Biological functionalities of Transglutaminase 2 and the possibility of its compensation by other members of the transglutaminase family

Odii, Benedict O. and Coussons, Peter J. (2014) Biological functionalities of Transglutaminase 2 and the possibility of its compensation by other members of the transglutaminase family. Scientific World Journal, 2014. p. 714561. ISSN 1537-744X

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Abstract

Transglutaminase 2 (TG2) is the most widely distributed and most abundantly expressed member of the transglutaminase family of enzymes, a group of intracellular and extracellular proteins that catalyze the Ca2+-dependent post-translational modification of proteins. It is a unique member of the transglutaminase family owing to its specialized biochemical, structural and functional elements, ubiquitous tissue distribution and sub-cellular localization, and substrate specificity. The broad substrate-specificity of TG2 and its flexible interaction with numerous other gene products may account for its multiple biological functions. In addition to the classic Ca2+-dependent transamidation of proteins, which is a hallmark of transglutaminase enzymes, additional Ca2+-independent enzymatic and non-enzymatic activities of TG2 have been identified. Many such activities have been directly or indirectly implicated in diverse cellular physiological events, including cell growth and differentiation, cell adhesion and morphology, extracellular matrix stabilization, wound healing, cellular development, receptor-mediated endocytosis, apoptosis, and disease pathology. Given the wide range of activities of the transglutaminase gene family it has been suggested that, in the absence of active versions of TG2, its function could be compensated for by other members of the transglutaminase family. It is in the light of this assertion that we review herein, TG2 activities and the possibilities and premises for compensation for its absence.

Item Type:	Journal Article
Keywords:	Transglutaminase 2, functions, activity, enzyme
Faculty:	ARCHIVED Faculty of Science & Technology (until September 2018)
Depositing User:	Repository Admin
Date Deposited:	20 Jan 2014 10:02
Last Modified:	23 Feb 2022 16:31
URI:	https://arro.anglia.ac.uk/id/eprint/311603

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