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Protective effect of L-arginine administration on proteins of unloaded m. soleus

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Abstract

Cytoskeletal and contractile proteins degenerate during functional unloading of muscle. The ratio of myosin heavy chain (MHC) expression changes simultaneously. We have supposed that NO can be a signal molecule related to the regulation of protein metabolism upon muscle unloading. To test this hypothesis, Wistar rats underwent functional unloading for 14 days without and with peroral administration of L-arginine (500 mg/kg) as NO precursor. Significant decreases in m. soleus mass, NO, nNOS, dystrophin, Hsp90, p-S6K, and type I MHC mRNA contents were found in the group of animals with unloading without preparation compared to those in control and in the group with unloading and administration of L-arginine; at the same time, increased contents of atrogin-1/MAFbx and MuRF-1 (p < 0.05) were found. No difference in the IGF-1 mRNA content between all three groups was found. Atrophy was significantly less pronounced in the group with unloading and L-arginine administration compared to that without the amino acid, and no destruction of cytoskeletal proteins was observed. We conclude that administration of L-arginine upon functional unloading decreases the extent of m. soleus atrophy, prevents the decrease in it of type I MHC mRNA, and blocks destructive changes in some cytoskeletal proteins. Such effect can be due to the absence of increase in this group of the content of some ubiquitin ligases and decreased intensity of the p70S6 kinase synthesis marker.

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Abbreviations

atrogin-1/MAFbx:

atrogin-1/Muscle Atrophy F-box

CSA:

cross sectional area

DETC:

diethyldithiocarbamate

GAPDH:

glyceraldehyde-3-phosphate dehydrogenase

Hsp90β:

90β heat shock proteins

IGF-1:

insulin-like growth factor 1

MF:

muscle fiber

MHC:

myosin heavy chain

mTOR:

mammalian target of rapamycin

MuRF-1:

muscle-specific RING finger protein 1

nNOS:

neuronal NO synthase

p70S6K:

p70S6 kinase

P-p70S6K:

phosphorylated form of p70S6 kinase

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Authors and Affiliations

  1. Faculty of Basic Medicine, Lomonosov Moscow State University, Lomonosovsky pr. 31/5, 117192, Moscow, Russia

    Yu. N. Lomonosova & T. L. Nemirovskaya

  2. Lomonosov Moscow Academy of Fine Chemical Technology, pr. Vernadskogo 86, 119571, Moscow, Russia

    Yu. N. Lomonosova & V. I. Shvets

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

    G. R. Kalamkarov, A. E. Bugrova & T. F. Shevchenko

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

    N. L. Kartashkina, E. A. Lysenko & T. L. Nemirovskaya

Authors
  1. Yu. N. Lomonosova
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  2. G. R. Kalamkarov
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  3. A. E. Bugrova
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  4. T. F. Shevchenko
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  5. N. L. Kartashkina
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  6. E. A. Lysenko
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  7. V. I. Shvets
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  8. T. L. Nemirovskaya
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Correspondence to T. L. Nemirovskaya.

Additional information

Original Russian Text © Yu. N. Lomonosova, G. R. Kalamkarov, A. E. Bugrova, T. F. Shevchenko, N. L. Kartashkina, E. A. Lysenko, V. I. Shvets, T. L. Nemirovskaya, 2011, published in Biokhimiya, 2011, Vol. 76, No. 5, pp. 701–712.

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Lomonosova, Y.N., Kalamkarov, G.R., Bugrova, A.E. et al. Protective effect of L-arginine administration on proteins of unloaded m. soleus . Biochemistry Moscow 76, 571–580 (2011). https://doi.org/10.1134/S0006297911050075

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