Cleavage of cartilage proteoglycan between G1 and G2 domains by stromelysins.
about
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 domainFibroblast and neutrophil collagenases cleave at two sites in the cartilage aggrecan interglobular domainMatrix metalloproteinases cleave at two distinct sites on human cartilage link proteinNeutrophil collagenase (MMP-8) cleaves at the aggrecanase site E373-A374 in the interglobular domain of cartilage aggrecanAggrecanases and cartilage matrix degradationAggrecanase versus matrix metalloproteinases in the catabolism of the interglobular domain of aggrecan in vitro.Proteoglycan depletion and size reduction in lesions of early grade chondromalacia of the patellaMetabolism of cartilage proteoglycans in health and diseaseArticular cartilage and osteoarthrosis. The role of molecular markers to monitor breakdown, repair and disease.VDIPEN, a metalloproteinase-generated neoepitope, is induced and immunolocalized in articular cartilage during inflammatory arthritis.MMPs are less efficient than ADAMTS5 in cleaving aggrecan core protein.Engineering of tissue inhibitor of metalloproteinases mutants as potential therapeuticsProteases involved in cartilage matrix degradation in osteoarthritis.Recent findings on the role of gelatinases (matrix metalloproteinase-2 and -9) in osteoarthritisSerum matrix metalloproteinase-3 levels correlate with disease activity in relapsing-remitting multiple sclerosis.Membrane 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.Mast cell-restricted, tetramer-forming tryptases induce aggrecanolysis in articular cartilage by activating matrix metalloproteinase-3 and -13 zymogensAggrecan 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.Curcumin reduces prostaglandin E2, matrix metalloproteinase-3 and proteoglycan release in the secretome of interleukin 1β-treated articular cartilageAnalysing the role of endogenous matrix molecules in the development of osteoarthritis.Hyaluronan-binding region of aggrecan from pig laryngeal cartilage. Amino acid sequence, analysis of N-linked oligosaccharides and location of the keratan sulphate.Current and emerging therapeutic strategies for preventing inflammation and aggrecanase-mediated cartilage destruction in arthritis.Proteolytic mechanisms of cartilage breakdown: a target for arthritis therapy?Inhibitors of collagenase but not of gelatinase reduce cartilage explant proteoglycan breakdown despite only low levels of matrix metalloproteinase activity.Inhibition of interleukin 1 beta induced rat and human cartilage degradation in vitro by the metalloproteinase inhibitor U27391.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.Mouse aggrecan, a large cartilage proteoglycan: protein sequence, gene structure and promoter sequence.Increased vulnerability of postarthritic cartilage to a second arthritic insult: accelerated MMP activity in a flare up of arthritis.Characterization of proteoglycans isolated from associative extracts of human articular cartilage.Monoclonal antibodies that specifically recognize neoepitope sequences generated by 'aggrecanase' and matrix metalloproteinase cleavage of aggrecan: application to catabolism in situ and in vitro.Quantification of a matrix metalloproteinase-generated aggrecan G1 fragment using monospecific anti-peptide serum.Metalloproteinase digestion of cartilage proteoglycan. Pattern of cleavage by stromelysin and susceptibility to collagenase.Inhibition of bovine nasal cartilage degradation by selective matrix metalloproteinase inhibitors.An aggrecan fragment drives osteoarthritis pain through Toll-like receptor 2.
P2860
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P2860
Cleavage of cartilage proteoglycan between G1 and G2 domains by stromelysins.
description
1991 nî lūn-bûn
@nan
1991 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
1991 թվականի օգոստոսին հրատարակված գիտական հոդված
@hy
1991年の論文
@ja
1991年論文
@yue
1991年論文
@zh-hant
1991年論文
@zh-hk
1991年論文
@zh-mo
1991年論文
@zh-tw
1991年论文
@wuu
name
Cleavage of cartilage proteoglycan between G1 and G2 domains by stromelysins.
@ast
Cleavage of cartilage proteoglycan between G1 and G2 domains by stromelysins.
@en
Cleavage of cartilage proteoglycan between G1 and G2 domains by stromelysins.
@nl
type
label
Cleavage of cartilage proteoglycan between G1 and G2 domains by stromelysins.
@ast
Cleavage of cartilage proteoglycan between G1 and G2 domains by stromelysins.
@en
Cleavage of cartilage proteoglycan between G1 and G2 domains by stromelysins.
@nl
prefLabel
Cleavage of cartilage proteoglycan between G1 and G2 domains by stromelysins.
@ast
Cleavage of cartilage proteoglycan between G1 and G2 domains by stromelysins.
@en
Cleavage of cartilage proteoglycan between G1 and G2 domains by stromelysins.
@nl
P2093
P1476
Cleavage of cartilage proteoglycan between G1 and G2 domains by stromelysins.
@en
P2093
P304
15579-15582
P407
P577
1991-08-01T00:00:00Z