ADAMTS-9 in Mouse Cartilage Has Aggrecanase Activity That Is Distinct from ADAMTS-4 and ADAMTS-5
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چکیده
منابع مشابه
A Patient 1 Patient 2 B ADAMTS 4 ADAMTS 5 GAPDH ADAMTS 4 ADAMTS 5 GAPDH
1Department of Rheumatology, Cardiff University and 2Connective Tissue Biology Laboratories, Cardiff School of Biosciences, Cardiff University, Cardiff, UK. Jan Bondeson, MD PhD; Shane Wainwright, PhD; Clare Hughes, PhD; Bruce Caterson PhD. This work has been supported by the Arthritis Research Campaign (UK), grants no. W0596, 13172 and 14570. Please address correspondence to: Prof. Bruce Cater...
متن کاملAggrecan degradation in human articular cartilage explants is mediated by both ADAMTS-4 and ADAMTS-5.
OBJECTIVE Recent published studies have shown that cartilage from ADAMTS-5-knockout mice, but not ADAMTS-4- or ADAMTS-1-knockout mice, is significantly protected from degradation. The present study was undertaken to evaluate the respective roles of these enzymes in human cartilage breakdown, using a small interfering RNA (siRNA) approach to assess the effects of inhibition of each enzyme in nor...
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Little is known about the expression or role of ADAMTS-1, -4 and -5 and their endogenous inhibitor TIMP3 in the liver in physiological and pathological conditions. Their expression was, therefore, investigated in the hepatocellular carcinoma cell lines HepG2 and HuH-7 using qRT-PCR and western blotting, and their cellular localisation by immunocytochemistry. Cytokine treatments were used to ass...
متن کاملMatrilin-2 is proteolytically cleaved by ADAMTS-4 and ADAMTS-5.
Matrilin-2 is a widely distributed, oligomeric extracellular matrix protein that forms a filamentous network by binding to a variety of different extracellular matrix proteins. We found matrilin-2 proteolytic products in transfected cell lines in vitro and in mouse tissues in vivo. Two putative cleavage sites were identified in the unique domain of matrilin-2; the first site was located between...
متن کاملAntibody-based exosite inhibitors of ADAMTS-5 (aggrecanase-2)
Adamalysin-like metalloproteinases with thrombospondin (TS) motifs (ADAMTS)-5 is the multi-domain metalloproteinase that most potently degrades aggrecan proteoglycan in the cartilage and its activity is implicated in the development of osteoarthritis (OA). To generate specific exosite inhibitors for it, we screened a phage display antibody library in the presence of the zinc-chelating active si...
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ژورنال
عنوان ژورنال: International Journal of Molecular Sciences
سال: 2019
ISSN: 1422-0067
DOI: 10.3390/ijms20030573