A putative second messenger of insulin action regulates hepatic microsomal glucose-6-phosphatase.
Physiological concentrations of insulin suppressed rat liver microsomal glucose-6-phosphatase activity in vitro. To attest a hypothesis that a putative second messenger of insulin action (insulin mediator) mediated this process, we isolated the low molecular factor from insulin-treated plasma membranes of rat liver, which was acid- and heat-stable substance of a peptide nature. The insulin mediator which was proved to activate the mitochondria pyruvate dehydrogenase suppressed microsomal glucose-6-phosphatase. The insulin mediator was linked to suppression of the gluconeogenic enzyme through the control of non-specific phosphohydroxylase.
D000818:Animals; D002462:Cell Membrane / Q000502:physiology; D005952:Glucose-6-Phosphatase / Q000378:metabolism*; D007295:Inositol Phosphates; D007328:Insulin / Q000494:pharmacology*; D007700:Kinetics; D008099:Liver / Q000502:physiology*; D008297:Male; D008862:Microsomes, Liver / Q000187:drug effects / Q000201:enzymology*; D011134:Polysaccharides; D051381:Rats; D011919:Rats, Inbred Strains; D011972:Receptor, Insulin / Q000302:isolation & purification / Q000502:physiology*
D007295:Inositol Phosphates; D007328:Insulin; D011134:Polysaccharides; C028039:inositol phosphate glycan; D011972:Receptor, Insulin; D005952:Glucose-6-Phosphatase