Pertussis toxin catalyzed ADP-ribosylation of a 41 kDa G-protein impairs insulin-stimulated glucose metabolism in BC3H-1 myocytes

Journal of Cellular Physiology
R S Moises, K A Heidenreich

Abstract

In this study, we examined the effects of pertussis toxin (PT) on the ADP-ribosylation of guanine nucleotide binding proteins (G-proteins) and various insulin-stimulated processes in cultured BC3H-1 myocytes. Treatment of intact myocytes with 0.1 microgram/ml PT for 24 hours resulted in the complete ribosylation of a 41 kDa protein. The 41 kDa PT substrate was immunoprecipitated with antibodies directed against a synthetic peptide corresponding to a unique sequence in the alpha subunit of Gi-proteins. PT treatment of intact cells had no effect on insulin receptor binding or internalization. However, PT inhibited insulin-stimulated glucose transport at all insulin-concentrations tested (1-100 ng/ml). Maximally stimulated glucose transport was reduced by 50% +/- 15%. Insulin-stimulated glucose oxidation was also decreased by 31% +/- 8%. The toxin had no significant effect on the basal rates of glucose transport and glucose oxidation. The time course of PT-induced inhibition on glucose transport correlated with the time course of the "in vivo" ADP-ribosylation of the 41 kDa protein. The results suggest that a 41 kDa PT-sensitive G-protein, identical or very similar to Gi, is involved in the regulation of glucose metabolism by insu...Continue Reading

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Citations

Nov 1, 1993·Journal of Cellular Biochemistry·R Ravindra, J F Caro
Mar 1, 1995·Endocrine·J L Larsen, T W Burkman
Apr 23, 1999·Journal of Basic and Clinical Physiology and Pharmacology·M A Rizzo, G Romero
Dec 8, 2017·PLoS Pathogens·Zachary Freyberg, Eric T Harvill
Feb 14, 1992·Biochemical and Biophysical Research Communications·R S Moises, K A Heidenreich

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