Unknown

Dataset Information

0

Insulin inhibits the phosphorylation of alpha-Gi-2 in intact hepatocytes.


ABSTRACT: Challenge of intact hepatocytes with insulin reduced the level of phosphorylated alpha-Gi-2 found under basal (resting) conditions. At maximally effective concentrations of insulin the steady-state labelling of alpha-Gi-2 was reduced by approximately 21%. Insulin achieved this in a time- and dose-dependent fashion, exhibiting an IC50 value of 109 +/- 22 pM. The increased labelling of alpha-Gi-2 seen after challenge of cells with phorbol 12-myristate 13-acetate was also attenuated by insulin. Treatment of hepatocytes with the protein phosphatase inhibitor okadaic acid increased the labelling of alpha-Gi-2 in a fashion which was insensitive to the action of insulin. It is suggested that insulin may reduce the level of phosphorylation of alpha-Gi-2 by stimulating intracellular protein phosphatase activity and that this action may offer a molecular explanation for the ability of insulin to inhibit adenylate cyclase activity in hepatocytes by increasing the level of non-phosphorylated alpha-Gi-2.

SUBMITTER: Morris NJ 

PROVIDER: S-EPMC1136981 | biostudies-other | 1995 Jun

REPOSITORIES: biostudies-other

Similar Datasets

| S-EPMC1131453 | biostudies-other
| S-EPMC1137044 | biostudies-other
| S-EPMC25332 | biostudies-literature
| S-EPMC1147530 | biostudies-other
| S-EPMC3534816 | biostudies-literature
| S-EPMC4113065 | biostudies-literature
| S-EPMC5118248 | biostudies-literature
| S-EPMC1138914 | biostudies-other
| S-EPMC307695 | biostudies-literature
| S-EPMC4049638 | biostudies-literature