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Role of NO-Synthase in Regulation of Protein Metabolism of Stretched Rat m. soleus Muscle during Functional Unloading

Yu. N. Lomonosova1,2, G. R. Kalamkarov3, A. E. Bugrova3, T. F. Shevchenko3, N. L. Kartashkina2, E. A. Lysenko2, B. S. Shenkman2, and T. L. Nemirovskaya1,2*

1Faculty of Basic Medicine, Lomonosov Moscow State University, 117191 Moscow, Russia; fax: (495) 932-9908; E-mail: nemirovskaya@bk.ru

2Institute for Bio-Medical Problems, Russian Academy of Sciences, Khoroshevskoe Shosse 76a, 123007 Moscow, Russia

3Emanuel Institute of Biochemical Physics, Russian Academy of Sciences, ul. Kosygina 4, 119334 Moscow, Russia

* To whom correspondence should be addressed.

Received August 29, 2011; Revision received September 23, 2011
Gravitational unloading causes atrophy of muscle fibers and can lead to destruction of cytoskeletal and contractile proteins. Along with the atrophic changes, unloaded muscle frequently demonstrates significant shifts in the ratio of muscle fibers expressing fast and slow myosin heavy chain isoforms. Stretching of the m. soleus during hindlimb suspension prevents its atrophy. We supposed that neuronal NO-synthase (NOS) (which is attached to membrane dystrophin–sarcoglycan complex) can contribute to maintenance of protein metabolism in the muscle and prevent its atrophy when m. soleus is stretched. To test this hypothesis, we used Wistar rats (56 animals) in experiments with hindlimb suspension during 14 days. The group of hindlimb suspended rats with stretched m. soleus was injected with L-NAME to block NOS activity. We found that m. soleus mass and its protein content in hindlimb-suspended rats with stretched m. soleus were preserved due to prevention of protein degradation. NOS is involved in maintenance of expression of some muscle proteins. Proliferation of satellite cells in stretched m. soleus may be due to nNOS activity, but maintenance of muscle mass upon stretching is regulated not by NOS alone.
KEY WORDS: m. soleus unloading, m. soleus stretching, L-NAME, cytoskeletal proteins, nNOS, Hsp90, E3 ligase, p70S6K

DOI: 10.1134/S0006297912020137