Proteomic Analysis of Human Skeletal Muscle (m. vastus lateralis) Proteins: Identification of 89 Gene Expression Products

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M. A. Kovalyova¹, L. I. Kovalyov^1*, I. Yu. Toropygin², S. V. Shigeev³, A. V. Ivanov¹, and S. S. Shishkin¹

¹Bach Institute of Biochemistry, Russian Academy of Sciences, Leninsky pr. 33, 119071 Moscow, Russia; fax: (495) 954-2733; E-mail: kovalyov@inbi.ras.ru

²Orekhovich Institute of Biomedical Chemistry, Russian Academy of Medical Sciences, Pogodinskaya ul. 10, 119121 Moscow, Russia; fax: (495) 245-0857

³People’s Friendship University of Russia, ul. Miklukho-Maklaya 8, 117198 Moscow, Russia; fax: (495) 433-2794

^* To whom correspondence should be addressed.

Received November 17, 2008; Revision received March 31, 2009

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Proteins from bioptates and autoptates of human skeletal muscle m. vastus lateralis were separated by O’Farrell two-dimensional gel electrophoresis (2DE). MALDI-TOF MS and MS/MS enabled identification of 89 protein spots as expression products of 55 genes. A modification of the O’Farrell’s method including non-equilibrium electrophoresis in a pH gradient allowed detection – among major sarcomeric, mitochondrial, and cytosolic proteins – of several proteins, such as PDZ- and LIM domain-containing ones (pI > 8.70), fragments of known proteins, and a stable complex of heavy and light ferritin chains. The data underlie further studies of human skeletal muscle proteins in terms of molecular mechanisms of some physiological and pathological processes.

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KEY WORDS: proteins of human skeletal muscle, proteomics

DOI: 10.1134/S0006297909110108

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