메뉴 건너뛰기




Volumn 62, Issue SUPPL. 2, 2003, Pages 43-47

Metalloproteinases, inflammation, and rheumatoid arthritis

Author keywords

[No Author keywords available]

Indexed keywords

AGGRECANASE; ALPHA CHEMOKINE; BETA CHEMOKINE; CELL ADHESION MOLECULE; CHEMOKINE; CHLOROTRIANISENE; COLLAGENASE 3; CX3C CHEMOKINE; GELATINASE A; INTERSTITIAL COLLAGENASE; MATRIX METALLOPROTEINASE 14; METALLOPROTEINASE; MONOCYTE CHEMOTACTIC PROTEIN 3; SYNDECAN 1; TISSUE INHIBITOR OF METALLOPROTEINASE 3; TUMOR NECROSIS FACTOR ALPHA; TUMOR NECROSIS FACTOR ALPHA CONVERTING ENZYME;

EID: 0142218538     PISSN: 00034967     EISSN: None     Source Type: Journal    
DOI: 10.1136/ard.62.1.43     Document Type: Conference Paper
Times cited : (122)

References (34)
  • 1
    • 0037180812 scopus 로고    scopus 로고
    • Points of control in inflammation
    • Nothon C. Points of control in inflammation. Nature 2002;420:846-52.
    • (2002) Nature , vol.420 , pp. 846-852
    • Nothon, C.1
  • 2
    • 0033848986 scopus 로고    scopus 로고
    • Matrix metalloproteinases: Effectors of development and normal physiology
    • Vu TH, Werb Z. Matrix metalloproteinases: effectors of development and normal physiology. Genes Dev 2000;14:2123-33.
    • (2000) Genes Dev , vol.14 , pp. 2123-2133
    • Vu, T.H.1    Werb, Z.2
  • 3
    • 0142250222 scopus 로고    scopus 로고
    • Directing cell fate through matrix metalloproteinases during cancer progression
    • in press
    • Hojillo C, Mohammed F, Khokha R. Directing cell fate through matrix metalloproteinases during cancer progression. Br J Cancer (in press).
    • Br J Cancer
    • Hojillo, C.1    Mohammed, F.2    Khokha, R.3
  • 4
    • 0037180757 scopus 로고    scopus 로고
    • Inflammation and cancer
    • Coussens LM, Werb Z. Inflammation and cancer. Nature 2002;420:860-7.
    • (2002) Nature , vol.420 , pp. 860-867
    • Coussens, L.M.1    Werb, Z.2
  • 5
    • 0033214433 scopus 로고    scopus 로고
    • Regulation of intestinal alpha-defensin activation by the metalloproteinase matrilysin in innate host defense
    • Wilson CL, Ouellette AJ, Satchell DP, Ayabe T, Lopez-Boado YS, Stratman JL, et al. Regulation of intestinal alpha-defensin activation by the metalloproteinase matrilysin in innate host defense. Science 1999;286:113-17.
    • (1999) Science , vol.286 , pp. 113-117
    • Wilson, C.L.1    Ouellette, A.J.2    Satchell, D.P.3    Ayabe, T.4    Lopez-Boado, Y.S.5    Stratman, J.L.6
  • 6
    • 18744383614 scopus 로고    scopus 로고
    • Matrilysin shedding of syndecan-1 regulates chemokine mobilization and transepithelial efflux of neutrophils in acute lung injury
    • Li Q, Park PW, Wilson CL, Parks WC. Matrilysin shedding of syndecan-1 regulates chemokine mobilization and transepithelial efflux of neutrophils in acute lung injury. Cell 2002;111:635-46.
    • (2002) Cell , vol.111 , pp. 635-646
    • Li, Q.1    Park, P.W.2    Wilson, C.L.3    Parks, W.C.4
  • 8
    • 0037103183 scopus 로고    scopus 로고
    • Matrix metalloproteinase processing of monocyte chemoattractant proteins generates CC chemokine receptor antagonists with anti-inflammatory properties in vivo
    • McQuibban GA, Gong JH, Wong JP, Wallace JL, Clark-Lewis I, Overall CM. Matrix metalloproteinase processing of monocyte chemoattractant proteins generates CC chemokine receptor antagonists with anti-inflammatory properties in vivo. Blood 2002;100:1160-7.
    • (2002) Blood , vol.100 , pp. 1160-1167
    • McQuibban, G.A.1    Gong, J.H.2    Wong, J.P.3    Wallace, J.L.4    Clark-Lewis, I.5    Overall, C.M.6
  • 9
    • 0035941359 scopus 로고    scopus 로고
    • Matrix metalloproteinase activity inactivates the CXC chemokine stromal cell-derived factor-1
    • McQuibban GA, Butler GS, Gong JH, Bendall L, Power C, Clark-Lewis I, et al. Matrix metalloproteinase activity inactivates the CXC chemokine stromal cell-derived factor-1. J Biol Chem 2001;276:43503-8.
    • (2001) J Biol Chem , vol.276 , pp. 43503-43508
    • McQuibban, G.A.1    Butler, G.S.2    Gong, J.H.3    Bendall, L.4    Power, C.5    Clark-Lewis, I.6
  • 10
    • 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
  • 11
    • 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;275:31226-32.
    • (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
  • 12
    • 0032479305 scopus 로고    scopus 로고
    • Localization of the functional domains of human tissue inhibitor of metalloproteinases-3 and the effects of Sorsby's fundus dystrophy mutation
    • Langton KP, Barker MD, McKie N. Localization of the functional domains of human tissue inhibitor of metalloproteinases-3 and the effects of Sorsby's fundus dystrophy mutation. J Biol Chem 1998;273:16778-81.
    • (1998) J Biol Chem , vol.273 , pp. 16778-16781
    • Langton, K.P.1    Barker, M.D.2    McKie, N.3
  • 13
    • 0028097367 scopus 로고
    • Mutations in the tissue inhibitor of metalloproteinases-3 (TIMP3) in patients with Sorsby's fundus dystrophy
    • Weber BHF, Vogt G, Pruett RC, Stohr H, Felbor U. Mutations in the tissue inhibitor of metalloproteinases-3 (TIMP3) in patients with Sorsby's fundus dystrophy. Nat Genet 1994;8:352-6.
    • (1994) Nat Genet , vol.8 , pp. 352-356
    • Weber, B.H.F.1    Vogt, G.2    Pruett, R.C.3    Stohr, H.4    Felbor, U.5
  • 15
    • 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). Biol Chem 2001;276:12501-4.
    • (2001) Biol Chem , vol.276 , pp. 12501-12504
    • Kashiwagi, M.1    Tortorella, M.2    Nagase, H.3    Brew, K.4
  • 16
    • 8044257704 scopus 로고    scopus 로고
    • A metalloproteinase disintegrin that releases tumour-necrosis factor alpha from cells
    • Black RA, Rauch CT, Kozlosky CJ, Peschon JJ, Slock JL, Wolfson MF, et al. A metalloproteinase disintegrin that releases tumour-necrosis factor alpha from cells. Nature 1997;385:729-33.
    • (1997) Nature , vol.385 , pp. 729-733
    • Black, R.A.1    Rauch, C.T.2    Kozlosky, C.J.3    Peschon, J.J.4    Slock, J.L.5    Wolfson, M.F.6
  • 17
    • 8044250278 scopus 로고    scopus 로고
    • Cloning of a disintegrin metalloproteinase that processes precursor tumour-necrosis factor-alpha
    • Moss ML, Jin SL, Milla ME, Bickett DM, Burkhart W, Carter HL, et al. Cloning of a disintegrin metalloproteinase that processes precursor tumour-necrosis factor-alpha. Nature 1997;385:733-6.
    • (1997) Nature , vol.385 , pp. 733-736
    • Moss, M.L.1    Jin, S.L.2    Milla, M.E.3    Bickett, D.M.4    Burkhart, W.5    Carter, H.L.6
  • 18
    • 0029617952 scopus 로고
    • Blockade of TNFα with chimeric anti-TNFα monoclonal antibody, cA2 reduces (IL-6 and IL-8) release in Ra NMC cultures: A comparison with IL-1ra
    • Butler D, Maini RN, Feldmann M, Brennan FM. Blockade of TNFα with chimeric anti-TNFα monoclonal antibody, cA2 reduces (IL-6 and IL-8) release in RA NMC cultures: a comparison with IL-1ra. Eur Cytokin Netwk 1995;6:225-30.
    • (1995) Eur Cytokin Netwk , vol.6 , pp. 225-230
    • Butler, D.1    Maini, R.N.2    Feldmann, M.3    Brennan, F.M.4
  • 19
    • 0032937320 scopus 로고    scopus 로고
    • IL-4 potentiates IL-beta-and TNF-alpha-stimulated IL-8 and MCP-1 protein production in human retinal pigment epithelial cells
    • Bian ZM, Elner SG, Strieter RM, Kunkel SL, Lukacs NW, Elner VM. IL-4 potentiates IL-beta-and TNF-alpha-stimulated IL-8 and MCP-1 protein production in human retinal pigment epithelial cells. Curr Eye Res 1999;18:349-57.
    • (1999) Curr Eye Res , vol.18 , pp. 349-357
    • Bian, Z.M.1    Elner, S.G.2    Strieter, R.M.3    Kunkel, S.L.4    Lukacs, N.W.5    Elner, V.M.6
  • 20
    • 0030892804 scopus 로고    scopus 로고
    • Transcriptional control of matrix metalloproteinases and the tissue inhibitors of matrix metalloproteinases
    • Borden P, Heller RA. Transcriptional control of matrix metalloproteinases and the tissue inhibitors of matrix metalloproteinases. Crit Rev Eukaryot Gene Exp 1997;7:159-78.
    • (1997) Crit Rev Eukaryot Gene Exp , vol.7 , pp. 159-178
    • Borden, P.1    Heller, R.A.2
  • 22
    • 0034640286 scopus 로고    scopus 로고
    • Functional analysis of the domain structure of tumor necrosis factor-alpha converting enzyme
    • Reddy P, Slack JL, Davis R, Cerretti DP, Kozlosky CJ, Blanton RA, et al. Functional analysis of the domain structure of tumor necrosis factor-alpha converting enzyme. J Biol Chem 2000;275:14608-14.
    • (2000) J Biol Chem , vol.275 , pp. 14608-14614
    • Reddy, P.1    Slack, J.L.2    Davis, R.3    Cerretti, D.P.4    Kozlosky, C.J.5    Blanton, R.A.6
  • 23
    • 0026516744 scopus 로고
    • Stabilization of the biooctivity of tumor necrosis factor by its soluble receptors
    • Aderka D, Engelmann H, Maor Y, Brokebusch C, Wallach D. Stabilization of the biooctivity of tumor necrosis factor by its soluble receptors. J Exp Med 1992;175:323-9.
    • (1992) J Exp Med , vol.175 , pp. 323-329
    • Aderka, D.1    Engelmann, H.2    Maor, Y.3    Brokebusch, C.4    Wallach, D.5
  • 24
    • 0026757201 scopus 로고
    • Modulation of two forms of tumor necrosis factor receptors and their cellular response by soluble receptors and their monoclonal antibodies
    • Higuchi M, Aggarwal BB. Modulation of two forms of tumor necrosis factor receptors and their cellular response by soluble receptors and their monoclonal antibodies. J Biol Chem 1992;267:20892-9.
    • (1992) J Biol Chem , vol.267 , pp. 20892-20899
    • Higuchi, M.1    Aggarwal, B.B.2
  • 25
    • 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;3:337-41.
    • (2001) Arthritis Res , vol.3 , pp. 337-341
    • Mort, J.S.1    Billington, C.J.2
  • 28
    • 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
  • 29
    • 0029019867 scopus 로고
    • The gene structure of tissue inhibitor of metalloproteinases (TIMP)-3 and its inhibitory activities define the distinct TIMP gene family
    • Apte SS, Olsen BR, Murphy G. The gene structure of tissue inhibitor of metalloproteinases (TIMP)-3 and its inhibitory activities define the distinct TIMP gene family. J Biol Chem 1995;270:14313-18.
    • (1995) J Biol Chem , vol.270 , pp. 14313-14318
    • Apte, S.S.1    Olsen, B.R.2    Murphy, G.3
  • 31
    • 0035068522 scopus 로고    scopus 로고
    • Physiology of cytokine pathways in rheumatoid arthritis
    • Arend WP. Physiology of cytokine pathways in rheumatoid arthritis. Arthritis Rheum 2001;45:101-6.
    • (2001) Arthritis Rheum , vol.45 , pp. 101-106
    • Arend, W.P.1
  • 32
    • 0035851124 scopus 로고    scopus 로고
    • Tumor necrosis factor-alpha-converting enzyme (ADAM17) mediates the cleavage and shedding of fractalkine (CX3CL1)
    • Garton KJ, Gough PJ, Blobel CP, Murphy G, Greoves DR, Dempsey PJ, et al. Tumor necrosis factor-alpha-converting enzyme (ADAM17) mediates the cleavage and shedding of fractalkine (CX3CL1). J Biol Chem 2001;276:37993-8001.
    • (2001) J Biol Chem , vol.276 , pp. 37993-38001
    • Garton, K.J.1    Gough, P.J.2    Blobel, C.P.3    Murphy, G.4    Greoves, D.R.5    Dempsey, P.J.6
  • 34
    • 0037319185 scopus 로고    scopus 로고
    • Cartilage degradation and invasion by rheumatoid synovial fibroblasts is inhibited by gene transfer of TIMP-1 and TIMP-3
    • van der Laan WH, Quax PH, Seemayer CA, Huisman LG, Pieterman EJ, Grimbergen JM, et al. Cartilage degradation and invasion by rheumatoid synovial fibroblasts is inhibited by gene transfer of TIMP-1 and TIMP-3. Gene Ther 2003;10:234-42.
    • (2003) Gene Ther , vol.10 , pp. 234-242
    • Van Der Laan, W.H.1    Quax, P.H.2    Seemayer, C.A.3    Huisman, L.G.4    Pieterman, E.J.5    Grimbergen, J.M.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.