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.
LanguageEnglish
Pages251-256
Number of pages6
JournalBiochemical and Biophysical Research Communications
Volume165
Issue number1
DOIs
Publication statusPublished - 30 Nov 1989

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Phosphorylation
Adenosine Diphosphate
Hepatocytes
Insulin
Pertussis Toxin
Guanosine Triphosphate
Cell Membrane
Membranes
Guanine Nucleotides
Diphosphates
Colforsin
Cell membranes
Adenylyl Cyclases
Sulfhydryl Compounds

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

Cite this

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title = "Insulin affects the ability of Gi to be ADP-ribosylated but does not elicit its phosphorylation in intact hepatocytes",
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.",
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",
author = "Pyne, {N J} and Heyworth, {C M} and Balfour, {N W} and Houslay, {M D}",
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month = "11",
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Insulin affects the ability of Gi to be ADP-ribosylated but does not elicit its phosphorylation in intact hepatocytes. / Pyne, N J; Heyworth, C M; Balfour, N W; Houslay, M D.

In: Biochemical and Biophysical Research Communications, Vol. 165, No. 1, 30.11.1989, p. 251-256.

Research output: Contribution to journalArticle

TY - JOUR

T1 - Insulin affects the ability of Gi to be ADP-ribosylated but does not elicit its phosphorylation in intact hepatocytes

AU - Pyne, N J

AU - Heyworth, C M

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N2 - 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.

AB - 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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