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- Title
The neuronal α[sub 6] subunit forms functional heteromeric acetylcholine receptors in human transfected cells.
- Authors
Fucile, Sergio; Matter, Jean-Marc; Erkman, Linda; Ragozzino, Davide; Barabino, Benedetta; Grassi, Francesca; Alemà, Stefano; Ballivet, Marc; Eusebi, Fabrizio
- Abstract
We examine some of the biological and physiological properties of the avian α[sub 6] neuronal nicotinic acetylcholine receptor (nAChR) subunit. We show here that, beginning at embryonic day 5, α[sub 6] mRNA is abundantly expressed in the developing chick neuroretina, where it coexists with other nicotinic receptor subunit mRNAs such as α[sub 3], β[sub 2] and β[sub 4]. In contrast, α[sub 6] mRNA is absent from the optic tectum and from the peripheral ganglia. Despite numerous efforts, the α[sub 6] subunit has long failed the critical test of functional reconstitution. Here we use patch-clamp techniques and confocal laser microscopy to measure ACh-activated currents and nicotine-elicited Ca[sup 2+] transients in human BOSC 23 cells transfected with chick α[sub 6] in combination with other chick nAChR neuronal subunits. Heterologously expressed α[sub 6] and β[sub 4] subunits form functional heteromeric nAChRs, which are permeable to Ca[sup 2+] ions and blocked by the nicotinic antagonist methyllycaconitine (10 μm). Likewise, ACh elicits measurable currents in cells transfected with α[sub 6] and β[sub 2]. Hill analysis of the dose–response curves in cells transfected with α[sub 3], β[sub 4] and α[sub 6] cDNAs, suggests the assembly of functional α[sub 3]β[sub 4]α[sub 6] receptor, with an apparent affinity for ACh threefold lower than α[sub 3]β[sub 4]. Our results indicate that α[sub 6]-containing nAChRs assemble in heterologous expression systems and are probably present in retinal cells.
- Subjects
NICOTINIC receptors; MESSENGER RNA
- Publication
European Journal of Neuroscience, 1998, Vol 10, Issue 1
- ISSN
0953-816X
- Publication type
Article
- DOI
10.1046/j.1460-9568.1998.00001.x