Insulin affects the ability of Gi to be ADP-ribosylated but does not elicit its phosphorylation in intact hepatocytes

N J Pyne, C M Heyworth, N W Balfour, M D Houslay

Research output: Contribution to journalArticle

18 Citations (Scopus)

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.
Original languageEnglish
Pages (from-to)251-256
Number of pages6
JournalBiochemical and Biophysical Research Communications
Volume165
Issue number1
DOIs
Publication statusPublished - 30 Nov 1989

Keywords

  • adenosine diphosphate ribose
  • adenylate cyclase
  • adenylate cyclase toxin
  • animals
  • cell membrane
  • cells, cultured
  • forskolin
  • GTP-binding proteins
  • guanylyl imidodiphosphate
  • insulin
  • kinetics
  • liver
  • male
  • pertussis toxin
  • phosphorylation
  • rats
  • rats, inbred strains
  • virulence factors, bordetella

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