Abstract：
:Interleukin-1 (IL-1) is the major prototypic proinflammatory cytokine that stimulates degradation of cartilage in arthritis by inducing prominent collagen II-degrading matrix metalloproteinase-13 (MMP-13). Nothing is known about the involvement of adaptor proteins, MyD88, IRAK1 and TRAF6 in MMP-13 regulation. Here we investigated for the first time the role of these proteins in IL-1-regulated MMP-13 expression in chondrocytes. MyD88 homodimerization inhibitory peptide diminished the expression of MMP-13 gene, promoter activity, phosphorylation of mitogen-activated protein kinases (MAPKs), c-Jun and activating protein 1 (AP-1) activity. Knockdown of MyD88, IRAK1 and TRAF6 by RNA interference (RNAi) drastically down-regulated the expression of IL-1-induced MMP-13 mRNA and protein levels and MMP-13 promoter-driven luciferase activity. Non-specific control siRNA had no effect. Mechanisms of MMP-13 inhibition involved reduced phosphorylation of ERK, p38, JNK and c-Jun as well as AP-1 transcription factor binding activity. The genetic evidence presented here demonstrates that MyD88, IRAK1 and TRAF6 proteins are crucial early mediators for the IL-1-induced MMP-13 regulation through MAPK pathways and AP-1 activity. These proteins could constitute important therapeutic targets for arthritis-associated cartilage loss by MMP-13.
journal_name
Cell Signaljournal_title
Cellular signallingauthors
Ahmad R,Sylvester J,Zafarullah Mdoi
10.1016/j.cellsig.2007.08.013subject
Has Abstractpub_date
2007-12-01 00:00:00pages
2549-57issue
12eissn
0898-6568issn
1873-3913pii
S0898-6568(07)00255-0journal_volume
19pub_type
杂志文章abstract：:The focal adhesion kinase Pyk2 integrates signals from cell adhesion receptors, growth factor receptors, and G-protein-coupled receptors leading to the activation of intracellular signaling pathways that regulate cellular phenotypes. The intrinsic mechanism for the activation of Pyk2 activity remains to be fully defin...
journal_title：Cellular signalling
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journal_title：Cellular signalling
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pub_type： 杂志文章
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journal_title：Cellular signalling
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journal_title：Cellular signalling
pub_type： 杂志文章
doi：10.1016/j.cellsig.2008.06.013
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abstract：:Epstein-Barr virus (EBV) encoded latent membrane protein 1 (LMP1) is essential for the immortalization of human B cells and is linked etiologically to several human tumors. LMP1 is an integral membrane protein which acts like a constitutively active receptor. It binds tumor necrosis factor (TNF)-receptor-associated fa...
journal_title：Cellular signalling
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doi：10.1016/j.cellsig.2004.03.014
更新日期：2004-10-01 00:00:00
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doi：10.1016/j.cellsig.2008.05.001
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journal_title：Cellular signalling
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journal_title：Cellular signalling
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journal_title：Cellular signalling
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journal_title：Cellular signalling
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journal_title：Cellular signalling
pub_type： 杂志文章,评审
doi：10.1016/0898-6568(95)00024-j
更新日期：1995-08-01 00:00:00
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journal_title：Cellular signalling
pub_type： 杂志文章
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