Potentiation of Rho-A-mediated lysophosphatidic acid activity by hyperinsulinemia

J Biol Chem. 2000 Oct 13;275(41):31792-7. doi: 10.1074/jbc.M004798200.

Abstract

We have shown previously that insulin promotes phosphorylation and activation of farnesyltransferase and geranylgeranyltransferase (GGTase) II. We have now examined the effect of insulin on geranylgeranyltransferase I in MCF-7 breast cancer cells. Insulin increased GGTase I activity 3-fold and augmented the amounts of geranylgeranylated Rho-A by 18%. Both effects of the insulin were blocked by an inhibitor of GGTase I, GGTI-286. The insulin-induced increases in the amounts of geranylgeranylated Rho-A resulted in potentiation of the Rho-A-mediated effects of lysophosphatidic acid (LPA) on a serum response element-luciferase construct. Preincubation of cells with insulin augmented the LPA-stimulated serum response element-luciferase activation to 12-fold, compared with just 6-fold for LPA alone (p < 0.05). The potentiating effect of insulin was dose-dependent, inhibited by GGTI-286 and not mimicked by insulin-like growth factor-1. We conclude that insulin activates GGTase I, increases the amounts of geranylgeranylated Rho-A protein, and potentiates the Rho-A-dependent nuclear effects of LPA in MCF-7 breast cancer cells.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Alkyl and Aryl Transferases / antagonists & inhibitors
  • Alkyl and Aryl Transferases / metabolism*
  • Breast Neoplasms
  • DNA-Binding Proteins / physiology
  • Dose-Response Relationship, Drug
  • Drug Synergism
  • Enzyme Activation / drug effects
  • Enzyme Inhibitors / pharmacology
  • Genes, Reporter / genetics
  • Guanosine Triphosphate / metabolism
  • Humans
  • Hyperinsulinism / enzymology
  • Hyperinsulinism / metabolism
  • Insulin / pharmacology*
  • Insulin-Like Growth Factor I / pharmacology
  • Luciferases / genetics
  • Lysophospholipids / pharmacology*
  • Nuclear Proteins / physiology
  • Phosphorylation / drug effects
  • Protein Processing, Post-Translational / drug effects
  • Response Elements / genetics
  • Serum Response Factor
  • Transcriptional Activation / drug effects
  • Tumor Cells, Cultured
  • rhoA GTP-Binding Protein / metabolism*

Substances

  • DNA-Binding Proteins
  • Enzyme Inhibitors
  • Insulin
  • Lysophospholipids
  • Nuclear Proteins
  • Serum Response Factor
  • Insulin-Like Growth Factor I
  • Guanosine Triphosphate
  • Luciferases
  • Alkyl and Aryl Transferases
  • geranylgeranyltransferase type-I
  • rhoA GTP-Binding Protein