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Degradation of transglutaminase 2 by calcium-mediated ubiquitination responding to high oxidative stress

Cited 19 time in Web of Science Cited 21 time in Scopus
Authors

Jeong, Eui Man; Kim, Chai-Wan; Cho, Sung-Yup; Jang, Gi-Yong; Shin, Dong-Myung; Jeon, Ju-Hong; Kim, In-Gyu

Issue Date
2009-02-03
Publisher
Elsevier
Citation
FEBS Lett. 583(4), 648-654
Keywords
Adenoviridae/geneticsAnti-Bacterial Agents/pharmacologyApoptosisCalcimycin/pharmacologyCalcium/*metabolismCell DeathCell LineCulture Media, Serum-FreeDose-Response Relationship, DrugEnzyme Inhibitors/pharmacologyGTP-Binding Proteins/*metabolismHela CellsHumansKidney/cytologyLeupeptins/pharmacologyTime FactorsTransglutaminases/*metabolismUbiquitinationOxidative Stress
Abstract
Transglutaminase 2 (TG2) is a calcium-dependent enzyme that catalyzes the transamidation reaction. There is conflicting evidence on the role of TG2 in apoptosis. In this report, we show that TG2 increases in response to low level of oxidative stress, whereas TG2 diminishes under high stress conditions. Monitoring TG2 expression, activity and calcium concentration in cells treated with A23187 revealed that the initial rise of calcium activates TG2 but subsequent calcium-overload induces the degradation of TG2 via calcium-mediated polyubiquitination. These results indicate that the role of TG2 in apoptosis depends on the level of calcium influx triggered by oxidative stress.
ISSN
1873-3468 (Electronic)
Language
English
URI
http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=19183553

http://www.sciencedirect.com/science?_ob=MImg&_imagekey=B6T36-4VGDKWR-2-F&_cdi=4938&_user=168665&_orig=search&_coverDate=02%2F18%2F2009&_sk=994169995&view=c&wchp=dGLzVtz-zSkWA&md5=6fff65f9511699162a762b3c2fa20ce3&ie=/sdarticle.pdf

https://hdl.handle.net/10371/68135
DOI
https://doi.org/10.1016/j.febslet.2009.01.032
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