메뉴 건너뛰기




Volumn 18, Issue 3, 2010, Pages 279-288

MAPKs are essential upstream signaling pathways in proteolytic cartilage degradation - divergence in pathways leading to aggrecanase and MMP-mediated articular cartilage degradation

Author keywords

Aggrecanase; Articular cartilage; Cartilage degradation; Cartilage metabolism; Catabolic enzymes; Cell signaling pathways; Enzyme pathways; Matrixmetalloprotinase; Mitogen activated protein kinases (MAPKs); Osteoarthritis

Indexed keywords

AGGRECANASE; CARBOXY TERMINAL TELOPEPTIDE; COLLAGEN TYPE 2; GELATINASE; GELATINASE A; GELATINASE B; HYDROXYPROLINE; MATRIX METALLOPROTEINASE; MITOGEN ACTIVATED PROTEIN KINASE 1; MITOGEN ACTIVATED PROTEIN KINASE 3; MITOGEN ACTIVATED PROTEIN KINASE P38; MITOGEN ACTIVATED PROTEIN KINASE P38 INHIBITOR; ONCOSTATIN M; PROTEIN TYROSINE KINASE; TUMOR NECROSIS FACTOR;

EID: 76549091830     PISSN: 10634584     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.joca.2009.11.005     Document Type: Review
Times cited : (148)

References (44)
  • 1
  • 2
    • 15844413814 scopus 로고    scopus 로고
    • Deletion of active ADAMTS5 prevents cartilage degradation in a murine model of osteoarthritis
    • Glasson S.S., Askew R., Sheppard B., Carito B., Blanchet T., Ma H.L., et al. Deletion of active ADAMTS5 prevents cartilage degradation in a murine model of osteoarthritis. Nature 434 7033 (2005 Mar 31) 644-648
    • (2005) Nature , vol.434 , Issue.7033 , pp. 644-648
    • Glasson, S.S.1    Askew, R.2    Sheppard, B.3    Carito, B.4    Blanchet, T.5    Ma, H.L.6
  • 3
    • 4043154293 scopus 로고    scopus 로고
    • Characterization of and osteoarthritis susceptibility in ADAMTS-4-knockout mice
    • Glasson S.S., Askew R., Sheppard B., Carito B.A., Blanchet T., Ma H.L., et al. Characterization of and osteoarthritis susceptibility in ADAMTS-4-knockout mice. Arthritis Rheum 50 8 (2004 Aug) 2547-2558
    • (2004) Arthritis Rheum , vol.50 , Issue.8 , pp. 2547-2558
    • Glasson, S.S.1    Askew, R.2    Sheppard, B.3    Carito, B.A.4    Blanchet, T.5    Ma, H.L.6
  • 4
    • 34247891816 scopus 로고    scopus 로고
    • ADAMTS-5 deficiency does not block aggrecanolysis at preferred cleavage sites in the chondroitin sulfate-rich region of aggrecan
    • East C.J., Stanton H., Golub S.B., Rogerson F.M., and Fosang A.J. ADAMTS-5 deficiency does not block aggrecanolysis at preferred cleavage sites in the chondroitin sulfate-rich region of aggrecan. J Biol Chem 282 12 (2007 Mar 23) 8632-8640
    • (2007) J Biol Chem , vol.282 , Issue.12 , pp. 8632-8640
    • East, C.J.1    Stanton, H.2    Golub, S.B.3    Rogerson, F.M.4    Fosang, A.J.5
  • 5
    • 15844384854 scopus 로고    scopus 로고
    • ADAMTS5 is the major aggrecanase in mouse cartilage in vivo and in vitro
    • Stanton H., Rogerson F.M., East C.J., Golub S.B., Lawlor K.E., Meeker C.T., et al. ADAMTS5 is the major aggrecanase in mouse cartilage in vivo and in vitro. Nature 434 7033 (2005 Mar 31) 648-652
    • (2005) Nature , vol.434 , Issue.7033 , pp. 648-652
    • Stanton, H.1    Rogerson, F.M.2    East, C.J.3    Golub, S.B.4    Lawlor, K.E.5    Meeker, C.T.6
  • 6
    • 0034693231 scopus 로고    scopus 로고
    • Generation and novel distribution of matrix metalloproteinase-derived aggrecan fragments in porcine cartilage explants
    • Fosang A.J., Last K., Stanton H., Weeks D.B., Campbell I.K., Hardingham T.E., et al. Generation and novel distribution of matrix metalloproteinase-derived aggrecan fragments in porcine cartilage explants. J Biol Chem 275 42 (2000 Oct 20) 33027-33037
    • (2000) J Biol Chem , vol.275 , Issue.42 , pp. 33027-33037
    • Fosang, A.J.1    Last, K.2    Stanton, H.3    Weeks, D.B.4    Campbell, I.K.5    Hardingham, T.E.6
  • 7
    • 0032479462 scopus 로고    scopus 로고
    • Membrane-type 1 MMP (MMP-14) cleaves at three sites in the aggrecan interglobular domain
    • Fosang A.J., Last K., Fujii Y., Seiki M., and Okada Y. Membrane-type 1 MMP (MMP-14) cleaves at three sites in the aggrecan interglobular domain. FEBS Lett 430 3 (1998 Jul 3) 186-190
    • (1998) FEBS Lett , vol.430 , Issue.3 , pp. 186-190
    • Fosang, A.J.1    Last, K.2    Fujii, Y.3    Seiki, M.4    Okada, Y.5
  • 8
    • 0029852094 scopus 로고    scopus 로고
    • Aggrecan is degraded by matrix metalloproteinases in human arthritis. Evidence that matrix metalloproteinase and aggrecanase activities can be independent
    • Fosang A.J., Last K., and Maciewicz R.A. Aggrecan is degraded by matrix metalloproteinases in human arthritis. Evidence that matrix metalloproteinase and aggrecanase activities can be independent. J Clin Invest 98 10 (1996 Nov 15) 2292-2299
    • (1996) J Clin Invest , vol.98 , Issue.10 , pp. 2292-2299
    • Fosang, A.J.1    Last, K.2    Maciewicz, R.A.3
  • 9
    • 29244440826 scopus 로고    scopus 로고
    • In vitro, ex vivo, and in vivo methodological approaches for studying therapeutic targets of osteoporosis and degenerative joint diseases: how biomarkers can assist?
    • Schaller S., Henriksen K., Hoegh-Andersen P., Sondergaard B.C., Sumer E.U., Tanko L.B., et al. In vitro, ex vivo, and in vivo methodological approaches for studying therapeutic targets of osteoporosis and degenerative joint diseases: how biomarkers can assist?. Assay Drug Dev Technol 3 5 (2005 Oct) 553-580
    • (2005) Assay Drug Dev Technol , vol.3 , Issue.5 , pp. 553-580
    • Schaller, S.1    Henriksen, K.2    Hoegh-Andersen, P.3    Sondergaard, B.C.4    Sumer, E.U.5    Tanko, L.B.6
  • 10
    • 33745584358 scopus 로고    scopus 로고
    • Relative contribution of matrix metalloprotease and cysteine protease activities to cytokine-stimulated articular cartilage degradation
    • Sondergaard B.C., Henriksen K., Wulf H., Oestergaard S., Schurigt U., Brauer R., et al. Relative contribution of matrix metalloprotease and cysteine protease activities to cytokine-stimulated articular cartilage degradation. Osteoarthritis Cartilage 14 8 (2006 Aug) 738-748
    • (2006) Osteoarthritis Cartilage , vol.14 , Issue.8 , pp. 738-748
    • Sondergaard, B.C.1    Henriksen, K.2    Wulf, H.3    Oestergaard, S.4    Schurigt, U.5    Brauer, R.6
  • 11
    • 33746952485 scopus 로고    scopus 로고
    • Effects of ovariectomy and estrogen therapy on type II collagen degradation and structural integrity of articular cartilage in rats: implications of the time of initiation
    • Oestergaard S., Sondergaard B.C., Hoegh-Andersen P., Henriksen K., Qvist P., Christiansen C., et al. Effects of ovariectomy and estrogen therapy on type II collagen degradation and structural integrity of articular cartilage in rats: implications of the time of initiation. Arthritis Rheum 54 8 (2006 Aug) 2441-2451
    • (2006) Arthritis Rheum , vol.54 , Issue.8 , pp. 2441-2451
    • Oestergaard, S.1    Sondergaard, B.C.2    Hoegh-Andersen, P.3    Henriksen, K.4    Qvist, P.5    Christiansen, C.6
  • 12
    • 0034041424 scopus 로고    scopus 로고
    • Comparison of the degradation of type II collagen and proteoglycan in nasal and articular cartilages induced by interleukin-1 and the selective inhibition of type II collagen cleavage by collagenase
    • Billinghurst R.C., Wu W., Ionescu M., Reiner A., Dahlberg L., Chen J., et al. Comparison of the degradation of type II collagen and proteoglycan in nasal and articular cartilages induced by interleukin-1 and the selective inhibition of type II collagen cleavage by collagenase. Arthritis Rheum 43 3 (2000 Mar) 664-672
    • (2000) Arthritis Rheum , vol.43 , Issue.3 , pp. 664-672
    • Billinghurst, R.C.1    Wu, W.2    Ionescu, M.3    Reiner, A.4    Dahlberg, L.5    Chen, J.6
  • 13
    • 0030891983 scopus 로고    scopus 로고
    • Enhanced cleavage of type II collagen by collagenases in osteoarthritic articular cartilage
    • Billinghurst R.C., Dahlberg L., Ionescu M., Reiner A., Bourne R., Rorabeck C., et al. Enhanced cleavage of type II collagen by collagenases in osteoarthritic articular cartilage. J Clin Invest 99 7 (1997 Apr 1) 1534-1545
    • (1997) J Clin Invest , vol.99 , Issue.7 , pp. 1534-1545
    • Billinghurst, R.C.1    Dahlberg, L.2    Ionescu, M.3    Reiner, A.4    Bourne, R.5    Rorabeck, C.6
  • 14
    • 0026701977 scopus 로고
    • The interglobular domain of cartilage aggrecan is cleaved by PUMP, gelatinases, and cathepsin B
    • Fosang A.J., Neame P.J., Last K., Hardingham T.E., Murphy G., and Hamilton J.A. The interglobular domain of cartilage aggrecan is cleaved by PUMP, gelatinases, and cathepsin B. J Biol Chem 267 27 (1992 Sep 25) 19470-19474
    • (1992) J Biol Chem , vol.267 , Issue.27 , 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
  • 15
    • 33846386045 scopus 로고    scopus 로고
    • MMP and non-MMP-mediated release of aggrecan and its fragments from articular cartilage: a comparative study of three different aggrecan and glycosaminoglycan assays
    • Sumer E.U., Sondergaard B.C., Rousseau J.C., Delmas P.D., Fosang A.J., Karsdal M.A., et al. MMP and non-MMP-mediated release of aggrecan and its fragments from articular cartilage: a comparative study of three different aggrecan and glycosaminoglycan assays. Osteoarthritis Cartilage 15 2 (2007 Feb) 212-221
    • (2007) Osteoarthritis Cartilage , vol.15 , Issue.2 , pp. 212-221
    • Sumer, E.U.1    Sondergaard, B.C.2    Rousseau, J.C.3    Delmas, P.D.4    Fosang, A.J.5    Karsdal, M.A.6
  • 16
    • 34248569434 scopus 로고    scopus 로고
    • Induction of increased cAMP levels in articular chondrocytes blocks matrix metalloproteinase-mediated cartilage degradation, but not aggrecanase-mediated cartilage degradation
    • Karsdal M.A., Sumer E.U., Wulf H., Madsen S.H., Christiansen C., Fosang A.J., et al. Induction of increased cAMP levels in articular chondrocytes blocks matrix metalloproteinase-mediated cartilage degradation, but not aggrecanase-mediated cartilage degradation. Arthritis Rheum 56 5 (2007 May) 1549-1558
    • (2007) Arthritis Rheum , vol.56 , Issue.5 , pp. 1549-1558
    • Karsdal, M.A.1    Sumer, E.U.2    Wulf, H.3    Madsen, S.H.4    Christiansen, C.5    Fosang, A.J.6
  • 17
  • 18
    • 33744932949 scopus 로고    scopus 로고
    • Prospects for disease modification in osteoarthritis
    • Abramson S.B., Attur M., and Yazici Y. Prospects for disease modification in osteoarthritis. Nat Clin Pract Rheumatol 2 6 (2006 Jun) 304-312
    • (2006) Nat Clin Pract Rheumatol , vol.2 , Issue.6 , pp. 304-312
    • Abramson, S.B.1    Attur, M.2    Yazici, Y.3
  • 19
    • 0034971296 scopus 로고    scopus 로고
    • Osteoarthritis, an inflammatory disease: potential implication for the selection of new therapeutic targets
    • Pelletier J.P., Martel-Pelletier J., and Abramson S.B. Osteoarthritis, an inflammatory disease: potential implication for the selection of new therapeutic targets. Arthritis Rheum 44 6 (2001 Jun) 1237-1247
    • (2001) Arthritis Rheum , vol.44 , Issue.6 , pp. 1237-1247
    • Pelletier, J.P.1    Martel-Pelletier, J.2    Abramson, S.B.3
  • 21
    • 0036286667 scopus 로고    scopus 로고
    • The role of cytokines in osteoarthritis pathophysiology
    • Fernandes J.C., Martel-Pelletier J., and Pelletier J.P. The role of cytokines in osteoarthritis pathophysiology. Biorheology 39 1-2 (2002) 237-246
    • (2002) Biorheology , vol.39 , Issue.1-2 , pp. 237-246
    • Fernandes, J.C.1    Martel-Pelletier, J.2    Pelletier, J.P.3
  • 22
    • 0035304643 scopus 로고    scopus 로고
    • Cytokine imbalance in the pathogenesis of rheumatoid arthritis: the role of interleukin-1 receptor antagonist
    • Arend W.P. Cytokine imbalance in the pathogenesis of rheumatoid arthritis: the role of interleukin-1 receptor antagonist. Semin Arthritis Rheum 30 5 Suppl 2 (2001 Apr) 1-6
    • (2001) Semin Arthritis Rheum , vol.30 , Issue.5 SUPPL. 2 , pp. 1-6
    • Arend, W.P.1
  • 23
    • 0025274640 scopus 로고
    • Cytokines and cytokine inhibitors or antagonists in rheumatoid arthritis
    • Arend W.P., and Dayer J.M. Cytokines and cytokine inhibitors or antagonists in rheumatoid arthritis. Arthritis Rheum 33 3 (1990 Mar) 305-315
    • (1990) Arthritis Rheum , vol.33 , Issue.3 , pp. 305-315
    • Arend, W.P.1    Dayer, J.M.2
  • 25
    • 0035914334 scopus 로고    scopus 로고
    • Transforming growth factor-beta-induced osteoblast elongation regulates osteoclastic bone resorption through a p38 mitogen-activated protein kinase- and matrix metalloproteinase-dependent pathway
    • Karsdal M.A., Fjording M.S., Foged N.T., Delaisse J.M., and Lochter A. Transforming growth factor-beta-induced osteoblast elongation regulates osteoclastic bone resorption through a p38 mitogen-activated protein kinase- and matrix metalloproteinase-dependent pathway. J Biol Chem 276 42 (2001 Oct 19) 39350-39358
    • (2001) J Biol Chem , vol.276 , Issue.42 , pp. 39350-39358
    • Karsdal, M.A.1    Fjording, M.S.2    Foged, N.T.3    Delaisse, J.M.4    Lochter, A.5
  • 26
    • 36549040859 scopus 로고    scopus 로고
    • The selectivity of protein kinase inhibitors: a further update
    • Bain J., Plater L., Elliott M., Shpiro N., Hastie C.J., McLauchlan H., et al. The selectivity of protein kinase inhibitors: a further update. Biochem J 408 3 (2007 Dec 15) 297-315
    • (2007) Biochem J , vol.408 , Issue.3 , pp. 297-315
    • Bain, J.1    Plater, L.2    Elliott, M.3    Shpiro, N.4    Hastie, C.J.5    McLauchlan, H.6
  • 27
    • 2642534318 scopus 로고    scopus 로고
    • Cartilage destruction in collagen induced arthritis assessed with a new biochemical marker for collagen type II C-telopeptide fragments
    • Ishikawa T., Nishigaki F., Christgau S., Noto T., Mo J., From N., et al. Cartilage destruction in collagen induced arthritis assessed with a new biochemical marker for collagen type II C-telopeptide fragments. J Rheumatol 31 6 (2004 Jun) 1174-1179
    • (2004) J Rheumatol , vol.31 , Issue.6 , pp. 1174-1179
    • Ishikawa, T.1    Nishigaki, F.2    Christgau, S.3    Noto, T.4    Mo, J.5    From, N.6
  • 29
    • 49449103020 scopus 로고    scopus 로고
    • Characterization of metalloprotease cleavage products of human articular cartilage
    • Zhen E.Y., Brittain I.J., Laska D.A., Mitchell P.G., Sumer E.U., Karsdal M.A., et al. Characterization of metalloprotease cleavage products of human articular cartilage. Arthritis Rheum 58 8 (2008 Aug) 2420-2431
    • (2008) Arthritis Rheum , vol.58 , Issue.8 , pp. 2420-2431
    • Zhen, E.Y.1    Brittain, I.J.2    Laska, D.A.3    Mitchell, P.G.4    Sumer, E.U.5    Karsdal, M.A.6
  • 30
    • 33846901629 scopus 로고    scopus 로고
    • Anabolic and catabolic function of chondrocyte ex vivo is reflected by the metabolic processing of type II collagen
    • Olsen A.K., Sondergaard B.C., Byrjalsen I., Tanko L.B., Christiansen C., Muller A., et al. Anabolic and catabolic function of chondrocyte ex vivo is reflected by the metabolic processing of type II collagen. Osteoarthritis Cartilage 15 3 (2007 Mar) 335-342
    • (2007) Osteoarthritis Cartilage , vol.15 , Issue.3 , pp. 335-342
    • Olsen, A.K.1    Sondergaard, B.C.2    Byrjalsen, I.3    Tanko, L.B.4    Christiansen, C.5    Muller, A.6
  • 31
    • 50949128814 scopus 로고    scopus 로고
    • The type II collagen fragments Helix-II and CTX-II reveal different enzymatic pathways of human cartilage collagen degradation
    • Charni-Ben T.N., Desmarais S., Bay-Jensen A.C., Delaisse J.M., Percival M.D., and Garnero P. The type II collagen fragments Helix-II and CTX-II reveal different enzymatic pathways of human cartilage collagen degradation. Osteoarthritis Cartilage 16 10 (2008 Oct) 1183-1191
    • (2008) Osteoarthritis Cartilage , vol.16 , Issue.10 , pp. 1183-1191
    • Charni-Ben, T.N.1    Desmarais, S.2    Bay-Jensen, A.C.3    Delaisse, J.M.4    Percival, M.D.5    Garnero, P.6
  • 32
    • 36749026266 scopus 로고    scopus 로고
    • Nitric oxide regulates matrix metalloproteinase-9 activity by guanylyl-cyclase-dependent and -independent pathways
    • Ridnour L.A., Windhausen A.N., Isenberg J.S., Yeung N., Thomas D.D., Vitek M.P., et al. Nitric oxide regulates matrix metalloproteinase-9 activity by guanylyl-cyclase-dependent and -independent pathways. Proc Natl Acad Sci USA 104 43 (2007 Oct 23) 16898-16903
    • (2007) Proc Natl Acad Sci USA , vol.104 , Issue.43 , pp. 16898-16903
    • Ridnour, L.A.1    Windhausen, A.N.2    Isenberg, J.S.3    Yeung, N.4    Thomas, D.D.5    Vitek, M.P.6
  • 33
    • 0036775227 scopus 로고    scopus 로고
    • Characterization of human aggrecanase 2 (ADAM-TS5): substrate specificity studies and comparison with aggrecanase 1 (ADAM-TS4)
    • Tortorella M.D., Liu R.Q., Burn T., Newton R.C., and Arner E. Characterization of human aggrecanase 2 (ADAM-TS5): substrate specificity studies and comparison with aggrecanase 1 (ADAM-TS4). Matrix Biol 21 6 (2002 Oct) 499-511
    • (2002) Matrix Biol , vol.21 , Issue.6 , pp. 499-511
    • Tortorella, M.D.1    Liu, R.Q.2    Burn, T.3    Newton, R.C.4    Arner, E.5
  • 34
    • 0346658321 scopus 로고    scopus 로고
    • Oncostatin M in combination with tumor necrosis factor alpha induces cartilage damage and matrix metalloproteinase expression in vitro and in vivo
    • Hui W., Rowan A.D., Richards C.D., and Cawston T.E. Oncostatin M in combination with tumor necrosis factor alpha induces cartilage damage and matrix metalloproteinase expression in vitro and in vivo. Arthritis Rheum 48 12 (2003 Dec) 3404-3418
    • (2003) Arthritis Rheum , vol.48 , Issue.12 , pp. 3404-3418
    • Hui, W.1    Rowan, A.D.2    Richards, C.D.3    Cawston, T.E.4
  • 35
    • 0033039398 scopus 로고    scopus 로고
    • An odyssey from breast to bone: multi-step control of mammary metastases and osteolysis by matrix metalloproteinases
    • Lochter A., and Bissell M.J. An odyssey from breast to bone: multi-step control of mammary metastases and osteolysis by matrix metalloproteinases. APMIS 107 (1999 Jan) 128-136
    • (1999) APMIS , vol.107 , pp. 128-136
    • Lochter, A.1    Bissell, M.J.2
  • 36
    • 0037114003 scopus 로고    scopus 로고
    • Matrix metalloproteinase-dependent activation of latent transforming growth factor-beta controls the conversion of osteoblasts into osteocytes by blocking osteoblast apoptosis
    • Karsdal M.A., Larsen L., Engsig M.T., Lou H., Ferreras M., Lochter A., et al. Matrix metalloproteinase-dependent activation of latent transforming growth factor-beta controls the conversion of osteoblasts into osteocytes by blocking osteoblast apoptosis. J Biol Chem 277 46 (2002 Nov 15) 44061-44067
    • (2002) J Biol Chem , vol.277 , Issue.46 , pp. 44061-44067
    • Karsdal, M.A.1    Larsen, L.2    Engsig, M.T.3    Lou, H.4    Ferreras, M.5    Lochter, A.6
  • 37
    • 0037811204 scopus 로고    scopus 로고
    • Induction of matrix metalloproteinase-13 gene expression by TNF-alpha is mediated by MAP kinases, AP-1, and NF-kappaB transcription factors in articular chondrocytes
    • Liacini A., Sylvester J., Li W.Q., Huang W., Dehnade F., Ahmad M., et al. Induction of matrix metalloproteinase-13 gene expression by TNF-alpha is mediated by MAP kinases, AP-1, and NF-kappaB transcription factors in articular chondrocytes. Exp Cell Res 288 1 (2003 Aug 1) 208-217
    • (2003) Exp Cell Res , vol.288 , Issue.1 , pp. 208-217
    • Liacini, A.1    Sylvester, J.2    Li, W.Q.3    Huang, W.4    Dehnade, F.5    Ahmad, M.6
  • 38
    • 38349161595 scopus 로고    scopus 로고
    • Alpha-MSH inhibits TNF-alpha-induced matrix metalloproteinase-13 expression by modulating p38 kinase and nuclear factor kappaB signaling in human chondrosarcoma HTB-94 cells
    • Yoon S.W., Chun J.S., Sung M.H., Kim J.Y., and Poo H. Alpha-MSH inhibits TNF-alpha-induced matrix metalloproteinase-13 expression by modulating p38 kinase and nuclear factor kappaB signaling in human chondrosarcoma HTB-94 cells. Osteoarthritis Cartilage 16 1 (2008 Jan) 115-124
    • (2008) Osteoarthritis Cartilage , vol.16 , Issue.1 , pp. 115-124
    • Yoon, S.W.1    Chun, J.S.2    Sung, M.H.3    Kim, J.Y.4    Poo, H.5
  • 39
    • 38849087358 scopus 로고    scopus 로고
    • Effects of intra-articular injection of p38 mitogen-activated protein kinase inhibitor on matrix metalloproteinase in articular cartilage of a rat model of osteoarthritis
    • Chen W.D., Jiang Q., Chen D.Y., Xu H., and Zhang Y.F. Effects of intra-articular injection of p38 mitogen-activated protein kinase inhibitor on matrix metalloproteinase in articular cartilage of a rat model of osteoarthritis. Zhongguo Yi Xue Ke Xue Yuan Xue Bao 29 6 (2007 Dec) 777-781
    • (2007) Zhongguo Yi Xue Ke Xue Yuan Xue Bao , vol.29 , Issue.6 , pp. 777-781
    • Chen, W.D.1    Jiang, Q.2    Chen, D.Y.3    Xu, H.4    Zhang, Y.F.5
  • 40
    • 0031114081 scopus 로고    scopus 로고
    • Actions of IL-1 are selectively controlled by p38 mitogen-activated protein kinase: regulation of prostaglandin H synthase-2, metalloproteinases, and IL-6 at different levels
    • Ridley S.H., Sarsfield S.J., Lee J.C., Bigg H.F., Cawston T.E., Taylor D.J., et al. Actions of IL-1 are selectively controlled by p38 mitogen-activated protein kinase: regulation of prostaglandin H synthase-2, metalloproteinases, and IL-6 at different levels. J Immunol 158 7 (1997 Apr 1) 3165-3173
    • (1997) J Immunol , vol.158 , Issue.7 , pp. 3165-3173
    • Ridley, S.H.1    Sarsfield, S.J.2    Lee, J.C.3    Bigg, H.F.4    Cawston, T.E.5    Taylor, D.J.6
  • 41
    • 0033851463 scopus 로고    scopus 로고
    • Interleukin-1 induction of collagenase 3 (matrix metalloproteinase 13) gene expression in chondrocytes requires p38, c-Jun N-terminal kinase, and nuclear factor kappaB: differential regulation of collagenase 1 and collagenase 3
    • Mengshol J.A., Vincenti M.P., Coon C.I., Barchowsky A., and Brinckerhoff C.E. Interleukin-1 induction of collagenase 3 (matrix metalloproteinase 13) gene expression in chondrocytes requires p38, c-Jun N-terminal kinase, and nuclear factor kappaB: differential regulation of collagenase 1 and collagenase 3. Arthritis Rheum 43 4 (2000 Apr) 801-811
    • (2000) Arthritis Rheum , vol.43 , Issue.4 , pp. 801-811
    • Mengshol, J.A.1    Vincenti, M.P.2    Coon, C.I.3    Barchowsky, A.4    Brinckerhoff, C.E.5
  • 42
    • 33847185270 scopus 로고    scopus 로고
    • Signaling pathways implicated in oncostatin M-induced aggrecanase-1 and matrix metalloproteinase-13 expression in human articular chondrocytes
    • El Mabrouk M., Sylvester J., and Zafarullah M. Signaling pathways implicated in oncostatin M-induced aggrecanase-1 and matrix metalloproteinase-13 expression in human articular chondrocytes. Biochim Biophys Acta 1773 3 (2007 Mar) 309-320
    • (2007) Biochim Biophys Acta , vol.1773 , Issue.3 , pp. 309-320
    • El Mabrouk, M.1    Sylvester, J.2    Zafarullah, M.3
  • 43
    • 65549146416 scopus 로고    scopus 로고
    • Role of Src signal transduction pathways in scatter factor-mediated cellular protection
    • Fan S., Meng Q., Laterra J.J., and Rosen E.M. Role of Src signal transduction pathways in scatter factor-mediated cellular protection. J Biol Chem 284 12 (2009 Mar 20) 7561-7577
    • (2009) J Biol Chem , vol.284 , Issue.12 , pp. 7561-7577
    • Fan, S.1    Meng, Q.2    Laterra, J.J.3    Rosen, E.M.4
  • 44
    • 45149106656 scopus 로고    scopus 로고
    • Transforming growth factor beta1 induces alphavbeta3 integrin expression in human lung fibroblasts via a beta3 integrin-, c-Src-, and p38 MAPK-dependent pathway
    • Pechkovsky D.V., Scaffidi A.K., Hackett T.L., Ballard J., Shaheen F., Thompson P.J., et al. Transforming growth factor beta1 induces alphavbeta3 integrin expression in human lung fibroblasts via a beta3 integrin-, c-Src-, and p38 MAPK-dependent pathway. J Biol Chem 283 19 (2008 May 9) 12898-12908
    • (2008) J Biol Chem , vol.283 , Issue.19 , pp. 12898-12908
    • Pechkovsky, D.V.1    Scaffidi, A.K.2    Hackett, T.L.3    Ballard, J.4    Shaheen, F.5    Thompson, P.J.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.