Gil-Longo J, Dufour M N, Guillon G, Lugnier C
Laboratoire de Pharmacologie Cellulaire et Moléculaire, Université Louis Pasteur de Strasbourg, Illkirch, France.
Eur J Pharmacol. 1993 Oct 15;247(2):119-25. doi: 10.1016/0922-4106(93)90068-k.
In bovine aortic endothelial cells (BAEC), pertussis toxin (PTx) ADP-ribosylated two major substrates with apparent molecular masses of 40 and 41 kDa, whereas cholera toxin (CTx) ADP-ribosylated two other substrates of 44 and 50 kDa. [alpha-32P]GTP bound to three bands in the 22-27 kDa range. Immunoblot analysis revealed the simultaneous presence of G alpha i1, G alpha i2, G alpha i3, G alpha q or G alpha 11 and of different forms of G alpha s but did not detect significant levels of G alpha 0. Bradykinin caused a 9-fold increase in intracellular cyclic GMP level in BAEC (measured as an index of NO production). Preincubation of BAEC with CTx, but not with PTx, inhibited bradykinin-dependent production of cyclic GMP. These results show that G alpha s, G alpha q or alpha 11, Gi and small GTP-binding proteins are present in BAEC and suggest that a CTx-sensitive G-protein (possibly either small G-protein, G alpha q or G alpha 11) could be associated with the bradykinin-mediated NO formation.
