambaugh G.E. III2    Elseth, K.M.3    Haines, G.K.4    Radosevich, J.A.5
  • 25
    • 0029881336 scopus 로고    scopus 로고
    • A simplified method for the analysis of hydroxyproline in biological tissues
    • Reddy GK, Enwemeka CS. A simplified method for the analysis of hydroxyproline in biological tissues. Clin Biochem 1996;29:225-9.
    • (1996) Clin. Biochem. , vol.29 , pp. 225-229
    • Reddy, G.K.1    Enwemeka, C.S.2
  • 26
    • 0020369710 scopus 로고
    • Dedifferentiated chondrocytes reexpress the differentiated collagen phenotype when cultured in agarose gels
    • Benya PD, Shaffer JD. Dedifferentiated chondrocytes reexpress the differentiated collagen phenotype when cultured in agarose gels. Cell 1982;30:215-24.
    • (1982) Cell , vol.30 , pp. 215-224
    • Benya, P.D.1    Shaffer, J.D.2
  • 29
    • 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;267:1008-14.
    • (1992) J. Biol. Chem. , vol.267 , pp. 1008-1014
    • Flannery, C.R.1    Lark, M.W.2    Sandy, J.D.3
  • 31
    • 0025944065 scopus 로고
    • The N-terminal domain of tissue inhibitor of metalloproteinases retains metalloproteinases inhibitory activity
    • Murphy G, Houbrechts A, Cockett MI, Williamson RA, O'Shea M, Docherty AJ. The N-terminal domain of tissue inhibitor of metalloproteinases retains metalloproteinases inhibitory activity. Biochemistry 1991; 30:8097-102.
    • (1991) Biochemistry , vol.30 , pp. 8097-8102
    • Murphy, G.1    Houbrechts, A.2    Cockett, M.I.3    Williamson, R.A.4    O'Shea, M.5    Docherty, A.J.6
  • 34
    • 0023193096 scopus 로고
    • Interleukin-1 and osteoarthritis
    • Pujol JP, Loyau G. Interleukin-1 and osteoarthritis. Life Sci 1987;41:1187-98.
    • (1987) Life Sci. , vol.41 , pp. 1187-1198
    • Pujol, J.P.1    Loyau, G.2
  • 36
    • 0025277732 scopus 로고
    • The effects of interleukin-1 on articular cartilage destruction as observed in arthritic disease, and its therapeutic control
    • Verschure PJ, Van Noorden CJ. The effects of interleukin-1 on articular cartilage destruction as observed in arthritic disease, and its therapeutic control. Clin Exp Rheumatol 1990;8:303-13.
    • (1990) Clin. Exp. Rheumatol. , vol.8 , pp. 303-313
    • Verschure, P.J.1    Van Noorden, C.J.2
  • 37
    • 0032170457 scopus 로고    scopus 로고
    • Matrix degradation by chondrocytes cultured in alginate: IL-1 beta induces proteoglycan degradation and proMMP synthesis but does not result in collagen degradation
    • Beekman B, Verzijl N, de Roos JA, TeKoppele JM. Matrix degradation by chondrocytes cultured in alginate: IL-1 beta induces proteoglycan degradation and proMMP synthesis but does not result in collagen degradation. Osteoarthritis Cartilage 1998;6:330-40.
    • (1998) Osteoarthritis Cartilage , vol.6 , pp. 330-340
    • Beekman, B.1    Verzijl, N.2    de Roos, J.A.3    TeKoppele, J.M.4
  • 38
    • 0002493437 scopus 로고
    • Degradation of articular cartilage in culture: Regulatory factors
    • Woessner JF, Howell DS, Eds. New York: Marcel Dekker
    • Goldring MB. Degradation of articular cartilage in culture: regulatory factors. In: Woessner JF, Howell DS, Eds. Joint Cartilage Degradation: Basic and Clinical Aspects. New York: Marcel Dekker 1993;281-345.
    • (1993) Joint Cartilage Degradation: Basic and Clinical Aspects , pp. 281-345
    • Goldring, M.B.1
  • 39
    • 0028349374 scopus 로고
    • Transforming growth factor beta 1 regulates tissue inhibitor of metalloproteinases-1 expression in differentiated human articular chondrocytes
    • Gunther M, Haubeck HD, van de Leur E, Blaser J, Bender S, Gutgemann I, et al. Transforming growth factor beta 1 regulates tissue inhibitor of metalloproteinases-1 expression in differentiated human articular chondrocytes. Arthritis Rheum 1994; 37:395-405.
    • (1994) Arthritis Rheum. , vol.37 , pp. 395-405
    • Gunther, M.1    Haubeck, H.D.2    van de Leur, E.3    Blaser, J.4    Bender, S.5    Gutgemann, I.6
  • 40
    • 0036190642 scopus 로고    scopus 로고
    • Control of extracellular matrix homeostasis of normal cartilage by a TGFbeta autocrine pathway. Validation of flow cytometry as a tool to study chondrocyte metabolism in vitro
    • Wang L, Almqvist KF, Veys EM, Verbruggen G. Control of extracellular matrix homeostasis of normal cartilage by a TGFbeta autocrine pathway. Validation of flow cytometry as a tool to study chondrocyte metabolism in vitro. Osteoarthritis Cartilage 2002; 10:188-98.
    • (2002) Osteoarthritis Cartilage , vol.10 , pp. 188-198
    • Wang, L.1    Almqvist, K.F.2    Veys, E.M.3    Verbruggen, G.4
  • 41
    • 0031656460 scopus 로고    scopus 로고
    • Matrix metalloproteinases: Structures, evolution, and diversification
    • Massova I, Kotra LP, Fridman R, Mobashery S. Matrix metalloproteinases: structures, evolution, and diversification. FASEB J 1998;12:1075-95.
    • (1998) FASEB J. , vol.12 , pp. 1075-1095
    • Massova, I.1    Kotra, L.P.2    Fridman, R.3    Mobashery, S.4
  • 42
    • 0034615550 scopus 로고    scopus 로고
    • Tissue inhibitors of metalloproteinases: Evolution, structure and function
    • Brew K, Dinakarpandian D, Nagase H. Tissue inhibitors of metalloproteinases: evolution, structure and function. Biochim Biophys Acta 2000;1477:267-83.
    • (2000) Biochim. Biophys. Acta , vol.1477 , pp. 267-283
    • Brew, K.1    Dinakarpandian, D.2    Nagase, H.3
  • 45
    • 0034212469 scopus 로고    scopus 로고
    • Periosteally derived osteoblast-like cells differentiate into chondrocytes in suspension culture in agarose
    • Bahrami S, Stratmann U, Wiesmann HP, Mokrys K, Bruckner P, Szuwart T. Periosteally derived osteoblast-like cells differentiate into chondrocytes in suspension culture in agarose. Anat Rec 2000; 259:124-30.
    • (2000) Anat. Rec. , vol.259 , pp. 124-130
    • Bahrami, S.1    Stratmann, U.2    Wiesmann, H.P.3    Mokrys, K.4    Bruckner, P.5    Szuwart, T.6
  • 46
    • 0343048983 scopus 로고    scopus 로고
    • IL-1 beta protects human chondrocytes from CD95-induced apoptosis
    • Kuhn K, Hashimoto S, Lotz M. IL-1 beta protects human chondrocytes from CD95-induced apoptosis. J Immunol 2000;164:2233-9.
    • (2000) J. Immunol. , vol.164 , pp. 2233-2239
    • Kuhn, K.1    Hashimoto, S.2    Lotz, M.3
  • 47
    • 0029043151 scopus 로고
    • IL-1-induced nitric oxide inhibits chondrocyte proliferation via PGE2
    • Blanco FJ, Lotz M. IL-1-induced nitric oxide inhibits chondrocyte proliferation via PGE2. Exp Cell Res 1995;218:319-25.
    • (1995) Exp. Cell Res. , vol.218 , pp. 319-325
    • Blanco, F.J.1    Lotz, M.2
  • 48
    • 0033525533 scopus 로고    scopus 로고
    • Generation and characterization of aggrecanase. A soluble, cartilage-derived aggrecandegrading activity
    • Arner EC, Pratta MA, Trzaskos JM, Decicco CP, Tortorella MD. Generation and characterization of aggrecanase. A soluble, cartilage-derived aggrecandegrading activity. J Biol Chem 1999;274:6594-601.
    • (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
  • 49
    • 1842365544 scopus 로고    scopus 로고
    • Degradation of type II collagen, but not proteoglycan, correlates with matrix metalloproteinase activity in cartilage explant cultures
    • Kozaci LD, Buttle DJ, Hollander AP. Degradation of type II collagen, but not proteoglycan, correlates with matrix metalloproteinase activity in cartilage explant cultures. Arthritis Rheum 1997;40:164-74.
    • (1997) Arthritis Rheum. , vol.40 , pp. 164-174
    • Kozaci, L.D.1    Buttle, D.J.2    Hollander, A.P.3
  • 51
    • 0345211445 scopus 로고    scopus 로고
    • Purification and cloning of aggrecanase-1: A member of the ADAMTS family of proteins
    • Tortorella MD, Burn TC, Pratta MA, Abbaszade I, Hollis JM, Liu R, et al. Purification and cloning of aggrecanase-1: a member of the ADAMTS family of proteins. Science 1999;284:1664-6.
    • (1999) Science , vol.284 , pp. 1664-1666
    • Tortorella, M.D.1    Burn, T.C.2    Pratta, M.A.3    Abbaszade, I.4    Hollis, J.M.5    Liu, R.6
  • 52
    • 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, Amer E. The role of ADAM-TS4 (aggrecanase-1) and ADAM-TS5 (aggrecanase-2) in a model of cartilage degradation. Osteoarthritis Cartilage 2001;9:539-52.
    • (2001) Osteoarthritis Cartilage , vol.9 , pp. 539-552
    • Tortorella, M.D.1    Malfait, A.M.2    Deccico, C.3    Amer, E.4
  • 54
    • 0037151084 scopus 로고    scopus 로고
    • Inhibition of ADAM-TS4 and ADAM-TS5 prevents aggrecan degradation in osteoarthritic cartilage
    • Malfait AM, Liu RQ, Ijiri K, Komiya S, Tortorella MD. Inhibition of ADAM-TS4 and ADAM-TS5 prevents aggrecan degradation in osteoarthritic cartilage. J Biol Chem 2002;277:22,201-8.
    • (2002) J. Biol. Chem. , vol.277
    • Malfait, A.M.1    Liu, R.Q.2    Ijiri, K.3    Komiya, S.4    Tortorella, M.D.5
  • 55
    • 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; 276:12501-4.
    • (2001) J. Biol. Chem. , vol.276 , pp. 12501-12504
    • Kashiwagi, M.1    Tortorella, M.2    Nagase, H.3    Brew, K.4
  • 56
    • 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;494:192-5.
    • (2001) FEBS Lett. , vol.494 , pp. 192-195
    • Hashimoto, G.1    Aoki, T.2    Nakamura, H.3    Tanzawa, K.4    Okada, Y.5
  • 57
    • 0035676661 scopus 로고    scopus 로고
    • Adenovirus-based over-expression of tissue inhibitor of metalloproteinase 1 reduces tissue damage in the joints of tumor necrosis factor α transgenic mice
    • Schett G, Hayer S, Tohidast-Akrad M, Schmid BJ, Lang S, Turk B, et al. Adenovirus-based over-expression of tissue inhibitor of metalloproteinase 1 reduces tissue damage in the joints of tumor necrosis factor α transgenic mice. Arthritis Rheum 2001; 44:2888-98.
    • (2001) Arthritis Rheum. , vol.44 , pp. 2888-2898
    • Schett, G.1    Hayer, S.2    Tohidast-Akrad, M.3    Schmid, B.J.4    Lang, S.5    Turk, B.6
  • 58
    • 0034975580 scopus 로고    scopus 로고
    • Paradoxical effects of tissue inhibitor of metalloproteinases 1 gene transfer in collagen-induced arthritis
    • Apparailly F, Noel D, Millet V, Baker AH, Lisignoli G, Jacquet C, et al. Paradoxical effects of tissue inhibitor of metalloproteinases 1 gene transfer in collagen-induced arthritis. Arthritis Rheum 2001;44:1444-54.
    • (2001) Arthritis Rheum. , vol.44 , pp. 1444-1454
    • Apparailly, F.1    Noel, D.2    Millet, V.3    Baker, A.H.4    Lisignoli, G.5    Jacquet, C.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.