Nurminskaya et al., Baltimore, United States. In Arterioscler Thromb Vasc Biol, 2012
Warfarin-induced calcification in A10 vascular smooth muscle cells is associated with the activation of beta-catenin signaling. Vascular cells with genetically or pharmacologically reduced TG2 activity fail to activate beta-catenin in response to warfarin.
Hitomi et al., Nagoya, Japan. In Cytotechnology, 2011
In this study, we have established a novel screening system that enables identification of cDNA sequence encoding favorable primary structure as a substrate for tissue-type transglutaminase (TGase 2), a multifunctional and ubiquitously expressing isozyme.
Bakker et al., Amsterdam, Netherlands. In Am J Pathol, 2009
Sections of the carotid artery specimens were registered to micro-computed tomography images and stained for tissue-type transglutaminase, plasma transglutaminase factor XIIIA (FXIIIA), the N(epsilon)(gamma-glutamyl)lysine cross-link, and the macrophage marker CD68.
Zheng et al., Beijing, China. In Hypertension, 2009
Tissue-typetransglutaminase (tTG) may actasa positive regulator of the hypertrophic program in response to ET-1. This is attributable to signaling activity of tTG rather than transglutaminase activity.
Mehta et al., Houston, United States. In Curr Cancer Drug Targets, 2007
Like NF-kappaB, tissue-type transglutaminase (TG2), the most diverse and ubiquitous member of the calcium-dependent transglutaminase family of enzymes, is also aberrantly overexpressed in many human cancer types, blocks apoptosis, and promotes drug resistance and metastatic phenotypes.