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Effects of formoterol on protein metabolism in myotubes during hyperthermia
Author(s) -
Ametller Elisabet,
Busquets Sílvia,
Fuster Gemma,
Figueras Maria T.,
Oliveira Cibely Cristine Fontes De,
Toledo Míriam,
Korzeniewska Katarzyna,
Argilés Josep M.,
LópezSoriano Francisco J.
Publication year - 2011
Publication title -
muscle and nerve
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.025
H-Index - 145
eISSN - 1097-4598
pISSN - 0148-639X
DOI - 10.1002/mus.21852
Subject(s) - protein degradation , myogenesis , ubiquitin , proteolysis , muscle atrophy , agonist , protein turnover , chemistry , adenylyl cyclase , skeletal muscle , proteasome , endocrinology , medicine , biology , biochemistry , protein biosynthesis , signal transduction , receptor , gene , enzyme
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 β 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 β 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. Muscle Nerve 43: 268–273, 2011