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Biosci Rep. 2008 Dec;28(6):299-306. doi: 10.1042/BSR20080055.

Molecular cloning and characterization of a novel human variant of RIC-3, a putative chaperone of nicotinic acetylcholine receptors.

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  • 1Siena Biotech S.p.A, Strada del Petriccio e Belriguardo 35, 53100 Siena, Italy.


Recent reports demonstrate that the RIC-3 (resistant to inhibitors of cholinesterase-3) protein is important for the maturation of nAChRs (nicotinic acetylcholine receptors). In the present study RIC-3e, a novel variant of RIC-3, is described. This variant contains a deletion of exons 4 and 5 of RIC-3, resulting in a protein product lacking a conserved coiled-coil domain. Like RIC-3, the new variant is predominantly, but not exclusively, expressed in the brain. The analysis of expression of variant RIC-3 mRNA and of alpha7-nAChR mRNA in a set of human tissues shows a similar profile. The RIC-3e protein is functionally active and enables surface expression of mature alpha7-nAChRs in cell lines not otherwise permissive for the expression of this receptor.

[PubMed - indexed for MEDLINE]
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