Chronic exposure of rat glioma C6 cells to cholera toxin induces loss of the alpha-subunit of the stimulatory guanine nucleotide-binding protein (Gs)

European Journal of Pharmacology
C CarrG Milligan

Abstract

Rat glioma C6 BU1 cells were treated in tissue culture with cholera toxin. Incubation of membranes derived from these cells with fresh cholera toxin and [32P]NAD+ failed to promote incorporation of radioactivity into polypeptides corresponding to forms of Gs alpha. This is generally assumed to reflect prior ADP ribosylation of these polypeptides in vivo using endogenous NAD+ as substrate. However, immunological studies with anti-peptide antisera which identify all forms of Gs alpha demonstrated that concentrations of this polypeptide were now substantially reduced in the membranes. This effect was specific for Gs alpha as neither the alpha-subunits of the pertussis toxin-sensitive G-proteins Gi2 and Gi3, nor the beta subunit common to the various G-proteins were lost in parallel. Pertussis toxin-catalysed ADP ribosylation did not cause the downregulation of Gs alpha nor of the alpha-subunits of Gi2 or Gi3 although it did cause ADP ribosylation of the entire complement of both Gi2 and Gi3 in the membranes. Despite the reduction in levels of immunoreactive Gs alpha from the membranes of cholera toxin-treated cells, no alterations in levels of mRNA corresponding to this G-protein were noted.

References

Jan 1, 1986·Proceedings of the National Academy of Sciences of the United States of America·S M MumbyA G Gilman
Jan 1, 1987·Annual Review of Biochemistry·A G Gilman
Apr 15, 1988·Biochemical and Biophysical Research Communications·H McArdleG Milligan

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Citations

Jun 2, 1994·European Journal of Pharmacology·R B RaffaC D Connelly
Jul 14, 1999·Neurochemistry International·M McLaughlinJ McCulloch
Jun 1, 1991·Trends in Pharmacological Sciences·G Milligan, A Green

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