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. 2017 Oct;434(1-2):61-73.
doi: 10.1007/s11010-017-3037-6. Epub 2017 Apr 21.

Proteomic analysis of mitochondrial proteins in the guinea pig heart following long-term normobaric hyperoxia

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Proteomic analysis of mitochondrial proteins in the guinea pig heart following long-term normobaric hyperoxia

Lucia Lichardusova et al. Mol Cell Biochem. 2017 Oct.

Abstract

Normobaric hyperoxia is applied for the treatment of a wide variety of diseases and clinical conditions related to ischemia or hypoxia, but it can increase the risk of tissue damage and its efficiency is controversial. In the present study, we analyzed cardiac mitochondrial proteome derived from guinea pigs after 60 h exposure to 100% molecular oxygen (NBO) or O2 enriched with oxygen cation (NBO+). Two-dimensional gel electrophoresis followed by MALDI-TOF/TOF mass spectrometry identified twenty-two different proteins (among them ten nonmitochondrial) that were overexpressed in NBO and/or NBO+ group. Identified proteins were mainly involved in cellular energy metabolism (tricarboxylic acid cycle, oxidative phosphorylation, glycolysis), cardioprotection against stress, control of mitochondrial function, muscle contraction, and oxygen transport. These findings support the viewpoint that hyperoxia is associated with cellular stress and suggest complex adaptive responses which probably contribute to maintain or improve intracellular ATP levels and contractile function of cardiomyocytes. In addition, the results suggest that hyperoxia-induced cellular stress may be partially attenuated by utilization of NBO+ treatment.

Keywords: Heart; Hyperoxia; Mass spectrometry; Mitochondria; Protein expression.

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