Aggrecanases and TIMP-3 in osteoarthritis: structure, function and in vivo challenges

Aggrecanases and TIMP-3 in osteoarthritis: structure, function and in vivo challenges

Номзүйн дэлгэрэнгүй
Үндсэн зохиолч:	Nagase, H
Формат:	Journal article
Хэвлэсэн:	2009

Ижил төстэй зүйлс

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Aggrecanases in cartilage matrix breakdown
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Aggrecanases and cartilage matrix degradation.
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Microvesicles shed by oligodendroglioma cells and rheumatoid synovial fibroblasts contain aggrecanase activity
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Microvesicles shed by oligodendroglioma cells and rheumatoid synovial fibroblasts contain aggrecanase activity.
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LRP-dependent and -independent internalisation of TIMP-3
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Proteolytic fragments of fibronectin containing the type III-13 and III-14 repeats induce aggrecanase activity in cartilage
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Substrate conformation modulates aggrecanase (ADAMTS-4) affinity and sequence specificity. Suggestion of a common topological specificity for functionally diverse proteases.
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Characterisation of N-TIMP-3 mutants that selectively inhibit the ADAMTSs
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Endocytic pathways of TIMP-3 and its N-terminal inhibitory domain
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TIMP-3 inhibits the procollagen N-proteinase ADAMTS-2.
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Mannosamine inhibits aggrecanase-mediated degradation of the mechanically functional portion of proteoglycans and of the physical properties of articular cartilage
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THE TYPE III 8-10 REPEATS OF FIBRONECTIN INDUCE AGGRECANASE ACTIVITY VIA ALPHA5BETA1 INTEGRIN AND THE TYPE III 13-14 REPEATS ACT VIA TLR 4 RECEPTORS
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