Non-hormonal and hormonal control of glycogen metabolism in isolated sheep liver cells

The International Journal of Biochemistry
C MorandC Demigné

Abstract

1. Control of glycogen metabolism by various substrates and hormones was studied in ruminant liver using isolated hepatocytes from fed sheep. 2. In these cells glucose appeared uneffective to stimulate glycogen synthesis whereas fructose and propionate activated glycogen synthase owing to (i) a decrease in phosphorylase a activity and (ii) changes in the intracellular concentrations of glucose 6-phosphate and adenine nucleotides. 3. The activation of hepatic glycogenolysis by glucagon and alpha 1-adrenergic agents was associated with increased phosphorylase a and decreased glycogen synthase activities. 4. The simultaneous changes in these two enzyme activities suggest that in sheep liver, activation of phosphorylase a is not a prerequisite step for synthase inactivation. 5. In sheep hepatocytes, in the presence of propionate and after a lag period, insulin activated glycogen synthase without affecting phosphorylase a. 6. This latter result suggests that the direct activation of glycogen synthase by insulin is mediated by a glycogen synthase-specific kinase or phosphatase. Insulin also antagonized glucagon effect on glycogen synthesis by counteracting the rise of cAMP.

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Citations

Aug 1, 1995·Molecular and Cellular Biochemistry·S Pugazhenthi, R L Khandelwal
Apr 18, 2002·Journal of Veterinary Medicine. A, Physiology, Pathology, Clinical Medicine·J B AndersenK L Ingvartsen
Dec 3, 2015·Pathology, Research and Practice·Monika VyasA Brian West
Mar 8, 2016·Journal of Dairy Science·Qian ZhangShawn S Donkin
Jan 13, 2015·Homeopathy : the Journal of the Faculty of Homeopathy·Oguz MutluFaruk Erden

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