메뉴 건너뛰기




Volumn 18, Issue 3, 1999, Pages 225-237

Effects of culture conditions and exposure to catabolic stimulators (IL-1 and retinoic acid) on the expression of matrix metalloproteinases (MMPs) and disintegrin metalloproteinases (ADAMs) by articular cartilage chondrocytes

Author keywords

ADAM (A Disintegrin And Metalloproteinase); Cartilage; Chondrocyte; Matrix metalloproteinase

Indexed keywords

DISINTEGRIN; INTERLEUKIN 1; MATRIX METALLOPROTEINASE; MESSENGER RNA; RETINOIC ACID; STROMELYSIN;

EID: 0032766969     PISSN: 0945053X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0945-053X(99)00024-4     Document Type: Article
Times cited : (104)

References (53)
  • 1
    • 0026737382 scopus 로고
    • A synthetic peptide metalloproteinase inhibitor, but not TIMP, prevents the breakdown of proteoglycan within articular cartilage in vitro
    • Andrews H.J., Plumpton T.A., Harper G.P., Cawston T.E. A synthetic peptide metalloproteinase inhibitor, but not TIMP, prevents the breakdown of proteoglycan within articular cartilage in vitro. Agents Actions. 37:1992;147-154.
    • (1992) Agents Actions , vol.37 , pp. 147-154
    • Andrews, H.J.1    Plumpton, T.A.2    Harper, G.P.3    Cawston, T.E.4
  • 2
    • 0028273238 scopus 로고
    • Inhibition of the chondrocyte phenotype by retinoic acid involves upregulation of metalloprotease genes independent of TGF-beta
    • Ballock R.T., Heydemann A., Wakefield L.M., Flanders K.C., Roberts A.B., Sporn M.B. Inhibition of the chondrocyte phenotype by retinoic acid involves upregulation of metalloprotease genes independent of TGF-beta. J. Cell. Physiol. 159:1994;340-346.
    • (1994) J. Cell. Physiol. , vol.159 , pp. 340-346
    • Ballock, R.T.1    Heydemann, A.2    Wakefield, L.M.3    Flanders, K.C.4    Roberts, A.B.5    Sporn, M.B.6
  • 3
    • 8044257704 scopus 로고    scopus 로고
    • A metalloproteinase disintegrin that releases tumor-necrosis factor-alpha from cells
    • Black R.A., Rauch C.T., Kozlosky C.J. et al. A metalloproteinase disintegrin that releases tumor-necrosis factor-alpha from cells. Nature. 385:1997;729-733.
    • (1997) Nature , vol.385 , pp. 729-733
    • Black, R.A.1    Rauch, C.T.2    Kozlosky, C.J.3
  • 4
    • 0030834283 scopus 로고    scopus 로고
    • Metalloprotease-Disintegrins: Links to cell adhesion and cleavage of TNF-alpha and notch
    • Blobel C.P. Metalloprotease-Disintegrins: links to cell adhesion and cleavage of TNF-alpha and notch. Cell. 90:1997;589-592.
    • (1997) Cell , vol.90 , pp. 589-592
    • Blobel, C.P.1
  • 5
    • 0027515396 scopus 로고
    • Astacins, serralysins, snake venom and matrix metalloproteinases exhibit identical zinc-binding environments (HEXXHXXGXXH and Met-turn) and topologies and should be grouped into a common family, the 'metzincins
    • Bode W., Gomis-Rüth F.X., Stocker W. Astacins, serralysins, snake venom and matrix metalloproteinases exhibit identical zinc-binding environments (HEXXHXXGXXH and Met-turn) and topologies and should be grouped into a common family, the 'metzincins. FEBS Lett. 331:1993;131-140.
    • (1993) FEBS Lett. , vol.331 , pp. 131-140
    • Bode, W.1    Gomis-Rüth, F.X.2    Stocker, W.3
  • 6
    • 0029833035 scopus 로고    scopus 로고
    • Cytokine control of interstitial collagenase and collagenase-3 gene expression in human chondrocytes
    • Borden P., Solymar D., Sucharczuk A., Lindman B., Cannon P., Heller R.A. Cytokine control of interstitial collagenase and collagenase-3 gene expression in human chondrocytes. J. Biol. Chem. 271:1996;23577-23581.
    • (1996) J. Biol. Chem. , vol.271 , pp. 23577-23581
    • Borden, P.1    Solymar, D.2    Sucharczuk, A.3    Lindman, B.4    Cannon, P.5    Heller, R.A.6
  • 7
    • 0027438713 scopus 로고
    • Inhibition of cartilage proteoglycan release by a specific inactivator of cathepsin B and an inhibitor of matrix metalloproteinases. Evidence for two converging pathways of chondrocyte-mediated proteoglycan degradation
    • Buttle D.J., Handley C.J., Ilic M.Z., Saklatvala J., Murata M., Barrett A.J. Inhibition of cartilage proteoglycan release by a specific inactivator of cathepsin B and an inhibitor of matrix metalloproteinases. Evidence for two converging pathways of chondrocyte-mediated proteoglycan degradation. Arthritis Rhem. 36:1993;1709-1717.
    • (1993) Arthritis Rhem. , 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
  • 8
    • 0032127129 scopus 로고    scopus 로고
    • Membrane type 1 matrix metalloproteinase (MT1-MMP) cleaves the recombinant aggrecan substrate rAgg1mut at the 'aggrecanase' and MMP sites
    • Büttner F.H., Hughes C.E., Margerie D. et al. Membrane type 1 matrix metalloproteinase (MT1-MMP) cleaves the recombinant aggrecan substrate rAgg1mut at the 'aggrecanase' and MMP sites. Biochem. J. 333:1998;159-165.
    • (1998) Biochem. J. , vol.333 , pp. 159-165
    • Büttner, F.H.1    Hughes, C.E.2    Margerie, D.3
  • 9
    • 0344294155 scopus 로고    scopus 로고
    • Identification of a protein motif common to haemopexins, hyaluronidase, vitronectin, some matrix metalloproteinases, and all hyaluronic acid-binding proteoglycans
    • Caterson B., Hughes C.E., Flannery C.R., Cole A.A., Hambor J.E., Neame P.J. Identification of a protein motif common to haemopexins, hyaluronidase, vitronectin, some matrix metalloproteinases, and all hyaluronic acid-binding proteoglycans. Trans. Orthop. Res. Soc. 21:1996;172.
    • (1996) Trans. Orthop. Res. Soc. , vol.21 , pp. 172
    • Caterson, B.1    Hughes, C.E.2    Flannery, C.R.3    Cole, A.A.4    Hambor, J.E.5    Neame, P.J.6
  • 11
    • 0028919856 scopus 로고
    • A metalloprotease inhibitor blocks shedding of the 80-kD TNF receptor and TNF processing in T lymphocytes
    • Crowe P.D., Walter B.N., Mohler K.M., Otten-Evans C., Black R.A., Ware C.F. A metalloprotease inhibitor blocks shedding of the 80-kD TNF receptor and TNF processing in T lymphocytes. J. Exp. Med. 181:1995;1205-1210.
    • (1995) J. Exp. Med. , vol.181 , pp. 1205-1210
    • Crowe, P.D.1    Walter, B.N.2    Mohler, K.M.3    Otten-Evans, C.4    Black, R.A.5    Ware, C.F.6
  • 12
    • 0025976188 scopus 로고
    • Complete coding sequence and deduced primary structure of the human cartilage large aggregating proteoglycan, aggrecan. Human-specific repeats, and additional alternatively spliced forms
    • Doege K.J., Sasaki M., Kimura T., Yamada Y. Complete coding sequence and deduced primary structure of the human cartilage large aggregating proteoglycan, aggrecan. Human-specific repeats, and additional alternatively spliced forms. J. Biol. Chem. 266:1991;894-902.
    • (1991) J. Biol. Chem. , vol.266 , pp. 894-902
    • Doege, K.J.1    Sasaki, M.2    Kimura, T.3    Yamada, Y.4
  • 13
    • 0028334568 scopus 로고
    • The prevention of collagen breakdown in bovine nasal cartilage by TIMP, TIMP-2 and a low molecular weight synthetic inhibitor
    • Ellis A.J., Curry V.A., Powell E.K., Cawston T.E. The prevention of collagen breakdown in bovine nasal cartilage by TIMP, TIMP-2 and a low molecular weight synthetic inhibitor. Biochem. Biophys. Res. Comm. 201:1994;94-101.
    • (1994) Biochem. Biophys. Res. Comm. , vol.201 , pp. 94-101
    • Ellis, A.J.1    Curry, V.A.2    Powell, E.K.3    Cawston, T.E.4
  • 14
    • 0026504563 scopus 로고
    • Identification of a stromelysin cleavage site within the interglobular domain of human aggrecan. Evidence for proteolysis at the site in vivo in human articular cartilage
    • Flannery C.R., Lark M.W., Sandy J.D. Identification of a stromelysin cleavage site within the interglobular domain of human aggrecan. Evidence for proteolysis at the site in vivo in human articular cartilage. J. Biol. Chem. 267:1992;1008-1014.
    • (1992) J. Biol. Chem. , vol.267 , pp. 1008-1014
    • Flannery, C.R.1    Lark, M.W.2    Sandy, J.D.3
  • 15
    • 0031911950 scopus 로고    scopus 로고
    • Molecular cloning and sequence analysis of the aggrecan interglobular domain from porcine, equine, bovine and ovine cartilage: Comparison of proteinase-susceptible regions and sites of keratan sulfate substitution
    • Flannery C.R., Little C.B., Caterson B. Molecular cloning and sequence analysis of the aggrecan interglobular domain from porcine, equine, bovine and ovine cartilage: comparison of proteinase-susceptible regions and sites of keratan sulfate substitution. Matrix Biol. 16:1998;507-511.
    • (1998) Matrix Biol. , vol.16 , pp. 507-511
    • Flannery, C.R.1    Little, C.B.2    Caterson, B.3
  • 16
    • 0028322352 scopus 로고
    • Molecular cloning and expression of collagenase-3, a novel human matrix metalloproteinase produced by breast carcinoma
    • Frieje J.M.P., Diez-Itza I., Balbin M. Molecular cloning and expression of collagenase-3, a novel human matrix metalloproteinase produced by breast carcinoma. J. Biol. Chem. 269:1994;16766-16773.
    • (1994) J. Biol. Chem. , vol.269 , pp. 16766-16773
    • Frieje, J.M.P.1    Diez-Itza, I.2    Balbin, M.3
  • 17
    • 0342502272 scopus 로고    scopus 로고
    • The C-terminal (haemopexin-like) domain structure of human gelatinase A (MMP2): Structural implications for its function
    • Gohlke U., Gomis-Rüth F.X., Crabbe T., Murphy G., Docherty A.J.P., Bode W. The C-terminal (haemopexin-like) domain structure of human gelatinase A (MMP2): structural implications for its function. FEBS Lett. 378:1996;126-130.
    • (1996) FEBS Lett. , vol.378 , pp. 126-130
    • Gohlke, U.1    Gomis-Rüth, F.X.2    Crabbe, T.3    Murphy, G.4    Docherty, A.J.P.5    Bode, W.6
  • 18
    • 0040051981 scopus 로고    scopus 로고
    • The helping hand of collagenase-3 (MMP-13): 2.7 angstrom crystal structure of its C-terminal haemopexin-like domain
    • Gomis-Rüth F.X., Gohlke U., Betz M. The helping hand of collagenase-3 (MMP-13): 2.7 angstrom crystal structure of its C-terminal haemopexin-like domain. J. Mol. Biol. 264:1996;556-566.
    • (1996) J. Mol. Biol. , vol.264 , pp. 556-566
    • Gomis-Rüth, F.X.1    Gohlke, U.2    Betz, M.3
  • 19
    • 0031025031 scopus 로고    scopus 로고
    • Expression of a disintegrin-like protein in cultured human vascular cells and in vivo
    • Herren B., Raines E.W., Ross R. Expression of a disintegrin-like protein in cultured human vascular cells and in vivo. FASEB J. 11:1997;173-180.
    • (1997) FASEB J. , vol.11 , pp. 173-180
    • Herren, B.1    Raines, E.W.2    Ross, R.3
  • 20
    • 0027941838 scopus 로고
    • Families of zinc metalloproteases
    • Hooper N.M. Families of zinc metalloproteases. FEBS Lett. 354:1994;1-6.
    • (1994) FEBS Lett. , vol.354 , pp. 1-6
    • Hooper, N.M.1
  • 22
    • 0029995478 scopus 로고    scopus 로고
    • Molecular cloning of MADM: A catalytically active mammalian disintegrin-metalloprotease expressed in various cell types
    • Howard L., Lu X., Mitchell S., Griffiths S., Glynn P. Molecular cloning of MADM: a catalytically active mammalian disintegrin-metalloprotease expressed in various cell types. Biochem. J. 317:1996;45-50.
    • (1996) Biochem. J. , vol.317 , pp. 45-50
    • Howard, L.1    Lu, X.2    Mitchell, S.3    Griffiths, S.4    Glynn, P.5
  • 23
    • 1842406549 scopus 로고    scopus 로고
    • Utilization of a recombinant substrate rAgg1 to study the biochemical properties of aggrecanase in cell culture systems
    • Hughes C.E., Büttner F.H., Eidenmüller B., Caterson B., Bartnik E. Utilization of a recombinant substrate rAgg1 to study the biochemical properties of aggrecanase in cell culture systems. J. Biol. Chem. 272:1997;20269-20274.
    • (1997) J. Biol. Chem. , vol.272 , pp. 20269-20274
    • Hughes, C.E.1    Büttner, F.H.2    Eidenmüller, B.3    Caterson, B.4    Bartnik, E.5
  • 24
    • 0032515157 scopus 로고    scopus 로고
    • Differential expression of aggrecanase and matrix metalloproteinase activity in chondrocytes isolated from bovine and porcine articular cartilage
    • Hughes C.E., Little C.B., Büttner F.H., Bartnik E., Caterson B. Differential expression of aggrecanase and matrix metalloproteinase activity in chondrocytes isolated from bovine and porcine articular cartilage. J. Biol. Chem. 273:1998;30576-30582.
    • (1998) J. Biol. Chem. , vol.273 , pp. 30576-30582
    • Hughes, C.E.1    Little, C.B.2    Büttner, F.H.3    Bartnik, E.4    Caterson, B.5
  • 26
    • 0029670028 scopus 로고    scopus 로고
    • Metargidin, a membrane-anchored metalloprotease-disintegrin protein with an RGD integrin binding sequence
    • Kratzschmar J., Lum L., Blobel C.P. Metargidin, a membrane-anchored metalloprotease-disintegrin protein with an RGD integrin binding sequence. J. Biol. Chem. 271:1996;4593-4596.
    • (1996) J. Biol. Chem. , vol.271 , pp. 4593-4596
    • Kratzschmar, J.1    Lum, L.2    Blobel, C.P.3
  • 27
    • 0029644935 scopus 로고
    • Structure of full-length porcine synovial collagenase reveals a C-terminal domain containing a calcium-linked four bladed beta-propeller
    • Li J., Brick P., O'Hare M.C. et al. Structure of full-length porcine synovial collagenase reveals a C-terminal domain containing a calcium-linked four bladed beta-propeller. Structure. 3:1995;541-549.
    • (1995) Structure , vol.3 , pp. 541-549
    • Li, J.1    Brick, P.2    O'Hare, M.C.3
  • 28
    • 0026409292 scopus 로고
    • Markers of cartilage matrix metabolism in arthrosis. A review
    • Lohmander L.S. Markers of cartilage matrix metabolism in arthrosis. A review. Acta Orthop. Scand. 62:1991;623-632.
    • (1991) Acta Orthop. Scand. , vol.62 , pp. 623-632
    • Lohmander, L.S.1
  • 29
    • 0026771893 scopus 로고
    • N-terminal sequence of proteoglycan fragments isolated from medium of interleukin-1 treated articular cartilage explant cultures
    • Loulakis P., Shrikhande A., Davis G., Maniglia C.A. N-terminal sequence of proteoglycan fragments isolated from medium of interleukin-1 treated articular cartilage explant cultures. Biochem. J. 284:1992;589-593.
    • (1992) Biochem. J. , vol.284 , pp. 589-593
    • Loulakis, P.1    Shrikhande, A.2    Davis, G.3    Maniglia, C.A.4
  • 31
    • 0031566190 scopus 로고    scopus 로고
    • Expression of members of a novel membrane linked metalloproteinase family (ADAM) in human articular chondrocytes
    • McKie N., Edwards T., Dallas D.J. et al. Expression of members of a novel membrane linked metalloproteinase family (ADAM) in human articular chondrocytes. Biochem. Biophys. Res. Comm. 230:1997;335-339\\.
    • (1997) Biochem. Biophys. Res. Comm. , vol.230 , pp. 335-339
    • McKie, N.1    Edwards, T.2    Dallas, D.J.3
  • 32
    • 0032540170 scopus 로고    scopus 로고
    • The metallo-disintegrin ADAM10 (MADM) from bovine kidney has type IV collagenase activity in vitro
    • Millichip M.I., Dallas D.J., Wu E., Dale S., McKie N. The metallo-disintegrin ADAM10 (MADM) from bovine kidney has type IV collagenase activity in vitro. Biochem. Biophys. Res. Comm. 245:1998;594-598.
    • (1998) Biochem. Biophys. Res. Comm. , vol.245 , pp. 594-598
    • Millichip, M.I.1    Dallas, D.J.2    Wu, E.3    Dale, S.4    McKie, N.5
  • 33
    • 0030032444 scopus 로고    scopus 로고
    • Cloning, expression and type II collagenolytic activity of matrix metalloproteinase-13 from human osteoarthritic cartilage
    • Mitchell P.G., Magna H.A., Reeves L.M. et al. Cloning, expression and type II collagenolytic activity of matrix metalloproteinase-13 from human osteoarthritic cartilage. J. Clin. Invest. 97:1996;761-768.
    • (1996) J. Clin. Invest. , vol.97 , pp. 761-768
    • Mitchell, P.G.1    Magna, H.A.2    Reeves, L.M.3
  • 34
    • 0027417543 scopus 로고
    • Direct evidence for active metalloproteinases mediating matrix degradation in interleukin 1-stimulated human articular cartilage
    • Mort J.S., Dodge G.R., Roughley P.J. et al. Direct evidence for active metalloproteinases mediating matrix degradation in interleukin 1-stimulated human articular cartilage. Matrix. 13:1993;95-102.
    • (1993) Matrix , vol.13 , pp. 95-102
    • Mort, J.S.1    Dodge, G.R.2    Roughley, P.J.3
  • 35
    • 8044250278 scopus 로고    scopus 로고
    • Cloning of a disintegrin metalloproteinase that processes precursor tumour-necrosis factor-alpha
    • Moss M.L., Jin S.-L.C., Milla M.E. et al. Cloning of a disintegrin metalloproteinase that processes precursor tumour-necrosis factor-alpha. Nature. 385:1997;733-736.
    • (1997) Nature , vol.385 , pp. 733-736
    • Moss, M.L.1    Jin, S.-L.C.2    Milla, M.E.3
  • 36
    • 0030866507 scopus 로고    scopus 로고
    • Polymerase chain reaction selects a novel disintegrin proteinase from CD40-activated germinal center dendritic cells
    • Mueller C.G.F., Rissoan M.-C., Salinas B. et al. Polymerase chain reaction selects a novel disintegrin proteinase from CD40-activated germinal center dendritic cells. J. Exp. Med. 186:1997;655-663.
    • (1997) J. Exp. Med. , vol.186 , pp. 655-663
    • Mueller, C.G.F.1    Rissoan, M.-C.2    Salinas, B.3
  • 37
    • 0028799113 scopus 로고
    • A metalloprotease inhibitor blocks shedding of the IL-6 receptor and the p60 TNF receptor
    • Mullberg J., Durie F.H., Otten-Evans C. et al. A metalloprotease inhibitor blocks shedding of the IL-6 receptor and the p60 TNF receptor. J. Immunol. 155:1995;5198-5205.
    • (1995) J. Immunol. , vol.155 , pp. 5198-5205
    • Mullberg, J.1    Durie, F.H.2    Otten-Evans, C.3
  • 38
    • 0026708439 scopus 로고
    • Preferential mRNA expression of prostromelysin relative to procollagenase and in situ localization in human articular cartilage
    • Nguyen Q., Mort J.S., Roughley P.J. Preferential mRNA expression of prostromelysin relative to procollagenase and in situ localization in human articular cartilage. J. Clin. Invest. 89:1992;1189-1197.
    • (1992) J. Clin. Invest. , vol.89 , pp. 1189-1197
    • Nguyen, Q.1    Mort, J.S.2    Roughley, P.J.3
  • 39
    • 0032080801 scopus 로고    scopus 로고
    • TNF-alpha convertase enzyme from human arthritis-affected cartilage: Isolation of cDNA by differential display, expression of the active enzyme, and regulation of TNF-alpha
    • Patel I.R., Attur M.G., Patel R.N. et al. TNF-alpha convertase enzyme from human arthritis-affected cartilage: isolation of cDNA by differential display, expression of the active enzyme, and regulation of TNF-alpha. J. Immunol. 160:1998;4570-4579.
    • (1998) J. Immunol. , vol.160 , pp. 4570-4579
    • Patel, I.R.1    Attur, M.G.2    Patel, R.N.3
  • 40
    • 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., Pelletier J.-P., Tardif G., Cloutier J.-M., Martel-Pelletier J. The new collagenase, collagenase-3, is expressed and synthesized by human chondrocytes but not by synoviocytes. A role in osteoarthritis. J. Clin. Invest. 97:1996;2011-2019.
    • (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
  • 41
    • 0030976489 scopus 로고    scopus 로고
    • Rapid isolation of total RNA from small samples of hypocellular, dense connective tissues
    • Reno C., Marchuk L., Sciore P., Frank C.B., Hart D.A. Rapid isolation of total RNA from small samples of hypocellular, dense connective tissues. BioTechniques. 22:1997;1082-1086.
    • (1997) BioTechniques , vol.22 , pp. 1082-1086
    • Reno, C.1    Marchuk, L.2    Sciore, P.3    Frank, C.B.4    Hart, D.A.5
  • 42
    • 0031568919 scopus 로고    scopus 로고
    • Product differentiation by analysis of DNA melting curves during the polymerase chain reaction
    • Ririe K.M., Rasmussen R.P., Wittwer C.T. Product differentiation by analysis of DNA melting curves during the polymerase chain reaction. Anal. Biochem. 245:1997;154-160.
    • (1997) Anal. Biochem. , vol.245 , pp. 154-160
    • Ririe, K.M.1    Rasmussen, R.P.2    Wittwer, C.T.3
  • 43
    • 0025776382 scopus 로고
    • Catabolism of aggrecan in cartilage explants. Identification of a major cleavage site within the interglobular domain
    • Sandy J.D., Neame P.J., Boynton R.E., Flannery C.R. Catabolism of aggrecan in cartilage explants. Identification of a major cleavage site within the interglobular domain. J. Biol. Chem. 266:1991;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
  • 44
    • 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 J.D., Flannery C.R., Neame P.J., Lohmander L.S. 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. 89:1992;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
  • 45
    • 0027448327 scopus 로고
    • Inhibition of interleukin 1beta induced rat and human cartilage degradation in vitro by the metalloproteinase inhibitor U27391
    • Seed M.P., Ismaiel S., Cheung C.Y. et al. Inhibition of interleukin 1beta induced rat and human cartilage degradation in vitro by the metalloproteinase inhibitor U27391. Ann. Rheum. Dis. 52:1993;37-43.
    • (1993) Ann. Rheum. Dis. , vol.52 , pp. 37-43
    • Seed, M.P.1    Ismaiel, S.2    Cheung, C.Y.3
  • 46
    • 0023608017 scopus 로고
    • Enhanced expression of a glyceraldehyde-3-phosphate dehydrogenase gene in human lung cancers
    • Tokunaga K., Nakamura Y., Sakata K. et al. Enhanced expression of a glyceraldehyde-3-phosphate dehydrogenase gene in human lung cancers. Cancer Res. 47:1987;5616-5619.
    • (1987) Cancer Res. , vol.47 , pp. 5616-5619
    • Tokunaga, K.1    Nakamura, Y.2    Sakata, K.3
  • 47
    • 0032489516 scopus 로고    scopus 로고
    • The interglobular domain of cartilage aggrecan is cleaved by hemorrhagic metalloproteinase HT-d (atrolysin C) at the matrix metalloproteinase and aggrecanase sites
    • Tortorella M.D., Pratta M.A., Fox J.W., Arner E.C. The interglobular domain of cartilage aggrecan is cleaved by hemorrhagic metalloproteinase HT-d (atrolysin C) at the matrix metalloproteinase and aggrecanase sites. J. Biol. Chem. 273:1998;5846-5850.
    • (1998) J. Biol. Chem. , vol.273 , pp. 5846-5850
    • Tortorella, M.D.1    Pratta, M.A.2    Fox, J.W.3    Arner, E.C.4
  • 48
    • 0030049705 scopus 로고    scopus 로고
    • MDC9, a widely expressed cellular disintegrin containing cytoplasmic SH3 ligand domains
    • Weskamp G., Kratzschmar J., Reid M.S., Blobel C.P. MDC9, a widely expressed cellular disintegrin containing cytoplasmic SH3 ligand domains. J. Cell Biol. 132:1996;717-726.
    • (1996) J. Cell Biol. , vol.132 , pp. 717-726
    • Weskamp, G.1    Kratzschmar, J.2    Reid, M.S.3    Blobel, C.P.4
  • 49
    • 0022917253 scopus 로고
    • Comparison of human stromelysin and collagenase by cloning and sequence analysis
    • Whitham S.E., Murphy G., Angel P. et al. Comparison of human stromelysin and collagenase by cloning and sequence analysis. Biochem. J. 240:1986;913-916.
    • (1986) Biochem. J. , vol.240 , pp. 913-916
    • Whitham, S.E.1    Murphy, G.2    Angel, P.3
  • 50
    • 0029891449 scopus 로고    scopus 로고
    • Paradoxical effects of a synthetic metalloproteinase inhibitor that blocks both P55 and P75 TNF receptor shedding and TNF- alpha processing in RA synovial membrane cell cultures
    • Williams L.M., Gibbons D.L., Gearing A., Maini R.N., Feldmann M., Brennan F.M. Paradoxical effects of a synthetic metalloproteinase inhibitor that blocks both P55 and P75 TNF receptor shedding and TNF- alpha processing in RA synovial membrane cell cultures. J. Clin. Invest. 97:1996;2833-2841.
    • (1996) J. Clin. Invest. , vol.97 , pp. 2833-2841
    • Williams, L.M.1    Gibbons, D.L.2    Gearing, A.3    Maini, R.N.4    Feldmann, M.5    Brennan, F.M.6
  • 52
    • 0028820623 scopus 로고
    • ADAM, a novel family of membrane proteins containing a disintegrin and metalloprotease domain: Multipotential functions in cell-cell and cell-matrix interactions
    • Wolfsberg T.G., Primakoff P., Myles D.G., White J.M. ADAM, a novel family of membrane proteins containing a disintegrin and metalloprotease domain: multipotential functions in cell-cell and cell-matrix interactions. J. Cell Biol. 131:1995;275-278.
    • (1995) J. Cell Biol. , vol.131 , pp. 275-278
    • Wolfsberg, T.G.1    Primakoff, P.2    Myles, D.G.3    White, J.M.4
  • 53
    • 0029045064 scopus 로고
    • ADAM, a widely distributed and developmentally regulated gene family encoding membrane proteins with a disintegrin and metalloprotease domain
    • Wolfsberg T.G., Straight P.D., Gerena R.L. ADAM, a widely distributed and developmentally regulated gene family encoding membrane proteins with a disintegrin and metalloprotease domain. Dev. Biol. 169:1995;378-383.
    • (1995) Dev. Biol. , vol.169 , pp. 378-383
    • Wolfsberg, T.G.1    Straight, P.D.2    Gerena, R.L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.