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© Marie Prévost, Institut Pasteur
Image of a portion of a Xenopus oocyte expressing a channel receptor.
Publication : Neuroreport

Paradoxical allosteric effects of competitive inhibitors on neuronal alpha7 nicotinic receptor mutants

Scientific Fields
Diseases
Organisms
Applications
Technique

Published in Neuroreport - 10 Nov 1997

Bertrand S, Devillers-Thiéry A, Palma E, Buisson B, Edelstein SJ, Corringer PJ, Changeux JP, Bertrand D

Link to Pubmed [PMID] – 9427332

Neuroreport 1997 Nov;8(16):3591-6

Mutation of the conserved leucine residue, in the second transmembrane domain of the neuronal alpha7 acetylcholine receptor to a threonine (L247T) causes pleiotropic alterations of receptor properties. In this study we examined the effects of competitive inhibitors on the alpha7-L247T physiological responses. While the alpha7 competitive inhibitor dihydro-beta-erythroidine evoked a current comparable to that induced by ACh, other inhibitors such as methyllycaconitine (MLA) and alpha-bungarotoxin (alpha-Bgt) caused a blockade of alpha7-L247T to ACh activation. When applied in the absence of ACh, MLA or alpha-Bgt reduced the cell leakage current, showing that alpha7-L247T displays a significant fraction (10%) of spontaneously open channels. These data can be interpreted in terms of an allosteric model, assuming that the L247T mutant possesses a low isomerization constant L and that MLA and alpha-Bgt stabilize the closed, resting state.

http://www.ncbi.nlm.nih.gov/pubmed/9427332