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

Molecular Medicine Reports

Volumn 13, Issue 1, 2016, Pages 961-966

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

^a SHANGHAI JIAO TONG UNIVERSITY SCHOOL OF MEDICINE   (China)

^b NATIONAL HEART AND LUNG INSTITUTE   (United Kingdom)

Author keywords

Matrix assisted laser desorption ionization time of flight mass spectrometry; Mobility; Molecular weight; Mutation; NADH dehydrogenase 1 subcomplex 10

Indexed keywords

AMINO ACID; ASPARAGINE; ASPARTIC ACID; MITOCHONDRIAL PROTEIN; NADH DEHYDROGENASE 1ALPHA SUBCOMPLEX 10; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE DEHYDROGENASE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE DEHYDROGENASE (UBIQUINONE); UNCLASSIFIED DRUG; NDUFA10 PROTEIN, RAT;

AMINO ACID SUBSTITUTION; ANIMAL EXPERIMENT; ANIMAL MODEL; ARTICLE; CONTROLLED STUDY; HEART MUSCLE; HYPERTENSION; ISOELECTRIC POINT; MASS SPECTROMETRY; MATRIX ASSISTED LASER DESORPTION IONIZATION TIME OF FLIGHT MASS SPECTROMETRY; MOLECULAR WEIGHT; MUTATION; NONHUMAN; OXIDATIVE PHOSPHORYLATION; PATHOGENESIS; PROTEIN PROCESSING; PROTEIN PURIFICATION; RAT; SPONTANEOUSLY HYPERTENSIVE RAT; TANDEM MASS SPECTROMETRY; TWO DIMENSIONAL GEL ELECTROPHORESIS; WESTERN BLOTTING; WISTAR RAT; AMINO ACID SEQUENCE; ANIMAL; BLOOD PRESSURE; CARDIAC MUSCLE; CARDIOMEGALY; GENETICS; HEART MITOCHONDRION; HUMAN; METABOLISM; PATHOLOGY;

AMINO ACID SEQUENCE; ANIMALS; BLOOD PRESSURE; CARDIOMEGALY; ELECTRON TRANSPORT COMPLEX I; HUMANS; HYPERTENSION; MITOCHONDRIA, HEART; MUTATION; MYOCARDIUM; NADH DEHYDROGENASE; OXIDATIVE PHOSPHORYLATION; RATS;

EID: 84954285981     PISSN: 17912997     EISSN: 17913004     Source Type: Journal    
DOI: 10.3892/mmr.2015.4607     Document Type: Article

References (15)

1. Di Lisa F, Canton M, Menabò R, Kaludercic N and Bernardi P: Mitochondria and cardioprotection. Heart Fail Rev 12: 249-260, 2007.
2. Lopez-Campistrous A, Hao L, Xiang W, Ton D, Semchuk P, Sander J, Ellison MJ and Fernandez-Patron C: Mitochondrial dysfunction in the hypertensive rat brain: Respiratory complexes exhibit assembly defects in hypertension. Hypertension 51: 412-419, 2008.
3. Takimoto E and Kass DA: Role of oxidative stress in cardiac hypertrophy and remodeling. Hypertension 49: 241-248, 2007.
4. Bernal-Mizrachi C, Gates AC, Weng S, Imamura T, Knutsen RH, DeSantis P, Coleman T, Townsend RR, Muglia LJ and Semenkovich CF: Vascular respiratory uncoupling increases blood pressure and atherosclerosis. Nature 435: 502-506, 2005.
5. Smeitink JA, van den Heuvel LW, Koopman WJ, Nijtmans LG, Ugalde C and Willems PH: Cell biological consequences of mitochondrial NADH: Ubiquinone oxidoreductase deficiency. Curr Neurovasc Res 1: 29-40, 2004.
6. Efremov RG and Sazanov LA: Structure of the membrane domain of respiratory complex I. Nature 476: 414-420, 2011.
7. Meng C, Jin X, Xia L, Shen SM, Wang XL, Cai J, Chen GQ, Wang LS and Fang NY: Alterations of mitochondrial enzymes contribute to cardiac hypertrophy before hypertension development in spontaneously hypertensive rats. J Proteome Res 8: 2463-2475, 2009.
8. Sardanelli AM, Technikova-Dobrova Z, Scacco SC, Speranza F and Papa S: Characterization of proteins phosphorylated by the cAMP-dependent protein kinase of bovine heart mitochondria. FEBS Lett 377: 470-474, 1995.
9. Schulenberg B, Aggeler R, Beechem JM, Capaldi RA and Patton WF: Analysis of steady-state protein phosphorylation in mitochondria using a novel fluorescent phosphosensor dye. J Biol Chem 278: 27251-27255, 2003.
10. Schilling B, Aggeler R, Schulenberg B, Murray J, Row RH, Capaldi RA and Gibson BW: Mass spectrometric identification of a novel phosphorylation site in subunit NDUFA10 of bovine mitochondrial complex I. FEBS Lett 579: 2485-2490, 2005.
11. Muñoz J, Fernández-Irigoyen J, Santamaría E, Parbel A, Obeso J and Corrales FJ: Mass spectrometric characterization of mitochondrial complex I NDUFA10 variants. Proteomics 8: 1898-1908, 2008.
12. Shirai A, Matsuyama A, Yashiroda Y, Hashimoto A, Kawamura Y, Arai R, Komatsu Y, Horinouchi S and Yoshida M: Global analysis of gel mobility of proteins and its use in target identification. J Biol Chem 283: 10745-10752, 2008.
13. Lazarou M, McKenzie M, Ohtake A, Thorburn DR and Ryan MT: Analysis of the assembly profiles for mitochondrial-and nuclear-DNA-encoded subunits into complex I. Mol Cell Biol 27: 4228-4237, 2007.
14. Distelmaier F, Koopman WJ, van den Heuvel LP, Rodenburg RJ, Mayatepek E, Willems PH and Smeitink JA: Mitochondrial complex I deficiency: From organelle dysfunction to clinical disease. Brain 132: 833-842, 2009.
15. Hoefs SJ, van Spronsen FJ, Lenssen EW, Nijtmans LG, Rodenburg RJ, Smeitink JA and van den Heuvel LP: NDUFA10 mutations cause complex I deficiency in a patient with Leigh disease. Eur J Hum Genet 19: 270-274, 2011.