The effect of iloprost on the ADP-ribosylation of Gs alpha (the alpha-subunit of Gs).

The Biochemical Journal
L Molina y VediaE G Lapetina

Abstract

Treatment of platelets with a prostacyclin analogue, iloprost, decreased the cholera-toxin-induced ADP-ribosylation of membrane-bound Gs alpha (alpha-subunit of G-protein that stimulates adenylate cyclase; 42 kDa protein) and a cytosolic substrate (44 kDa protein) [Molina y Vedia, Reep & Lapetina (1988) Proc. Natl. Acad. Sci. U.S.A. 85, 5899-5902]. This decrease is apparently not correlated with a significant change in the quantity of membrane Gs alpha, as detected by two Gs alpha-specific antisera. This finding contrasts with the suggestion in a previous report [Edwards, MacDermot & Wilkins (1987) Br. J. Pharmacol. 90, 501-510], indicating that iloprost caused a loss of Gs alpha from the membrane. Our evidence points to a modification in the ability of the 42 kDa protein to be ADP-ribosylated by cholera toxin. This modification of Gs alpha might be related to its ADP-ribosylation by endogenous ADP-ribosyltransferase activity. Here we present evidence showing that Gs alpha was ADP-ribosylated in platelets that had been electropermeabilized and incubated with [alpha-32P]NAD+. This endogenous ADP-ribosylation of Gs alpha is inhibited by nicotinamide and stimulated by iloprost.

Citations

Sep 1, 1994·Molecular and Cellular Biochemistry·A ZolkiewskaJ Moss
Jan 23, 1999·European Journal of Biochemistry·P FerreiraT Pfeuffer
Sep 3, 1998·The Journal of Biological Chemistry·I J Okazaki, J Moss
Dec 1, 1991·Journal of Neurochemistry·R S DumanE J Nestler
Jun 22, 1999·Journal of Neuroscience Research·S AndreopoulosJ J Warsh
Nov 1, 1994·Biochemical Pharmacology·L E DonnellyJ MacDermot
Oct 2, 1992·Brain Research·M B WilliamsR S Jope

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