Criado_2012_J.Neurochem_123_504

Reference

Title : Expression and functional properties of alpha7 acetylcholine nicotinic receptors are modified in the presence of other receptor subunits - Criado_2012_J.Neurochem_123_504
Author(s) : Criado M , Valor LM , Mulet J , Gerber S , Sala S , Sala F
Ref : Journal of Neurochemistry , 123 :504 , 2012
Abstract :

Although alpha7 nicotinic receptors are predominantly homopentamers, previous reports have indicated that alpha7 and beta2 subunits are able to form heteromers. We have studied whether other nicotinic receptor subunits can also assemble with alpha7 subunits and the effect of this potential association. Coexpression of alpha7 with alpha2, alpha3, or beta4 subunits reduced to about half, surface alpha-bungarotoxin binding sites and acetylcholine-gated currents. This is probably because of inhibition of membrane trafficking, as the total amount of alpha7 subunits was similar in all cases and a significant proportion of mature alpha7 receptors was present inside the cell. Only beta4 subunits appeared to directly associate with alpha7 receptors at the membrane and these heteromeric receptors showed some kinetic and pharmacological differences when compared with homomeric alpha7 receptors. Finally, we emulated the situation of bovine chromaffin cells in Xenopus laevis oocytes by using the same proportion of alpha3, beta4, alpha5, and alpha7 mRNAs, finding that alpha-bungarotoxin binding was similarly reduced in spite of increased currents, apparently mediated by alpha3beta4(alpha5) receptors.

PubMedSearch : Criado_2012_J.Neurochem_123_504
PubMedID: 22913551

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Citations formats

Criado M, Valor LM, Mulet J, Gerber S, Sala S, Sala F (2012)
Expression and functional properties of alpha7 acetylcholine nicotinic receptors are modified in the presence of other receptor subunits
Journal of Neurochemistry 123 :504

Criado M, Valor LM, Mulet J, Gerber S, Sala S, Sala F (2012)
Journal of Neurochemistry 123 :504