MnSOD non-acetylation mimic knock-in mice exhibit dilated cardiomyopathy.

Joseph R Schell, Sung-Jen Wei, Jun Zhang, Rolando Trevino, Wan Hsi Chen, Leonardo Aguilar, Wei Qian, Cole W Corbett, Haiyan Jiang, Felix F Dong, E Sandra Chocron, Alia Nazarullah, Jenny Chang, Margaret E Flanagan, Vaida Glatt, Sergey Dikalov, Erin Munkácsy, Nobuo Horikoshi, David Gius

Department of Radiation Oncology, Mays Cancer Center at UT Health San Antonio MD Anderson, Joe R. and Teresa Lozano Long School of Medicine, TX, USA; Barshop Institute for Longevity and Aging Studies, UT Health San Antonio, TX, USA.Department of Radiation Oncology, Mays Cancer Center at UT Health San Antonio MD Anderson, Joe R. and Teresa Lozano Long School of Medicine, TX, USA; Barshop Institute for Longevity and Aging Studies, UT Health San Antonio, TX, USA. · pubmed

Paper

Abstract

Manganese superoxide dismutase (MnSOD/SOD2) is an essential mitochondrial enzyme that detoxifies superoxide radicals generated during oxidative respiration. MnSOD/SOD2 lysine 68 acetylation (K68-Ac) is an important post-translational modification (PTM) that regulates enzymatic activity, responding to nutrient status or oxidative stress, and elevated levels have been associated with human illness. To determine the in vivo role of MnSOD-K68 in the heart, we used a whole-body non-acetylation mimic mutant (MnSOD

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Research summary

The paper investigates the role of MnSOD-K68 acetylation in the heart and its implications for cardiomyopathy. This research is relevant as it explores a potential mechanism related to oxidative stress, which is a significant factor in aging and age-related diseases.

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