Activation of glycogen phosphorylase and glycogenolysis in rat skeletal muscle by AICAR — an activator of AMP-activated protein kinase

<p>We determined whether the cell permeable molecule AICAR, whose metabolite activates AMP-activated protein kinase (AMPK) in cells, affected glycogen metabolism in rat seleus muscle preparations in vitro. The basal and insulin-stimulated rates of radiochemical lactate formation, net lactate r...

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Main Authors: Young, M, Radda, G, Leighton, B
Other Authors: Federation of European Biochemical Societies
Format: Journal article
Language:English
Published: Elsevier 1996
Subjects:
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author Young, M
Radda, G
Leighton, B
author2 Federation of European Biochemical Societies
author_facet Federation of European Biochemical Societies
Young, M
Radda, G
Leighton, B
author_sort Young, M
collection OXFORD
description <p>We determined whether the cell permeable molecule AICAR, whose metabolite activates AMP-activated protein kinase (AMPK) in cells, affected glycogen metabolism in rat seleus muscle preparations in vitro. The basal and insulin-stimulated rates of radiochemical lactate formation, net lactate release and glycogen synthesis were determined. AICAR stimulated net lactate release (but not radiochemical lactate formation) only at a basal concentration of insulin. An increased rate of glycogenolysis was the likely cause of increased net lactate release as glycogen phosphorylase activity was significantly increased by AICAR. AICAR-stimulated net lactate release and phosphorylase activity were potently inhibited by insulin.</p>
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spelling oxford-uuid:1616cd97-6eea-411c-ac17-ad4899fed69e2022-03-26T10:29:14ZActivation of glycogen phosphorylase and glycogenolysis in rat skeletal muscle by AICAR — an activator of AMP-activated protein kinaseJournal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:1616cd97-6eea-411c-ac17-ad4899fed69eBiochemistryEnglishOxford University Research Archive - ValetElsevier1996Young, MRadda, GLeighton, BFederation of European Biochemical Societies<p>We determined whether the cell permeable molecule AICAR, whose metabolite activates AMP-activated protein kinase (AMPK) in cells, affected glycogen metabolism in rat seleus muscle preparations in vitro. The basal and insulin-stimulated rates of radiochemical lactate formation, net lactate release and glycogen synthesis were determined. AICAR stimulated net lactate release (but not radiochemical lactate formation) only at a basal concentration of insulin. An increased rate of glycogenolysis was the likely cause of increased net lactate release as glycogen phosphorylase activity was significantly increased by AICAR. AICAR-stimulated net lactate release and phosphorylase activity were potently inhibited by insulin.</p>
spellingShingle Biochemistry
Young, M
Radda, G
Leighton, B
Activation of glycogen phosphorylase and glycogenolysis in rat skeletal muscle by AICAR — an activator of AMP-activated protein kinase
title Activation of glycogen phosphorylase and glycogenolysis in rat skeletal muscle by AICAR — an activator of AMP-activated protein kinase
title_full Activation of glycogen phosphorylase and glycogenolysis in rat skeletal muscle by AICAR — an activator of AMP-activated protein kinase
title_fullStr Activation of glycogen phosphorylase and glycogenolysis in rat skeletal muscle by AICAR — an activator of AMP-activated protein kinase
title_full_unstemmed Activation of glycogen phosphorylase and glycogenolysis in rat skeletal muscle by AICAR — an activator of AMP-activated protein kinase
title_short Activation of glycogen phosphorylase and glycogenolysis in rat skeletal muscle by AICAR — an activator of AMP-activated protein kinase
title_sort activation of glycogen phosphorylase and glycogenolysis in rat skeletal muscle by aicar an activator of amp activated protein kinase
topic Biochemistry
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AT raddag activationofglycogenphosphorylaseandglycogenolysisinratskeletalmusclebyaicaranactivatorofampactivatedproteinkinase
AT leightonb activationofglycogenphosphorylaseandglycogenolysisinratskeletalmusclebyaicaranactivatorofampactivatedproteinkinase