Characterization of mitochondrial NADH dehydrogenase 1α subcomplex 10 variants in cardiac muscles from normal Wistar rats and spontaneously hypertensive rats: Implications in the pathogenesis of hypertension

Huang,Liying; Jin,Xian; Xia,Li; Wang,Xiaoling; Yu,Yun; Liu,Cunfei; Shao,Dongmin; Fang,Ningyuan; Meng,Chao

doi:10.3892/mmr.2015.4607

January-2016 Volume 13 Issue 1

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January-2016 Volume 13 Issue 1

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Article

Characterization of mitochondrial NADH dehydrogenase 1α subcomplex 10 variants in cardiac muscles from normal Wistar rats and spontaneously hypertensive rats: Implications in the pathogenesis of hypertension

Authors:
- Liying Huang
- Xian Jin
- Li Xia
- Xiaoling Wang
- Yun Yu
- Cunfei Liu
- Dongmin Shao
- Ningyuan Fang
- Chao Meng
View Affiliations / Copyright

Affiliations: Department of Geriatrics, Ren Ji Hospital, School of Medicine, Shanghai Jiao Tong University, Shanghai 200001, P.R. China, Department of Pathophysiology, School of Medicine, Shanghai Jiao Tong University, Shanghai 200025, P.R. China, Section of Vascular Biology, National Heart and Lung Institute, Imperial College London, London SW3 6LY, UK
Pages: 961-966
|
Published online on: November 23, 2015

https://doi.org/10.3892/mmr.2015.4607
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Abstract

Mitochondrial dysfunction has been increasingly associated with the development of cardiovascular diseases, including hypertension and cardiac hypertrophy. In the present study, NADH dehydrogenase 1α subcomplex 10 (Ndufa10) was characterized from the left ventricular muscles of spontaneously hypertensive rats (SHRs) and normal Wistar Kyoto (WKY) rats. Western blot analysis demonstrated that there was a shift in the molecular weight (MW) and in the isoelectric point (pI) of the Ndufa10 protein from SHRs and WKY rats. Mass spectrometric analysis revealed that the replacement of an aspartate residue with asparagine at amino acid position 120 was the biochemical difference between the two Ndufa10 isoforms. Further analysis using the bacterially expressed proteins Ndufa10‑120N (WKY) and Ndufa10‑120D (SHR) revealed that the shift in the pI and MW of the two Ndufa10 isoforms was solely caused by the amino acid mutation, and not by post‑translational modifications. Since deficiencies of the mitochondrial complex I are the most common defects in the oxidative phosphorylation system, further studies are required to study the difference between the activities of the two Ndufa10 variants, and their role in the pathogenesis of hypertension.

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