Review article

Transglutaminase 2 in human diseases

¹ Dental Biochemistry, Department of Biochemistry and Molecular Biology, University of Debrecen, Debrecen 4010, Hungary
² Department of Pediatrics and Biochemistry and Molecular Biology, University of Debrecen, Debrecen 4010, Hungary
³ Celiac Disease Center, Heim Pál Children’s Hospital, Budapest 1089, Hungary
⁴ Department of Biochemistry and Molecular Biology, University of Debrecen, Debrecen 4010, Hungary
⁵ Division of Immunology and Rheumatology, Department of Internal Medicine, China Medical University Hospital, Taichung 404, Taiwan
⁶ School of medicine, College of Medicine, China Medical University, Taichung 404, Taiwan

^* Corresponding author. Department of Dental Biochemistry Signaling and Apoptosis Research Group Research Center of Molecular Medicine University of Debrecen H-4012 Debrecen Nagyerdei krt. 98. Hungary. E-mail address: szondy@med.unideb.hu (Zsuzsa Szondy).

Received: 23 April 2017
Accepted: 15 May 2017

Abstract

Transglutaminase 2 (TG2) is an inducible transamidating acyltransferase that catalyzes Ca(2+)-dependent protein modifications. In addition to being an enzyme, TG2 also serves as a G protein for several seven transmembrane receptors and acts as a co-receptor for integrin β1 and β3 integrins distinguishing it from other members of the transglutaminase family. TG2 is ubiquitously expressed in almost all cell types and all cell compartments, and is also present on the cell surface and gets secreted to the extracellular matrix via non-classical mechanisms. TG2 has been associated with various human diseases including inflammation, cancer, fibrosis, cardiovascular disease, neurodegenerative diseases, celiac disease in which it plays either a protective role, or contributes to the pathogenesis. Thus modulating the biological activities of TG2 in these diseases will have a therapeutic value.