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

M. A. Kovalyova1, L. I. Kovalyov1*, 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
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.
KEY WORDS: proteins of human skeletal muscle, proteomics

DOI: 10.1134/S0006297909110108