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Cross-talk between apparently independent receptors

Timothy J. Searl and Eugene M. Silinsky

Nicotinic receptors and P2X ATP receptors both incorporate transmembrane cation channels as part of the receptor moiety. However, the nicotinic and P2X ATP receptors are regarded as entirely independent molecular entities and the receptor subunits have distinctly different transmembrane topologies. Given this difference, it is of interest that recent papers (Searl et al. 1998; and two papers appearing in this issue of The Journal of Physiology: Zhou & Galligan, 1998; Barajas-Lopez et al. 1998) have confirmed earlier findings (Nakazawa et al. 1991; Silinsky & Gerzanich, 1993) that co-application of nicotinic agonists and P2X ATP receptor agonists produce less than the additive responses predicted by independent receptor activation. These papers, when taken together, suggest that such interdependent, mutually occlusive interactions are: (i) receptor mediated (as antagonists reveal full responses of the unaffected agonist); (ii) not mediated by soluble second messengers (as non-additivity is also seen in excised patches); and (iii) not due to pH changes produced by high concentrations of agonist (Wildman et al. 1997).

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