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Am J Physiol Cell Physiol ; 293(1): C35-44, 2007 Jul.
Artigo em Inglês | MEDLINE | ID: mdl-17182729

RESUMO

Effects of 14 days of hindlimb unloading or synergist ablation-related overloading with or without deafferentation on the fiber cross-sectional area, myonuclear number, size, and domain, the number of nucleoli in a single myonucleus, and the levels in the phosphorylation of the ribosomal protein S6 (S6) and 27-kDa heat shock protein (HSP27) were studied in rat soleus. Hypertrophy of fibers (+24%), associated with increased nucleolar number (from 1-2 to 3-5) within a myonucleus and myonuclear domain (+27%) compared with the preexperimental level, was induced by synergist ablation. Such phenomena were associated with increased levels of phosphorylated S6 (+84%) and HSP27 (+28%). Fiber atrophy (-52%), associated with decreased number (-31%) and domain size (-28%) of myonuclei and phosphorylation of S6 (-98%) and HSP27 (-63%), and with increased myonuclear size (+19%) and ubiquitination of myosin heavy chain (+33%, P > 0.05), was observed after unloading, which inhibited the mechanical load. Responses to deafferentation, which inhibited electromyogram level (-47%), were basically similar to those caused by hindlimb unloading, although the magnitudes were minor. The deafferentation-related responses were prevented and nucleolar number was even increased (+18%) by addition of synergist ablation, even though the integrated electromyogram level was still 30% less than controls. It is suggested that the load-dependent maintenance or upregulation of the nucleolar number and/or phosphorylation of S6 and HSP27 plays the important role(s) in the regulation of muscle mass. It was also indicated that such regulation was not necessarily associated with the neural activity.


Assuntos
Nucléolo Celular/metabolismo , Proteínas de Choque Térmico/metabolismo , Músculo Esquelético/metabolismo , Atrofia Muscular/metabolismo , Doenças Musculares/metabolismo , Proteínas de Neoplasias/metabolismo , Proteína S6 Ribossômica/metabolismo , Animais , Nucléolo Celular/patologia , Modelos Animais de Doenças , Eletromiografia , Proteínas de Choque Térmico HSP27 , Elevação dos Membros Posteriores , Hipertrofia , Masculino , Denervação Muscular , Fibras Musculares Esqueléticas/metabolismo , Fibras Musculares Esqueléticas/patologia , Força Muscular , Músculo Esquelético/inervação , Músculo Esquelético/patologia , Músculo Esquelético/fisiopatologia , Atrofia Muscular/patologia , Atrofia Muscular/fisiopatologia , Doenças Musculares/patologia , Doenças Musculares/fisiopatologia , Cadeias Pesadas de Miosina/metabolismo , Fosforilação , Processamento de Proteína Pós-Traducional , Ratos , Ratos Wistar , Ubiquitina/metabolismo
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