ADAMTS-1 cleaves a cartilage proteoglycan, aggrecan (Q28142856)

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Y Okada

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H Kawashima

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H Nakamura

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M Miyasaka

5

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H Ohno

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K Matsushima

ADAM, a novel family of membrane proteins containing A Disintegrin And Metalloprotease domain: multipotential functions in cell-cell and cell-matrix interactions

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language of work or name

English

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publication date

4 August 2000

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published in

FEBS Letters

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volume

478

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issue

3

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page(s)

241-5

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cites work

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ADAMTS-1 protein anchors at the extracellular matrix through the thrombospondin type I motifs and its spacing region

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ADAMTS-1 is an active metalloproteinase associated with the extracellular matrix

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METH-1, a human ortholog of ADAMTS-1, and METH-2 are members of a new family of proteins with angio-inhibitory activity

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The role of link-protein in the structure of cartilage proteoglycan aggregates

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N-terminal sequence of proteoglycan fragments isolated from medium of interleukin-1-treated articular-cartilage cultures. Putative site(s) of enzymic cleavage

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Catabolism of aggrecan by explant cultures of human articular cartilage in the presence of retinoic acid

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Cell-mediated catabolism of aggrecan. Evidence that cleavage at the "aggrecanase" site (Glu373-Ala374) is a primary event in proteolysis of the interglobular domain

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The structure of aggrecan fragments in human synovial fluid. Evidence for the involvement in osteoarthritis of a novel proteinase which cleaves the Glu 373-Ala 374 bond of the interglobular domain

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Aggrecan degradation in human cartilage. Evidence for both matrix metalloproteinase and aggrecanase activity in normal, osteoarthritic, and rheumatoid joints

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Purification and cloning of aggrecanase-1: a member of the ADAMTS family of proteins

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Cloning and characterization of ADAMTS11, an aggrecanase from the ADAMTS family

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cDNA cloning and expression of bovine procollagen I N-proteinase: a new member of the superfamily of zinc-metalloproteinases with binding sites for cells and other matrix components.

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ADAMTS: a novel family of proteases with an ADAM protease domain and thrombospondin 1 repeats

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Expression of ADAMTS homologues in articular cartilage

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The ins and outs of aggrecan

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Generation and characterization of aggrecanase. A soluble, cartilage-derived aggrecan-degrading activity

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The structure of aggrecan fragments in human synovial fluid. Evidence that aggrecanase mediates cartilage degradation in inflammatory joint disease, joint injury, and osteoarthritis

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