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Transglutaminase 2 in human diseases
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 distingui...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
EDP Sciences
2017
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5571667/ https://www.ncbi.nlm.nih.gov/pubmed/28840829 http://dx.doi.org/10.1051/bmdcn/2017070315 |
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author | Szondy, Zsuzsa Korponay-Szabó, Ilma Király, Robert Sarang, Zsolt Tsay, Gregory J. |
author_facet | Szondy, Zsuzsa Korponay-Szabó, Ilma Király, Robert Sarang, Zsolt Tsay, Gregory J. |
author_sort | Szondy, Zsuzsa |
collection | PubMed |
description | 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. |
format | Online Article Text |
id | pubmed-5571667 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2017 |
publisher | EDP Sciences |
record_format | MEDLINE/PubMed |
spelling | pubmed-55716672017-09-01 Transglutaminase 2 in human diseases Szondy, Zsuzsa Korponay-Szabó, Ilma Király, Robert Sarang, Zsolt Tsay, Gregory J. Biomedicine (Taipei) Review Article 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. EDP Sciences 2017-08-25 /pmc/articles/PMC5571667/ /pubmed/28840829 http://dx.doi.org/10.1051/bmdcn/2017070315 Text en © Author(s) 2017. This article is published with open access by China Medical University Open Access This article is distributed under terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0) which permits any use, distribution, and reproduction in any medium, provided original author(s) and source are credited. |
spellingShingle | Review Article Szondy, Zsuzsa Korponay-Szabó, Ilma Király, Robert Sarang, Zsolt Tsay, Gregory J. Transglutaminase 2 in human diseases |
title | Transglutaminase 2 in human diseases |
title_full | Transglutaminase 2 in human diseases |
title_fullStr | Transglutaminase 2 in human diseases |
title_full_unstemmed | Transglutaminase 2 in human diseases |
title_short | Transglutaminase 2 in human diseases |
title_sort | transglutaminase 2 in human diseases |
topic | Review Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5571667/ https://www.ncbi.nlm.nih.gov/pubmed/28840829 http://dx.doi.org/10.1051/bmdcn/2017070315 |
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