Age-associated oxidative modifications of mitochondrial α-subunit of F1 ATP synthase from mouse skeletal muscles

Free Radical Research
N Das, Chandan K Jana

Abstract

The objective of this study was to investigate the pattern of age-associated oxidative post-translational modifications in the skeletal muscles of a mammalian species and to address whether the modifications result in the loss of function of the oxidatively modified protein(s). Accordingly, proteins in the mitochondrial matrix of the hind limb of C57BL/6Nnia mice were examined for modifications by carbonylation--an established marker of oxidative post-translational modifications--by Western blotting using anti-2,4-dinitrophenyl antibodies and tritiated sodium borohydride methods. An age-associated increase in carbonylation of mitochondrial matrix proteins was observed, but not all proteins were equally susceptible. A 55 kDa protein, identified as the α-subunit of the F1 complex of ATP synthase (ATP phosphohydrolase [H(+)-transporting]), had approximately 17% and 27% higher levels of protein carbonyls in adult and old animals, respectively, in comparison to the young controls as estimated using tritiated sodium borohydride. In addition, an age-associated decline in its activity was observed, with approximately 9% and 28% decrease in the activity in the adult and old animals, respectively, in comparison to young controls. It may ...Continue Reading

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Citations

Apr 2, 2016·Oxidative Medicine and Cellular Longevity·Nina Kaludercic, Valentina Giorgio
Sep 14, 2019·FASEB Journal : Official Publication of the Federation of American Societies for Experimental Biology·Shousheng NiShicui Zhang
Feb 20, 2021·Oxidative Medicine and Cellular Longevity·Leonardo MattaRodrigo S Fortunato

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