ISSN:
1432-2013
Keywords:
Allosteric model Binding Gating Neuronal nicotinic receptors Single channel
Source:
Springer Online Journal Archives 1860-2000
Topics:
Medicine
Notes:
Abstract. Previous studies have shown that the gating mechanism of α3β4 neuronal nicotinic receptors is affected by a residue in the middle of the M2-M3 loop of the β4 subunit. We have extended the study of the same location to the α3 subunit. Bovine α3β4 receptors were mutated in position 268, substituting the residue present in wild-type receptors, i.e. leucine in α3 and asparagine in β4, for an aspartate. Wild-type and mutated α3 and β4 subunits were combined to form four different receptors. We have measured macroscopic currents in Xenopus oocytes elicited by nicotine, and related them to surface receptor expression measured with an epibatidine-binding essay. We also obtained single-channel recordings of the receptors to study their kinetic behaviour. The results were analysed in terms of an allosteric model with three states. We found that the effect of the mutation in the α3 subunit on the gating of the receptor was similar to the corresponding mutation in the β4 subunit. The effect when both subunits were mutated was additive, suggesting that the contribution of each subunit to the gating mechanism is independent.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1007/s004249900143
Permalink
