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Degradation of cartilage aggrecan by collagenase‐3 (MMP‐13)
Degradation of the large cartilage proteoglycan aggrecan in arthritis involves an unidentified enzyme aggrecanase, and at least one of the matrix metalloproteinases. Proteinase‐sensitive cleavageExpand
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The interglobular domain of cartilage aggrecan is cleaved by PUMP, gelatinases, and cathepsin B.
The action of three matrix metalloproteinases (MMPs), 72- and 95-kDa gelatinases (MMP-2 and MMP-9) and PUMP (MMP-7), and a cysteine proteinase, cathepsin B, were investigated on aggrecan the majorExpand
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Identification and Characterization of Asporin
Asporin, a novel member of the leucine-rich repeat family of proteins, was partially purified from human articular cartilage and meniscus. Cloning of human and mouse asporin cDNAs revealed that theExpand
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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
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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.
Synovial fluid was collected from patients with recent knee injury and from patients with early or late stage osteoarthritis. Chondroitin sulfate-substituted aggrecan fragments present in theseExpand
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Catabolism of aggrecan in cartilage explants. Identification of a major cleavage site within the interglobular domain.
The catabolism of aggrecan has been studied in calf articular cartilage explant cultures. The chondroitin sulfate-rich, high buoyant density products that accumulate in culture medium have beenExpand
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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
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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. The uronate-rich fraction from DEAE-SepharoseExpand
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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.
OBJECTIVE To determine the proteolytic fragmentation patterns and N-terminal sequence of aggrecan fragments in human synovial fluid from patients with inflammatory arthritides, joint injury, orExpand
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Cleavage of cartilage proteoglycan between G1 and G2 domains by stromelysins.
Normal and pathological turnover of proteoglycans in articular cartilage involves its cleavage close to the N-terminal G1 domain responsible for aggregation. A fragment containing G1 and G2Expand
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