Please use this identifier to cite or link to this item:
Scopus Web of Science® Altmetric
Type: Journal article
Title: Overexpression of catalase diminishes oxidative cysteine modifications of cardiac proteins
Author: Yao, C.
Behring, J.
Shao, D.
Sverdlov, A.
Whelan, S.
Elezaby, A.
Yin, X.
Siwik, D.
Seta, F.
Costello, C.
Cohen, R.
Matsui, R.
Colucci, W.
McComb, M.
Bachschmid, M.
Citation: PLoS One, 2015; 10(12):e0144025-1-e0144025-20
Publisher: Public Library of Science
Issue Date: 2015
ISSN: 1932-6203
Editor: Franco, R.
Statement of
Chunxiang Yao, Jessica B. Behring, Di Shao, Aaron L. Sverdlov, Stephen A. Whelan, Aly Elezaby, Xiaoyan Yin, Deborah A. Siwik, Francesca Seta, Catherine E. Costello, Richard A. Cohen, Reiko Matsui, Wilson S. Colucci, Mark E. McComb, Markus M. Bachschmid
Abstract: Reactive protein cysteine thiolates are instrumental in redox regulation. Oxidants, such as hydrogen peroxide (H2O2), react with thiolates to form oxidative post-translational modifications, enabling physiological redox signaling. Cardiac disease and aging are associated with oxidative stress which can impair redox signaling by altering essential cysteine thiolates. We previously found that cardiac-specific overexpression of catalase (Cat), an enzyme that detoxifies excess H2O2, protected from oxidative stress and delayed cardiac aging in mice. Using redox proteomics and systems biology, we sought to identify the cysteines that could play a key role in cardiac disease and aging. With a 'Tandem Mass Tag' (TMT) labeling strategy and mass spectrometry, we investigated differential reversible cysteine oxidation in the cardiac proteome of wild type and Cat transgenic (Tg) mice. Reversible cysteine oxidation was measured as thiol occupancy, the ratio of total available versus reversibly oxidized cysteine thiols. Catalase overexpression globally decreased thiol occupancy by ≥1.3 fold in 82 proteins, including numerous mitochondrial and contractile proteins. Systems biology analysis assigned the majority of proteins with differentially modified thiols in Cat Tg mice to pathways of aging and cardiac disease, including cellular stress response, proteostasis, and apoptosis. In addition, Cat Tg mice exhibited diminished protein glutathione adducts and decreased H2O2 production from mitochondrial complex I and II, suggesting improved function of cardiac mitochondria. In conclusion, our data suggest that catalase may alleviate cardiac disease and aging by moderating global protein cysteine thiol oxidation.
Keywords: Myocardium
Mitochondria, Heart
Mice, Transgenic
Heart Diseases
Hydrogen Peroxide
Muscle Proteins
Signal Transduction
Protein Processing, Post-Translational
Oxidative Stress
Rights: © 2015 Yao et al. This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited
DOI: 10.1371/journal.pone.0144025
Grant ID:
Appears in Collections:Aurora harvest 3
Medicine publications

Files in This Item:
File Description SizeFormat 
hdl_98431.pdfPublished version4.72 MBAdobe PDFView/Open

Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.