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Articular Cartilage and Osteoarthritis.
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Degradation of cartilage aggrecan by collagenase‐3 (MMP‐13)
The results show that MMP‐13 cleaves aggrecan in the IGD at the same site (PEN341‐FFG..) identified for other members of the MMP family, and also at a novel site ..VKP384‐VFE.. not previously observed for other proteinases. Expand
The interglobular domain of cartilage aggrecan is cleaved by PUMP, gelatinases, and cathepsin B.
Investigation on aggrecan the major proteoglycan of cartilage shows that in spite of a high keratan sulfate content the interglobular domain provides important sites for cleavage by different proteinases, including several members of the matrix metalloproteinase family. Expand
Identification and Characterization of Asporin
The deduced amino acid sequence of asporin was confirmed by mass spectrometry of the isolated protein resulting in 84% sequence coverage and reflects the aspartate-rich amino terminus and the overall similarity to decorin. Expand
The structure of a 38-kDa leucine-rich protein (chondroadherin) isolated from bovine cartilage.
A leucine-rich protein, chondroadherin, has been isolated from dissociative extracts of articular cartilage, and its primary structure has been determined by both direct protein sequencing and DNAExpand
The structure of aggrecan fragments in human synovial fluid. Evidence that aggrecanase mediates cartilage degradation in inflammatory joint disease, joint injury, and osteoarthritis.
The consistent pattern of fragments seen on SDS-PAGE and the single predominant N-terminal sequence suggest a common degradative mechanism of aggrecan in these different joint conditions, which appear to have important implications with regard to the development of therapies to protect cartilage from degradation in patients with joint disease. Expand
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.
It is concluded that the release of aggrecan fragments from articular cartilage into the synovial fluid seen at all stages of human osteoarthritis is promoted by the action of a normal cartilage proteinase which cleaves the Glu 373-Ala 374 bond of the interglobular domain. Expand
Catabolism of aggrecan in cartilage explants. Identification of a major cleavage site within the interglobular domain.
Results indicate that catabolism of aggrecan in cartilage explants involves proteolytic cleavage within a conserved region of the interglobular domain and that this results in the separation of the G1 domain from the remainder of the molecule. Expand
The isolation and primary structure of a 22-kDa extracellular matrix protein from bovine skin.
The primary structure of a 22-kDa protein which was isolated during the purification of bovine skin dermatan sulfate proteoglycan is described and found to contain three repeat regions which may be involved in associations of the molecule with other extracellular matrix components. Expand
Characterization of the dermatan sulfate proteoglycans, DS-PGI and DS-PGII, from bovine articular cartilage and skin isolated by octyl-sepharose chromatography.
Two forms of dermatan sulfate proteoglycans, called DS-PGI and DS-PGII, have been isolated from both bovine fetal skin and calf articular cartilage and characterized. The proteoglycans were isolatedExpand