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Activation of glycogen phosphorylase and glycogenolysis in rat skeletal muscle by AICAR — an activator of AMP‐activated protein kinase
Author(s) -
Young Martin E,
Radda George K,
Leighton Brendan
Publication year - 1996
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(96)00129-9
Subject(s) - glycogenolysis , glycogen phosphorylase , medicine , ampk , glycogen , endocrinology , glycogen synthase , chemistry , glycogenesis , phosphorylase kinase , amp activated protein kinase , glycogen branching enzyme , insulin , protein kinase a , activator (genetics) , biochemistry , kinase , biology , gene
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.