Low insulin concentrations stimulate in vitro the soluble guanylate cyclase activity of rat liver.
The soluble guanylate cyclase activity of rat liver appears to be stimulated in VITRO by insulin at pMolar concentrations, while proinsulin, denaturated insulin or desoctapeptide insulin, are not able to stimulate the studied enzymic activity. Corresponding concentrations of other peptide hormones such as corticotropin (ACTH) or glucagon, either in the absence or in the presence of bacitracin, do not show any effect on the investigated enzymic system. Insulin stimulation of the soluble guanylate cyclase is characterized by a significant increase in the Vmax together with a decrease of the apparent Km. Insulin at low concentrations doesn't affect the cyclic GMP hydrolyzing activity; conversely higher concentrations of the hormone, while exerting a less marked effect on the guanylate cyclase activity, inhibit the cyclic GMP hydrolyzing activity.
D000818:Animals; D003600:Cytosol / Q000201:enzymology; D006162:Guanylate Cyclase / Q000378:metabolism*; D007328:Insulin / Q000494:pharmacology*; D007700:Kinetics; D008099:Liver / Q000187:drug effects / Q000201:enzymology*; D011384:Proinsulin / Q000494:pharmacology; D051381:Rats; D011919:Rats, Inbred Strains; D012995:Solubility
D007328:Insulin; D011384:Proinsulin; D006162:Guanylate Cyclase