Abstract
Activation of glycogen synthase (GS) by insulin in isolated, aerated muscle was abolished when oxygen was replaced by nitrogen. Reoxygenation of the muscle after prior exposure to nitrogen restored the insulin effect. In the presence of cyanide (inhibitor of mitochondrial respiration) insulin did not activate GS. These data demonstrate that adequate mitochondrial respiration is required for insulin-mediated activation of GS.
Publication types
-
Research Support, Non-U.S. Gov't
MeSH terms
-
Adenosine Triphosphate / metabolism
-
Animals
-
Cyanides / pharmacology
-
Enzyme Activation / drug effects
-
Glycogen / metabolism
-
Glycogen Synthase / metabolism*
-
Insulin / pharmacology*
-
Male
-
Mice
-
Mitochondria, Muscle / metabolism*
-
Muscles / metabolism*
-
Nitrogen / pharmacology
-
Oxygen Consumption
-
Phosphocreatine / metabolism
Substances
-
Cyanides
-
Insulin
-
Phosphocreatine
-
Adenosine Triphosphate
-
Glycogen
-
Glycogen Synthase
-
Nitrogen