Expression of ADAMTS-1, ADAMTS-4, ADAMTS-5 and TIMP3 by hepatocellular carcinoma cell lines

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Expression of ADAMTS-1, ADAMTS-4, ADAMTS-5 and TIMP3 by hepatocellular carcinoma cell lines.

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...

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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...

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Matrilin-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...

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Aggrecan 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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ADAMTS Expression in Colorectal Cancer

ADAMTSs are a family of secreted proteinases that share the metalloproteinase domain with matrix metalloproteinases (MMPs). By acting on a large panel of extracellular substrates, they control several cell functions such as fusion, adhesion, proliferation and migration. Through their thrombospondin motifs they also possess anti-angiogenic properties. We investigated whether ADAMTSs participate ...

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ژورنال

عنوان ژورنال: International Journal of Oncology

سال: 2012

ISSN: 1019-6439,1791-2423

DOI: 10.3892/ijo.2012.1525