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Am J Physiol Endocrinol Metab 281: E449-E454, 2001;
0193-1849/01 $5.00
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Vol. 281, Issue 3, E449-E454, September 2001

Catecholamines inhibit Ca2+-dependent proteolysis in rat skeletal muscle through beta 2-adrenoceptors and cAMP

Luiz Carlos C. Navegantes, Neusa M. Z. Resano, Renato H. Migliorini, and Ísis C. Kettelhut

Department of Physiology and Biochemistry, School of Medicine, University of São Paulo, Ribeirão Preto, 14049 - 900 São Paulo, Brazil

Overall proteolysis and the activity of skeletal muscle proteolytic systems were investigated in rats 1, 2, or 4 days after adrenodemedullation. Adrenodemedullation reduced plasma epinephrine by 95% and norepinephrine by 35% but did not affect muscle norepinephrine content. In soleus and extensor digitorum longus (EDL) muscles, rates of overall proteolysis increased by 15-20% by 2 days after surgery but returned to normal levels after 4 days. The rise in rates of protein degradation was accompanied by an increased activity of Ca2+-dependent proteolysis in both muscles, with no significant change in the activity of lysosomal and ATP-dependent proteolytic systems. In vitro rates of Ca2+-dependent proteolysis in soleus and EDL from normal rats decreased by ~35% in the presence of either 10-5 M clenbuterol, a beta 2-adrenergic agonist, or epinephrine or norepinephrine. In the presence of dibutyryl cAMP, proteolysis was reduced by 62% in soleus and 34% in EDL. The data suggest that catecholamines secreted by the adrenal medulla exert an inhibitory control of Ca2+-dependent proteolysis in rat skeletal muscle, mediated by beta 2-adrenoceptors, with the participation of a cAMP-dependent pathway.

adrenodemedullation; epinephrine; clenbuterol; dibutyryl cyclic adenosine monophosphate; proteolytic systems


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