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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Cloning and characterization of ADAMTS11, an aggrecanase from the ADAMTS familySites of aggrecan cleavage by recombinant human aggrecanase-1 (ADAMTS-4)Proprotein convertase furin interacts with and cleaves pro-ADAMTS4 (Aggrecanase-1) in the trans-Golgi networkNeutrophil collagenase (MMP-8) cleaves at the aggrecanase site E373-A374 in the interglobular domain of cartilage aggrecanAge-related changes in the content of the C-terminal region of aggrecan in human articular cartilageAggrecanases and cartilage matrix degradationArticular cartilage and changes in arthritis: matrix degradation.ADAMTS-1 cleaves a cartilage proteoglycan, aggrecanAggrecanase versus matrix metalloproteinases in the catabolism of the interglobular domain of aggrecan in vitro.Pathologic indicators of degradation and inflammation in human osteoarthritic cartilage are abrogated by exposure to n-3 fatty acids.Effect of IL-1beta-induced macromolecular depletion on residual quadrupolar interaction in articular cartilageThe thrombospondin motif of aggrecanase-1 (ADAMTS-4) is critical for aggrecan substrate recognition and cleavage.Articular cartilage and osteoarthrosis. The role of molecular markers to monitor breakdown, repair and disease.Inhibition of ADAM-TS4 and ADAM-TS5 prevents aggrecan degradation in osteoarthritic cartilage.ADAMTS4 (aggrecanase-1) activation on the cell surface involves C-terminal cleavage by glycosylphosphatidyl inositol-anchored membrane type 4-matrix metalloproteinase and binding of the activated proteinase to chondroitin sulfate and heparan sulfateADAMTS-5 deficiency does not block aggrecanolysis at preferred cleavage sites in the chondroitin sulfate-rich region of aggrecan.MMPs are less efficient than ADAMTS5 in cleaving aggrecan core protein.Chondrocyte-mediated catabolism of aggrecan: aggrecanase-dependent cleavage induced by interleukin-1 or retinoic acid can be inhibited by glucosamine.Involvement of ADAMTS5 and hyaluronidase in aggrecan degradation and release from OSM-stimulated cartilageBlocking aggrecanase cleavage in the aggrecan interglobular domain abrogates cartilage erosion and promotes cartilage repairA Disintegrin and Metalloproteinase with Thrombospondin Motifs-5 (ADAMTS-5) Forms Catalytically Active OligomersMembrane type 1 matrix metalloproteinase (MT1-MMP) cleaves the recombinant aggrecan substrate rAgg1mut at the 'aggrecanase' and the MMP sites. Characterization of MT1-MMP catabolic activities on the interglobular domain of aggrecan.Recent progress in understanding molecular mechanisms of cartilage degeneration during osteoarthritis.Aggrecan is degraded by matrix metalloproteinases in human arthritis. Evidence that matrix metalloproteinase and aggrecanase activities can be independent.Aggrecan degradation in human cartilage. Evidence for both matrix metalloproteinase and aggrecanase activity in normal, osteoarthritic, and rheumatoid joints.Suppression of aggrecanase: a novel protective mechanism of dehydroepiandrosterone in osteoarthritis?Mutations in the interglobular domain of aggrecan alter matrix metalloproteinase and aggrecanase cleavage patterns. Evidence that matrix metalloproteinase cleavage interferes with aggrecanase activity.Aggrecan: A Target Molecule of Autoimmune Reactions.Alpha2-macroglobulin is a novel substrate for ADAMTS-4 and ADAMTS-5 and represents an endogenous inhibitor of these enzymes."Aggrecanase" activity is implicated in tumour necrosis factor alpha mediated cartilage aggrecan breakdown but is not detected by an in vitro assay.Proteolytic mechanisms of cartilage breakdown: a target for arthritis therapy?Cell-mediated catabolism of aggrecan. Evidence that cleavage at the "aggrecanase" site (Glu373-Ala374) is a primary event in proteolysis of the interglobular domain.Changes in cartilage proteoglycan aggrecan after intra-articular injection of interleukin-1 in rabbits: studies of synovial fluid and articular cartilage.Variations in aggrecan structure modulate its susceptibility to aggrecanases.Proteoglycans isolated from dissociative extracts of differently aged human articular cartilage: characterization of naturally occurring hyaluronan-binding fragments of aggrecanDevelopment of a cleavage-site-specific monoclonal antibody for detecting metalloproteinase-derived aggrecan fragments: detection of fragments in human synovial fluids.Monoclonal antibodies that specifically recognize neoepitope sequences generated by 'aggrecanase' and matrix metalloproteinase cleavage of aggrecan: application to catabolism in situ and in vitro.Inhibition of bovine nasal cartilage degradation by selective matrix metalloproteinase inhibitors.Aggrecan degradation in human intervertebral disc and articular cartilage.An aggrecan-degrading activity associated with chondrocyte membranes.
P2860
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P2860
N-terminal sequence of proteoglycan fragments isolated from medium of interleukin-1-treated articular-cartilage cultures. Putative site(s) of enzymic cleavage.
description
1992 nî lūn-bûn
@nan
1992年の論文
@ja
1992年論文
@yue
1992年論文
@zh-hant
1992年論文
@zh-hk
1992年論文
@zh-mo
1992年論文
@zh-tw
1992年论文
@wuu
1992年论文
@zh
1992年论文
@zh-cn
name
N-terminal sequence of proteog ...... tilage cultures. Putative site
@nl
N-terminal sequence of proteog ...... e site(s) of enzymic cleavage.
@en
type
label
N-terminal sequence of proteog ...... tilage cultures. Putative site
@nl
N-terminal sequence of proteog ...... e site(s) of enzymic cleavage.
@en
prefLabel
N-terminal sequence of proteog ...... tilage cultures. Putative site
@nl
N-terminal sequence of proteog ...... e site(s) of enzymic cleavage.
@en
P2093
P2860
P356
P1433
P1476
N-terminal sequence of proteog ...... e site(s) of enzymic cleavage.
@en
P2093
Loulakis P
Maniglia CA
Shrikhande A
P2860
P304
P356
10.1042/BJ2840589
P407
P478
284 ( Pt 2)
P577
1992-06-01T00:00:00Z