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REVIEW: Proteomic Studies of Human and Other Vertebrate Muscle Proteins

S. S. Shishkin*, L. I. Kovalyov, and M. A. Kovalyova

Bach Institute of Biochemistry, Russian Academy of Sciences, Leninsky pr. 33, Moscow 119071, Russia; fax: (7-095) 954-2733; E-mail: shishkin@inbi.ras.ru

* To whom correspondence should be addressed.

Received July 9, 2004
This review summarizes results of some systemic studies of muscle proteins of humans and some other vertebrates. The studies, started after introduction of two-dimensional gel electrophoresis of O'Farrell, were significantly extended during development of proteomics, a special branch of functional genomics. Special attention is paid to analysis of characteristic features of strategy for practical realization of the systemic approach during three main stages of these studies: pre-genomic, genomic (with organizational registration of proteomics), and post-genomic characterized by active use of structural genomics data. Proteomic technologies play an important role in detection of changes in isoforms of various muscle proteins (myosins, troponins, etc.). These changes possibly reflecting tissue specificity of gene expression may underline functional state of muscle tissues under normal and pathological conditions, and such proteomic analysis is now used in various fields of medicine.
KEY WORDS: muscle protein isoforms, proteomics, myosin and troponin families