The interglobular domain of cartilage aggrecan is cleaved by PUMP, gelatinases, and cathepsin B.
TLDR
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.About:
This article is published in Journal of Biological Chemistry.The article was published on 1992-09-25 and is currently open access. It has received 292 citations till now. The article focuses on the topics: ADAMTS4 Protein & Cartilage metabolism.read more
Citations
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Journal ArticleDOI
Matrix metalloproteinases: role in arthritis.
TL;DR: Increasing knowledge of the crystal structures of these enzymes and of the signal transduction pathways and molecular mechanisms that control MMP gene expression may provide new opportunities for the development of therapeutics to prevent the joint destruction seen in arthritis.
Journal ArticleDOI
Biochemistry and Molecular Biology of Gelatinase B or Matrix Metalloproteinase-9 (MMP-9)
Philippe E. Van den Steen,Bénédicte Dubois,Inge Nelissen,Pauline M. Rudd,Raymond A. Dwek,Ghislain Opdenakker +5 more
TL;DR: The ability of gelatinase B to degrade components of the extracellular matrix and to regulate the activity of a number of soluble proteins confers an important role in various physiological and pathological processes, including reproduction, growth, development, inflammation, and vascular and proliferative diseases.
Journal ArticleDOI
Neutrophil gelatinase B potentiates interleukin-8 tenfold by aminoterminal processing, whereas it degrades CTAP-III, PF-4, and GRO-α and leaves RANTES and MCP-2 intact
TL;DR: A better understanding of regulator (IL-8) and effector molecules (gelatinase B) of neutrophils and of mechanisms underlying leukocytosis, shock syndromes, and stem cell mobilization by IL-8 is led to.
Journal ArticleDOI
Gelatinase-mediated migration and invasion of cancer cells.
Mikael Björklund,Erkki Koivunen +1 more
TL;DR: Inhibition of the association of the gelatinases with cell-surface integrins appears to offer highly specific means to target these enzymes without inhibiting their catalytic activity in multiple cell types including endothelial cells, tumor cells and leukocytes.
Journal ArticleDOI
Structure and function of aggrecan
TL;DR: ABSTRACTAggrecan is the major proteoglycan in the articular cartilage because it provides a hydrated gel structure (via its interaction with hyaluronan and link protein) that endows the cartilage with load-bearing properties and is crucial in chondroskeletal morphogenesis during development.
References
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Electrophoretic analysis of the major polypeptides of the human erythrocyte membrane.
Journal ArticleDOI
Silver stain for proteins in polyacrylamide gels: A modified procedure with enhanced uniform sensitivity
TL;DR: It was found that treatment of gels with dithiothreitol prior to impregnation with silver nitrate results in more reproducible staining patterns that are also qualitatively similar to those obtained with Coomassie blue.
Book ChapterDOI
Cathepsin B, Cathepsin H, and cathepsin L.
Alan J. Barrett,Heidrun Kirschke +1 more
TL;DR: Two types of purification methods for Cathepsin B, CathePSin H, and Cathepsypsin L are described: method I is applicable to large amounts of frozen tissues, whereas method II is used with flesh tissue and takes advantage of a 50-fold purification factor attainable by isolation of lysosomes.
Journal ArticleDOI
Matrix metalloproteinase 3 (stromelysin) activates the precursor for the human matrix metalloproteinase 9.
TL;DR: The results imply that MMP-3 may be an effective activator of proMMP-9 in vivo, and is the first example of zymogen activation that can be triggered by another member of the MMP family.
Journal ArticleDOI
Matrix metalloproteinase degradation of elastin, type IV collagen and proteoglycan. A quantitative comparison of the activities of 95 kDa and 72 kDa gelatinases, stromelysins-1 and -2 and punctuated metalloproteinase (PUMP).
TL;DR: All of the enzymes studied degraded soluble native type IV collagen, but the gelatinases were more effective at higher temperatures, and the PUMP and the stromelysins were more potent proteoglycan-degrading enzymes.
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