메뉴 건너뛰기




Volumn 74, Issue 8, 2015, Pages 1580-1587

Protection against murine osteoarthritis by inhibition of the 26S proteasome and lysine-48 linked ubiquitination

Author keywords

[No Author keywords available]

Indexed keywords

ARGININE; BENZYLOXYCARBONYLLEUCYLLEUCYLLEUCINAL; COLLAGENASE 3; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; INTERLEUKIN 6; LYSINE; PROTEASOME; UBIQUITIN; ATP DEPENDENT 26S PROTEASE; BENZYLOXYCARBONYLLEUCYL-LEUCYL-LEUCINE ALDEHYDE; CYSTEINE PROTEINASE INHIBITOR; LEUPEPTIN; MMP13 PROTEIN, MOUSE; SIGNAL PEPTIDE; ZINC FINGER PROTEIN;

EID: 84940377826     PISSN: 00034967     EISSN: 14682060     Source Type: Journal    
DOI: 10.1136/annrheumdis-2013-204962     Document Type: Article
Times cited : (30)

References (41)
  • 2
    • 63249118366 scopus 로고    scopus 로고
    • Molecular mechanisms of cartilage destruction in osteoarthritis
    • Loeser R. Molecular mechanisms of cartilage destruction in osteoarthritis. Biochem J 2008;8:303-6.
    • (2008) Biochem J , vol.8 , pp. 303-306
    • Loeser, R.1
  • 3
    • 0029583775 scopus 로고
    • The chondrocyte, architect of cartilage. Biomechanics, structure, function and molecular biology of cartilage matrix macromolecules
    • Muir H. The chondrocyte, architect of cartilage. Biomechanics, structure, function and molecular biology of cartilage matrix macromolecules. Bioessays 1995;17:1039-48.
    • (1995) Bioessays , vol.17 , pp. 1039-1048
    • Muir, H.1
  • 4
    • 15844413814 scopus 로고    scopus 로고
    • Deletion of active ADAMTS5 prevents cartilage degradation in a murine model of osteoarthritis
    • Glasson SS, Askew R, Sheppard B, et al. Deletion of active ADAMTS5 prevents cartilage degradation in a murine model of osteoarthritis. Nature. 2005;434:644-8.
    • (2005) Nature. , vol.434 , pp. 644-648
    • Glasson, S.S.1    Askew, R.2    Sheppard, B.3
  • 5
    • 84862529832 scopus 로고    scopus 로고
    • The ubiquitin proteasome system and efficacy of proteasome inhibitors in diseases
    • Chitra S, Nalini G, Rajasekhar G. The ubiquitin proteasome system and efficacy of proteasome inhibitors in diseases. Int J Rheum Dis 2012;15:249-60.
    • (2012) Int J Rheum Dis , vol.15 , pp. 249-260
    • Chitra, S.1    Nalini, G.2    Rajasekhar, G.3
  • 6
    • 49249120530 scopus 로고    scopus 로고
    • Polyubiquitin chains: Functions, structures, and mechanisms
    • Li W, Ye Y. Polyubiquitin chains: functions, structures, and mechanisms. Cell Mol Life Sci 2008;65:2397-406.
    • (2008) Cell Mol Life Sci , vol.65 , pp. 2397-2406
    • Li, W.1    Ye, Y.2
  • 7
    • 54349103091 scopus 로고    scopus 로고
    • Differential Toll-like receptor-dependent collagenase expression in chondrocytes
    • Zhang Q, Hui W, Litherland GJ, et al. Differential Toll-like receptor-dependent collagenase expression in chondrocytes. Ann Rheum Dis 2008;67:1633-41.
    • (2008) Ann Rheum Dis , vol.67 , pp. 1633-1641
    • Zhang, Q.1    Hui, W.2    Litherland, G.J.3
  • 8
    • 84876591815 scopus 로고    scopus 로고
    • Matrix metalloproteinase 13 expression in response to double-stranded RNA in human chondrocytes
    • Radwan M, Gavriilidis C, Robinson JH, et al. Matrix metalloproteinase 13 expression in response to double-stranded RNA in human chondrocytes. Arthritis Rheum 2013;65:1290-301.
    • (2013) Arthritis Rheum , vol.65 , pp. 1290-1301
    • Radwan, M.1    Gavriilidis, C.2    Robinson, J.H.3
  • 9
    • 84861344026 scopus 로고    scopus 로고
    • Integrative analysis of the ubiquitin proteome isolated using Tandem Ubiquitin Binding Entities (TUBEs)
    • Lopitz-Otsoa F, Rodriguez-Suarez E, Aillet F, et al. Integrative analysis of the ubiquitin proteome isolated using Tandem Ubiquitin Binding Entities (TUBEs). J Proteomics 2012;75:2998-3014.
    • (2012) J Proteomics , vol.75 , pp. 2998-3014
    • Lopitz-Otsoa, F.1    Rodriguez-Suarez, E.2    Aillet, F.3
  • 10
    • 26844559000 scopus 로고    scopus 로고
    • Exponentially modified protein abundance index (emPAI) for estimation of absolute protein amount in proteomics by the number of sequenced peptides per protein
    • Ishihama Y, Oda Y, Tabata T, et al. Exponentially modified protein abundance index (emPAI) for estimation of absolute protein amount in proteomics by the number of sequenced peptides per protein. Mol Cell Proteomics 2005;4:1265-72.
    • (2005) Mol Cell Proteomics , vol.4 , pp. 1265-1272
    • Ishihama, Y.1    Oda, Y.2    Tabata, T.3
  • 11
    • 77957752356 scopus 로고    scopus 로고
    • HDAC-mediated control of ERK- and PI3K-dependent TGF-beta-induced extracellular matrix-regulating genes
    • Barter MJ, Pybus L, Litherland GJ, et al. HDAC-mediated control of ERK- and PI3K-dependent TGF-beta-induced extracellular matrix-regulating genes. Matrix Biol 2010;29:602-12.
    • (2010) Matrix Biol , vol.29 , pp. 602-612
    • Barter, M.J.1    Pybus, L.2    Litherland, G.J.3
  • 12
    • 77957555605 scopus 로고    scopus 로고
    • Lipophilic statins prevent matrix metalloproteinase-mediated cartilage collagen breakdown by inhibiting protein geranylgeranylation
    • Barter MJ, Hui W, Lakey RL, et al. Lipophilic statins prevent matrix metalloproteinase-mediated cartilage collagen breakdown by inhibiting protein geranylgeranylation. Ann Rheum Dis 2010;69:2189-98.
    • (2010) Ann Rheum Dis , vol.69 , pp. 2189-2198
    • Barter, M.J.1    Hui, W.2    Lakey, R.L.3
  • 13
    • 77950367411 scopus 로고    scopus 로고
    • In vitro model of cartilage degradation
    • Hui W, Cawston TE. In vitro model of cartilage degradation. Methods Mol Biol 2010;622:341-8.
    • (2010) Methods Mol Biol , vol.622 , pp. 341-348
    • Hui, W.1    Cawston, T.E.2
  • 14
    • 34548566958 scopus 로고    scopus 로고
    • The surgical destabilization of the medial meniscus (DMM) model of osteoarthritis in the 129/SvEv mouse
    • Glasson SS, Blanchet TJ, Morris EA. The surgical destabilization of the medial meniscus (DMM) model of osteoarthritis in the 129/SvEv mouse. Osteoarthritis Cartilage 2007;15:1061-9.
    • (2007) Osteoarthritis Cartilage , vol.15 , pp. 1061-1069
    • Glasson, S.S.1    Blanchet, T.J.2    Morris, E.A.3
  • 15
    • 77954236941 scopus 로고    scopus 로고
    • Attenuation of pain and inflammation in adjuvant-induced arthritis by the proteasome inhibitor MG132
    • Ahmed AS, Li J, Ahmed M, et al. Attenuation of pain and inflammation in adjuvant-induced arthritis by the proteasome inhibitor MG132. Arthritis Rheum 2010;62:2160-9.
    • (2010) Arthritis Rheum , vol.62 , pp. 2160-2169
    • Ahmed, A.S.1    Li, J.2    Ahmed, M.3
  • 16
    • 77956924858 scopus 로고    scopus 로고
    • The OARSI histopathology initiative-recommendations for histological assessments of osteoarthritis in the mouse
    • Glasson SS, Chambers MG, Van Den Berg WB, et al. The OARSI histopathology initiative-recommendations for histological assessments of osteoarthritis in the mouse. Osteoarthritis Cartilage 2010;18(Suppl 3):S17-23.
    • (2010) Osteoarthritis Cartilage , vol.18 , pp. S17-S23
    • Glasson, S.S.1    Chambers, M.G.2    Van Den Berg, W.B.3
  • 17
    • 84879851334 scopus 로고    scopus 로고
    • Class i histone deacetylase inhibition modulates metalloproteinase expression and blocks cytokine-induced cartilage degradation
    • Culley KL, Hui W, Barter MJ, et al. Class I histone deacetylase inhibition modulates metalloproteinase expression and blocks cytokine-induced cartilage degradation. Arthritis Rheum 2013;65:1822-30.
    • (2013) Arthritis Rheum , vol.65 , pp. 1822-1830
    • Culley, K.L.1    Hui, W.2    Barter, M.J.3
  • 18
    • 0037663945 scopus 로고    scopus 로고
    • Effects of mutant ubiquitin on ts1 retrovirus-mediated neuropathology
    • Zhang M, Thurig S, Tsirigotis M, et al. Effects of mutant ubiquitin on ts1 retrovirus-mediated neuropathology. J Virol 2003;77:7193-201.
    • (2003) J Virol , vol.77 , pp. 7193-7201
    • Zhang, M.1    Thurig, S.2    Tsirigotis, M.3
  • 19
    • 0034959450 scopus 로고    scopus 로고
    • Analysis of ubiquitination in vivo using a transgenic mouse model
    • 8, 30
    • Tsirigotis M, Thurig S, Dube M, et al. Analysis of ubiquitination in vivo using a transgenic mouse model. Biotechniques 2001;31:120-6, 8, 30.
    • (2001) Biotechniques , vol.31 , pp. 120-126
    • Tsirigotis, M.1    Thurig, S.2    Dube, M.3
  • 20
    • 84862761186 scopus 로고    scopus 로고
    • Diverse ubiquitin signaling in NF-kappaB activation
    • Iwai K. Diverse ubiquitin signaling in NF-kappaB activation. Trends Cell Biol 2012;22:355-64.
    • (2012) Trends Cell Biol , vol.22 , pp. 355-364
    • Iwai, K.1
  • 21
    • 11244285329 scopus 로고    scopus 로고
    • Constitutive and interleukin-1-inducible phosphorylation of p65 NF-{kappa}B at serine 536 is mediated by multiple protein kinases including I{kappa}B kinase (IKK)-{alpha}, IKK{beta}, IKK{epsilon}, TRAF family member-associated (TANK)-binding kinase 1(TBK1), and an unknown kinase and couples p65 to TATA-binding protein-associated factor II31-mediated interleukin-8 transcription
    • Buss H, Dorrie A, Schmitz ML, et al. Constitutive and interleukin-1-inducible phosphorylation of p65 NF-{kappa}B at serine 536 is mediated by multiple protein kinases including I{kappa}B kinase (IKK)-{alpha}, IKK{beta}, IKK{epsilon}, TRAF family member-associated (TANK)-binding kinase 1(TBK1), and an unknown kinase and couples p65 to TATA-binding protein-associated factor II31-mediated interleukin-8 transcription. J Biol Chem 2004;279:55633-43.
    • (2004) J Biol Chem , vol.279 , pp. 55633-55643
    • Buss, H.1    Dorrie, A.2    Schmitz, M.L.3
  • 22
    • 84855857580 scopus 로고    scopus 로고
    • Tyrosine nitration of PA700 links proteasome activation to endothelial dysfunction in mouse models with cardiovascular risk factors
    • Xu J, Wang S, Zhang M, et al. Tyrosine nitration of PA700 links proteasome activation to endothelial dysfunction in mouse models with cardiovascular risk factors. PLoS ONE 2012;7:e29649.
    • (2012) PLoS ONE , vol.7 , pp. e29649
    • Xu, J.1    Wang, S.2    Zhang, M.3
  • 23
    • 57749107726 scopus 로고    scopus 로고
    • FLN29 deficiency reveals its negative regulatory role in the Toll-like receptor (TLR) and retinoic acid-inducible gene i (RIG-I)-like helicase signaling pathway
    • Sanada T, Takaesu G, Mashima R, et al. FLN29 deficiency reveals its negative regulatory role in the Toll-like receptor (TLR) and retinoic acid-inducible gene I (RIG-I)-like helicase signaling pathway. J Biol Chem 2008;283:33858-64.
    • (2008) J Biol Chem , vol.283 , pp. 33858-33864
    • Sanada, T.1    Takaesu, G.2    Mashima, R.3
  • 24
    • 78049497262 scopus 로고    scopus 로고
    • The proteasome inhibitor bortezomib drastically affects inflammation and bone disease in adjuvant-induced arthritis in rats
    • Yannaki E, Papadopoulou A, Athanasiou E, et al. The proteasome inhibitor bortezomib drastically affects inflammation and bone disease in adjuvant-induced arthritis in rats. Arthritis Rheum 2010;62:3277-88.
    • (2010) Arthritis Rheum , vol.62 , pp. 3277-3288
    • Yannaki, E.1    Papadopoulou, A.2    Athanasiou, E.3
  • 25
    • 84887329412 scopus 로고    scopus 로고
    • Effects of a proteasome inhibitor on the NF-kappaB signalling pathway in experimental osteoarthritis
    • Quan R, Huang Z, Yue Z, et al. Effects of a proteasome inhibitor on the NF-kappaB signalling pathway in experimental osteoarthritis. Scand J Rheumatol 2013;42:400-7.
    • (2013) Scand J Rheumatol , vol.42 , pp. 400-407
    • Quan, R.1    Huang, Z.2    Yue, Z.3
  • 26
    • 0027980321 scopus 로고
    • The ubiquitin-proteasome pathway is required for processing the NF-kappa B1 precursor protein and the activation of NF-kappa B
    • Palombella VJ, Rando OJ, Goldberg AL, et al. The ubiquitin-proteasome pathway is required for processing the NF-kappa B1 precursor protein and the activation of NF-kappa B. Cell 1994;78:773-85.
    • (1994) Cell , vol.78 , pp. 773-785
    • Palombella, V.J.1    Rando, O.J.2    Goldberg, A.L.3
  • 27
    • 84858725584 scopus 로고    scopus 로고
    • Regulation of NF-kappaB by deubiquitinases
    • Harhaj EW, Dixit VM. Regulation of NF-kappaB by deubiquitinases. Immunol Rev 2012;246:107-24.
    • (2012) Immunol Rev , vol.246 , pp. 107-124
    • Harhaj, E.W.1    Dixit, V.M.2
  • 28
    • 79952843826 scopus 로고    scopus 로고
    • The role of ubiquitin in autophagy-dependent protein aggregate processing
    • Yao TP. The role of ubiquitin in autophagy-dependent protein aggregate processing. Genes Cancer 2010;1:779-86.
    • (2010) Genes Cancer , vol.1 , pp. 779-786
    • Yao, T.P.1
  • 29
    • 77649128750 scopus 로고    scopus 로고
    • Autophagy is a protective mechanism in normal cartilage, and its aging-related loss is linked with cell death and osteoarthritis
    • Carames B, Taniguchi N, Otsuki S, et al. Autophagy is a protective mechanism in normal cartilage, and its aging-related loss is linked with cell death and osteoarthritis. Arthritis Rheum 2010;62:791-801.
    • (2010) Arthritis Rheum , vol.62 , pp. 791-801
    • Carames, B.1    Taniguchi, N.2    Otsuki, S.3
  • 30
    • 77953715170 scopus 로고    scopus 로고
    • Regulatory mechanisms involved in the control of ubiquitin homeostasis
    • Kimura Y, Tanaka K. Regulatory mechanisms involved in the control of ubiquitin homeostasis. J Biochem 2010;147:793-8.
    • (2010) J Biochem , vol.147 , pp. 793-798
    • Kimura, Y.1    Tanaka, K.2
  • 31
    • 38949205532 scopus 로고    scopus 로고
    • Suppression of early experimental osteoarthritis by in vivo delivery of the adenoviral vector-mediated NF-kappaBp65-specific siRNA
    • Chen LX, Lin L, Wang HJ, et al. Suppression of early experimental osteoarthritis by in vivo delivery of the adenoviral vector-mediated NF-kappaBp65-specific siRNA. Osteoarthritis Cartilage 2008;16:174-84.
    • (2008) Osteoarthritis Cartilage , vol.16 , pp. 174-184
    • Chen, L.X.1    Lin, L.2    Wang, H.J.3
  • 33
    • 65349083779 scopus 로고    scopus 로고
    • Biomechanical thresholds regulate inflammation through the NF-kappaB pathway: Experiments and modeling
    • Nam J, Aguda BD, Rath B, et al. Biomechanical thresholds regulate inflammation through the NF-kappaB pathway: experiments and modeling. PLoS ONE 2009;4:e5262.
    • (2009) PLoS ONE , vol.4 , pp. e5262
    • Nam, J.1    Aguda, B.D.2    Rath, B.3
  • 34
    • 84863226474 scopus 로고    scopus 로고
    • Joint immobilization prevents murine osteoarthritis and reveals the highly mechanosensitive nature of protease expression in vivo
    • Burleigh A, Chanalaris A, Gardiner MD, et al. Joint immobilization prevents murine osteoarthritis and reveals the highly mechanosensitive nature of protease expression in vivo. Arthritis Rheum 2012;64:2278-88.
    • (2012) Arthritis Rheum , vol.64 , pp. 2278-2288
    • Burleigh, A.1    Chanalaris, A.2    Gardiner, M.D.3
  • 35
    • 84859445754 scopus 로고    scopus 로고
    • Age-dependent alteration of TGF-beta signalling in osteoarthritis
    • van der Kraan PM, Goumans MJ, Blaney Davidson E, et al. Age-dependent alteration of TGF-beta signalling in osteoarthritis. Cell Tissue Res 2012;347:257-65.
    • (2012) Cell Tissue Res , vol.347 , pp. 257-265
    • Van Der Kraan, P.M.1    Goumans, M.J.2    Blaney Davidson, E.3
  • 36
    • 84870653657 scopus 로고    scopus 로고
    • Cartilage development and degeneration: A Wnt Wnt situation
    • Staines KA, Macrae VE, Farquharson C. Cartilage development and degeneration: a Wnt Wnt situation. Cell Biochem Funct 2012;30:633-42.
    • (2012) Cell Biochem Funct , vol.30 , pp. 633-642
    • Staines, K.A.1    Macrae, V.E.2    Farquharson, C.3
  • 37
    • 82455179484 scopus 로고    scopus 로고
    • Systematic and quantitative assessment of the ubiquitin-modified proteome
    • Kim W, Bennett EJ, Huttlin EL, et al. Systematic and quantitative assessment of the ubiquitin-modified proteome. Mol Cell 2011;44:325-40.
    • (2011) Mol Cell , vol.44 , pp. 325-340
    • Kim, W.1    Bennett, E.J.2    Huttlin, E.L.3
  • 38
    • 84867103151 scopus 로고    scopus 로고
    • Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues
    • Wagner SA, Beli P, Weinert BT, et al. Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues. Mol Cell Proteomics 2012;11:1578-85.
    • (2012) Mol Cell Proteomics , vol.11 , pp. 1578-1585
    • Wagner, S.A.1    Beli, P.2    Weinert, B.T.3
  • 39
    • 84857047339 scopus 로고    scopus 로고
    • PhosphoSitePlus: A comprehensive resource for investigating the structure and function of experimentally determined post-translational modifications in man and mouse
    • Hornbeck PV, Kornhauser JM, Tkachev S, et al. PhosphoSitePlus: a comprehensive resource for investigating the structure and function of experimentally determined post-translational modifications in man and mouse. Nucleic Acids Res 2012;40:D261-70.
    • (2012) Nucleic Acids Res , vol.40 , pp. D261-D270
    • Hornbeck, P.V.1    Kornhauser, J.M.2    Tkachev, S.3
  • 40
    • 29244467708 scopus 로고    scopus 로고
    • FLN29, a novel interferon- and LPS-inducible gene acting as a negative regulator of toll-like receptor signaling
    • Mashima R, Saeki K, Aki D, et al. FLN29, a novel interferon- and LPS-inducible gene acting as a negative regulator of toll-like receptor signaling. J Biol Chem 2005;280:41289-97.
    • (2005) J Biol Chem , vol.280 , pp. 41289-41297
    • Mashima, R.1    Saeki, K.2    Aki, D.3
  • 41
    • 84885186818 scopus 로고    scopus 로고
    • Regulation of matrixmetalloproteinase-3 and matrixmetalloproteinase-13 by SUMO-2/3 through the transcription factor NF-kappaB
    • Frank S, Peters MA, Wehmeyer C, et al. Regulation of matrixmetalloproteinase-3 and matrixmetalloproteinase-13 by SUMO-2/3 through the transcription factor NF-kappaB. Ann Rheum Dis 2013;72:1874-81.
    • (2013) Ann Rheum Dis , vol.72 , pp. 1874-1881
    • Frank, S.1    Peters, M.A.2    Wehmeyer, C.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.