Guanine nucleotides can activate the insulin-stimulated phosphodiesterase in liver plasma membranes.
The insulin-stimulated cyclic AMP phosphodiesterase from liver plasma membranes is shown to be activated upon incubation with guanine nucleotides in the presence of ATP. The non-hydrolysable analogue of ATP, adenylyl imidodiphosphate failed to substitute for ATP in achieving activation. GTP, its non-hydrolysable analogues p[NH]ppG and GTP-gamma-S, as well as GDP, all elicited activation. It is suggested that guanine nucleotides, and probably insulin, exert their effect on this enzyme through a distinct species of guanine nucleotide regulatory protein.
D015105:3',5'-Cyclic-AMP Phosphodiesterases / Q000378:metabolism*; D000818:Animals; D002462:Cell Membrane / Q000201:enzymology; D004789:Enzyme Activation / Q000187:drug effects; D006150:Guanine Nucleotides / Q000494:pharmacology*; D006160:Guanosine Triphosphate / Q000494:pharmacology; D066298:In Vitro Techniques; D007328:Insulin / Q000494:pharmacology*; D008099:Liver / Q000201:enzymology*; D008297:Male; D051381:Rats; D011919:Rats, Inbred Strains
D006150:Guanine Nucleotides; D007328:Insulin; D006160:Guanosine Triphosphate; D015105:3',5'-Cyclic-AMP Phosphodiesterases