Extracellular transglutaminase 2 is catalytically inactive, but is transiently activated upon tissue injury.

Transglutaminase 2 (TG2) is a multifunctional mammalian protein with transamidase and signaling properties. Using selective TG2 inhibitors and tagged nucleophilic amine substrates, we show that the majority of extracellular TG2 is inactive under normal physiological conditions in cell culture and in...

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Autores principales:	Matthew Siegel, Pavel Strnad, R Edward Watts, Kihang Choi, Bana Jabri, M Bishr Omary, Chaitan Khosla
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2008
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/5cf5c1b6f2524e95bdbec9e682de5187
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spelling	oai:doaj.org-article:5cf5c1b6f2524e95bdbec9e682de51872021-11-25T06:12:58ZExtracellular transglutaminase 2 is catalytically inactive, but is transiently activated upon tissue injury.1932-620310.1371/journal.pone.0001861https://doaj.org/article/5cf5c1b6f2524e95bdbec9e682de51872008-03-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/18365016/?tool=EBIhttps://doaj.org/toc/1932-6203Transglutaminase 2 (TG2) is a multifunctional mammalian protein with transamidase and signaling properties. Using selective TG2 inhibitors and tagged nucleophilic amine substrates, we show that the majority of extracellular TG2 is inactive under normal physiological conditions in cell culture and in vivo. However, abundant TG2 activity was detected around the wound in a standard cultured fibroblast scratch assay. To demonstrate wounding-induced activation of TG2 in vivo, the toll-like receptor 3 ligand, polyinosinic-polycytidylic acid (poly(I:C)), was injected in mice to trigger small intestinal injury. Although no TG2 activity was detected in vehicle-treated mice, acute poly(I:C) injury resulted in rapid TG2 activation in the small intestinal mucosa. Our findings provide a new basis for understanding the role of TG2 in physiology and disease.Matthew SiegelPavel StrnadR Edward WattsKihang ChoiBana JabriM Bishr OmaryChaitan KhoslaPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 3, Iss 3, p e1861 (2008)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Matthew Siegel Pavel Strnad R Edward Watts Kihang Choi Bana Jabri M Bishr Omary Chaitan Khosla Extracellular transglutaminase 2 is catalytically inactive, but is transiently activated upon tissue injury.
description	Transglutaminase 2 (TG2) is a multifunctional mammalian protein with transamidase and signaling properties. Using selective TG2 inhibitors and tagged nucleophilic amine substrates, we show that the majority of extracellular TG2 is inactive under normal physiological conditions in cell culture and in vivo. However, abundant TG2 activity was detected around the wound in a standard cultured fibroblast scratch assay. To demonstrate wounding-induced activation of TG2 in vivo, the toll-like receptor 3 ligand, polyinosinic-polycytidylic acid (poly(I:C)), was injected in mice to trigger small intestinal injury. Although no TG2 activity was detected in vehicle-treated mice, acute poly(I:C) injury resulted in rapid TG2 activation in the small intestinal mucosa. Our findings provide a new basis for understanding the role of TG2 in physiology and disease.
format	article
author	Matthew Siegel Pavel Strnad R Edward Watts Kihang Choi Bana Jabri M Bishr Omary Chaitan Khosla
author_facet	Matthew Siegel Pavel Strnad R Edward Watts Kihang Choi Bana Jabri M Bishr Omary Chaitan Khosla
author_sort	Matthew Siegel
title	Extracellular transglutaminase 2 is catalytically inactive, but is transiently activated upon tissue injury.
title_short	Extracellular transglutaminase 2 is catalytically inactive, but is transiently activated upon tissue injury.
title_full	Extracellular transglutaminase 2 is catalytically inactive, but is transiently activated upon tissue injury.
title_fullStr	Extracellular transglutaminase 2 is catalytically inactive, but is transiently activated upon tissue injury.
title_full_unstemmed	Extracellular transglutaminase 2 is catalytically inactive, but is transiently activated upon tissue injury.
title_sort	extracellular transglutaminase 2 is catalytically inactive, but is transiently activated upon tissue injury.
publisher	Public Library of Science (PLoS)
publishDate	2008
url	https://doaj.org/article/5cf5c1b6f2524e95bdbec9e682de5187
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Extracellular transglutaminase 2 is catalytically inactive, but is transiently activated upon tissue injury.

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