SECIS-binding protein 2 promotes cell survival by protecting against oxidative stress

Papp, Laura V., Lu, Jun, Bolderson, Emma, Boucher, Didier, Singh, Ravindra, Holmgren, Arne and Khanna, Kum Kum (2010) SECIS-binding protein 2 promotes cell survival by protecting against oxidative stress. Antioxidants and Redox Signaling, 12 7: 797-808. doi:10.1089/ars.2009.2913

Attached Files (Some files may be inaccessible until you login with your UQ eSpace credentials)
Name Description MIMEType Size Downloads
Khanna_authaffil_staffdata.pdf Khanna_authaffil_staffdata.pdf application/pdf 146.99KB 0

Author Papp, Laura V.
Lu, Jun
Bolderson, Emma
Boucher, Didier
Singh, Ravindra
Holmgren, Arne
Khanna, Kum Kum
Title SECIS-binding protein 2 promotes cell survival by protecting against oxidative stress
Journal name Antioxidants and Redox Signaling   Check publisher's open access policy
ISSN 1523-0864
Publication date 2010-04-01
Year available 2009
Sub-type Article (original research)
DOI 10.1089/ars.2009.2913
Volume 12
Issue 7
Start page 797
End page 808
Total pages 12
Editor Chandan K. Sen
Dipak K. Das
Place of publication New Rochelle, NY, U.S.A.
Publisher Mary Ann Liebert Publishers
Collection year 2011
Language eng
Formatted abstract
Reactive oxygen species (ROS) are a primary cause of cellular damage that leads to cell death. In cells, protection from ROS-induced damage and maintenance of the redox balance is mediated to a large extent by selenoproteins, a distinct family of proteins that contain selenium in form of selenocysteine (Sec) within their active site. Incorporation of Sec requires the Sec-insertion sequence element (SECIS) in the 3′-untranslated region of selenoproteins mRNAs and the SECIS-binding protein 2 (SBP2). Previous studies have shown that SBP2 is required for the Sec-incorporation mechanism; however, additional roles of SBP2 in the cell have remained undefined. We herein show that depletion of SBP2 by using antisense oligonucleotides (ASOs) causes oxidative stress and induction of caspase- and cytochrome c-dependent apoptosis. Cells depleted of SBP2 have increased levels of ROS, which lead to cellular stress manifested as 8-oxo-7,8-dihydroguanine (8-oxo-dG) DNA lesions, stress granules, and lipid peroxidation. Small-molecule antioxidants N-acetylcysteine, glutathione, and α-tocopherol only marginally reduced ROS and were unable to rescue cells fully from apoptosis, indicating that apoptosis might be directly mediated by selenoproteins. Our results demonstrate that SBP2 is required for protection against ROS-induced cellular damage and cell survival.
© Mary Ann Liebert, Inc.
Keyword Transfer-RNA gene
Selenocysteine insertion
Thioredoxin reductase
Q-Index Code C1
Q-Index Status Confirmed Code
Institutional Status UQ
Additional Notes Online Ahead of Editing: October 5, 2009. Online Ahead of Print: January 21, 2010.

Document type: Journal Article
Sub-type: Article (original research)
Collections: Official 2011 Collection
School of Medicine Publications
Version Filter Type
Citation counts: TR Web of Science Citation Count  Cited 11 times in Thomson Reuters Web of Science Article | Citations
Scopus Citation Count Cited 11 times in Scopus Article | Citations
Google Scholar Search Google Scholar
Created: Fri, 01 Apr 2011, 09:12:32 EST by Debbie Banks on behalf of !NON-HERDC