Cloning and Characterization of ADAMTS-14, a Novel ADAMTS Displaying High Homology with ADAMTS-2 and ADAMTS-3

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...

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...

ADAMTS evolution and structure

Members of the ADAMTS (a disintegrin and metalloproteinase with thrombospondin motifs) family are known to influence development, angiogenesis, coagulation and progression of arthritis. As proteinases their substrates include the von Willebrand factor precursor and extracellular matrix components such as procollagen, hyalectans (hyaluronan-binding proteoglycans including aggrecan), decorin, fib...

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...

ADAMTS revenge on Eve?