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COMPARATIVE AND EVOLUTIONARY PHYSIOLOGY

Hormonal regulation of glycogen metabolism in white muscle slices from rainbow trout (Oncorhynchus mykiss Walbaum)

Department of Biology, The University of Western Ontario, London, Ontario N6A 5B7, Canada

Submitted 15 September 2003 ; accepted in final form 13 August 2004

To test the hypothesis that cortisol and epinephrine have direct regulatory roles in muscle glycogen metabolism and to determine what those roles might be, we developed an in vitro white muscle slice preparation from rainbow trout (Oncorhynchus mykiss Walbaum). In the absence of hormones, glycogen-depleted muscle slices obtained from exercised trout were capable of significant glycogen synthesis, and the amount of glycogen synthesized was inversely correlated with the initial postexercise glycogen content. When postexercise glycogen levels were <5 µmol/g, about 4.3 µmol/g of glycogen were synthesized, but when postexercise glycogen levels were >5 µmol/g, only about 1.7 µmol/g of glycogen was synthesized. This difference in the amount of glycogen synthesized was reflected in the degree of activation of glycogen synthase. Postexercise glycogen content also influenced the response of the muscle to 10^–8 M epinephrine and 10^–8 M dexamethasone (a glucocorticoid analog). At high glycogen levels (>5 µmol/g), epinephrine and dexamethasone stimulated glycogen phosphorylase activity and net glycogenolysis, whereas at low (<5 µmol/g) glycogen levels, glycogenesis and activation of glycogen synthase activity prevailed. These data clearly indicate not only is trout muscle capable of in situ glycogenesis, but the amount of glycogen synthesized is a function of initial glycogen content. Furthermore, whereas dexamethasone and epinephrine directly stimulate muscle glycogen metabolism, the net effect is dependent on initial glycogen content.

cortisol; glycogen phosphorylase; glycogen synthase

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