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  • Title: Insulin affects the ability of Gi to be ADP-ribosylated but does not elicit its phosphorylation in intact hepatocytes.
    Author: Pyne NJ, Heyworth CM, Balfour NW, Houslay MD.
    Journal: Biochem Biophys Res Commun; 1989 Nov 30; 165(1):251-6. PubMed ID: 2511846.
    Abstract:
    Insulin inhibited the ability of activated pertussis toxin to catalyse the ADP-ribosylation of alpha-Gi in isolated plasma membranes in either the absence of added guanine nucleotides or in the presence of GTP. In contrast, when the non-hydrolysable GTP analogue guanylyl-5'-imido-diphosphate (p[NH]ppG) was added to ribosylation mixtures, to inhibit the action of pertussis toxin in catalysing the ADP-ribosylation of alpha-Gi, then the addition of insulin attenuated the action of p[NH]ppG causing an increase in alpha-Gi ribosylation. Pre treatment of intact hepatocytes with insulin had no effect on the subsequent ability of thiol-preactivated pertussis toxin to cause the ADP-ribosylation of alpha Gi using isolated membranes from such cells. The ability of p[NH]ppG to inhibit forskolin-stimulated adenylate cyclase activity was attenuated in the presence of insulin. Insulin did not cause the phosphorylation of alpha-Gi in either intact hepatocytes or in isolated membranes.
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