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Sci Rep. 2018 Dec 11;8(1):17772. doi: 10.1038/s41598-018-35728-2.

Differential regulation of cysteine oxidative post-translational modifications in high and low aerobic capacity.

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School of Physical Education and Sport, University of São Paulo, São Paulo, Brazil.
School of Physical Education and Sport, University of São Paulo, São Paulo, Brazil.
Section on Integrative Physiology and Metabolism, Joslin Diabetes Center, Harvard Medical School, Boston, Massachusetts, USA.
Biosciences Department, Federal University of São Paulo, Santos, Brazil.
K.G. Jebsen Center of Exercise in Medicine, Department of Circulation and Medical Imaging, Norwegian University of Science and Technology (NTNU), Trondheim, Norway.
Department of Cancer Research and Molecular Medicine and PROMEC Core Facility for Proteomics and Modomics, Norwegian University of Science and Technology (NTNU), and Central Norway Regional Health Authority, Trondheim, Norway.
Department of Physiology & Pharmacology, The University of Toledo, Toledo, Ohio, USA.
Department of Anesthesiology, University of Michigan - Medical School, Ann Arbor, Michigan, USA.
Department of Molecular and Integrative Physiology, University of Michigan, Ann Arbor, Michigan, USA.
School of Human Movement & Nutrition Sciences, University of Queensland, Brisbane, Australia.
School of Physical Education and Sport, University of São Paulo, São Paulo, Brazil.


Given the association between high aerobic capacity and the prevention of metabolic diseases, elucidating the mechanisms by which high aerobic capacity regulates whole-body metabolic homeostasis is a major research challenge. Oxidative post-translational modifications (Ox-PTMs) of proteins can regulate cellular homeostasis in skeletal and cardiac muscles, but the relationship between Ox-PTMs and intrinsic components of oxidative energy metabolism is still unclear. Here, we evaluated the Ox-PTM profile in cardiac and skeletal muscles of rats bred for low (LCR) and high (HCR) intrinsic aerobic capacity. Redox proteomics screening revealed different cysteine (Cys) Ox-PTM profile between HCR and LCR rats. HCR showed a higher number of oxidized Cys residues in skeletal muscle compared to LCR, while the opposite was observed in the heart. Most proteins with differentially oxidized Cys residues in the skeletal muscle are important regulators of oxidative metabolism. The most oxidized protein in the skeletal muscle of HCR rats was malate dehydrogenase (MDH1). HCR showed higher MDH1 activity compared to LCR in skeletal, but not cardiac muscle. These novel findings indicate a clear association between Cys Ox-PTMs and aerobic capacity, leading to novel insights into the role of Ox-PTMs as an essential signal to maintain metabolic homeostasis.

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