Effects of formoterol on protein metabolism in myotubes during hyperthermia.
Muscle Nerve
; 43(2): 268-73, 2011 Feb.
Article
en En
| MEDLINE
| ID: mdl-21254094
ABSTRACT
Proteolysis in skeletal muscle is mainly carried out by the activity of the ubiquitin-dependent proteolytic system. For the study of protein degradation through the ubiquitin-proteasome pathway, we used a model of hyperthermia in murine myotubes. In C2C12 cells, hyperthermia (41°C) induced a significant increase in both the rate of protein synthesis (18%) and degradation (51%). Interestingly, the addition of the ß(2) -adrenoceptor agonist formoterol resulted in a significant decrease in protein degradation (21%) without affecting protein synthesis. The decrease in proteolytic rate was associated with decreases in gene expression of the different components of the ubiquitin-dependent proteolytic system. The effects of the ß(2) -agonist on protein degradation were dependent exclusively on cAMP formation, because inhibition of adenylyl cyclase completely abolished the effects of formoterol on protein degradation. It can be concluded that hyperthermia is a suitable model for studying the anti-proteolytic potential of drugs used in the treatment of muscle wasting.
Texto completo:
1
Bases de datos:
MEDLINE
Asunto principal:
Ubiquitinas
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Fibras Musculares Esqueléticas
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Complejo de la Endopetidasa Proteasomal
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Etanolaminas
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Agonistas de Receptores Adrenérgicos beta 2
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Hipertermia Inducida
Límite:
Animals
Idioma:
En
Revista:
Muscle Nerve
Año:
2011
Tipo del documento:
Article
País de afiliación:
España