ArticleMolecular pharmacology2011
Functional characterization of the α5(Asn398) variant associated with risk for nicotine dependence in the α3β4α5 nicotinic receptor.
Article in Molecular pharmacology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 25 citations in OpenAlex.
- The Human Alpha3 Beta2 Neuronal Nicotinic Acetylcholine Receptor Can Form Two Distinguishable Subtypes.International journal of molecular sciences · 2025Article
- A common SNP in Chrna5 enhances morphine reward in female mice.Neuropharmacology · 2022Article
- E-cigarette vape and lung ACE2 expression: Implications for coronavirus vulnerability.Environmental toxicology and pharmacology · 2021Article
- Linking the CHRNA5 SNP to drug abuse liability: From circuitry to cellular mechanisms.Neuropharmacology · 2021Review
- Concatemers to re-investigate the role of α5 in α4β2 nicotinic receptors.Cellular and molecular life sciences : CMLS · 2021Article
- The α5 Nicotinic Acetylcholine Receptor Subunit Differentially Modulates α4β2Frontiers in synaptic neuroscience · 2020Review
- Insights Into Nicotinic Receptor Signaling in Nicotine Addiction: Implications for Prevention and Treatment.Current neuropharmacology · 2018Review
- Isoform-specific mechanisms of α3β4*-nicotinic acetylcholine receptor modulation by the prototoxin lynx1.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2017Article
- Electrophysiology-Based Assays to Detect Subtype-Selective Modulation of Human Nicotinic Acetylcholine Receptors.Assay and drug development technologies · 2016Article
- Introduced Amino Terminal Epitopes Can Reduce Surface Expression of Neuronal Nicotinic Receptors.PloS one · 2016Article
- Crucial role of nicotinic α5 subunit variants for Ca2+ fluxes in ventral midbrain neurons.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2015Article
- Two rare variations, D478N and D478E, that occur at the same amino acid residue in nicotinic acetylcholine receptor (nAChR) α2 subunit influence nAChR function.Neuropharmacology · 2014Article
- A signal peptide missense mutation associated with nicotine dependence alters α2*-nicotinic acetylcholine receptor function.Neuropharmacology · 2014Article
- Probing the non-canonical interface for agonist interaction with an α5 containing nicotinic acetylcholine receptor.Neuropharmacology · 2014Article
- Functional characterization improves associations between rare non-synonymous variants in CHRNB4 and smoking behavior.PloS one · 2014Article
- Impact of human D398N single nucleotide polymorphism on intracellular calcium response mediated by α3β4α5 nicotinic acetylcholine receptors.Neuropharmacology · 2012Article
- Insights into the neurobiology of the nicotinic cholinergic system and nicotine addiction from mice expressing nicotinic receptors harboring gain-of-function mutations.Pharmacological reviews · 2012Review
- Use of an α3β4 nicotinic acetylcholine receptor subunit concatamer to characterize ganglionic receptor subtypes with specific subunit composition reveals species-specific pharmacologic properties.Neuropharmacology · 2012Article
- Function of human α3β4α5 nicotinic acetylcholine receptors is reduced by the α5(D398N) variant.The Journal of biological chemistry · 2012Article
- Modulation of gain-of-function α6*-nicotinic acetylcholine receptor by β3 subunits.The Journal of biological chemistry · 2012Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Smoking is a major cause for premature death. Work aimed at identifying genetic factors that contribute to nicotine addiction has revealed several single nucleotide polymorphisms (SNPs) that are linked to smoking-related behaviors such as nicotine dependence and level of smoking. One of these SNPs leads to an aspartic acid-to-asparagine substitution in the nicotinic receptor α5 subunit at amino acid position 398 [rs16969968; α5(Asn398)]. The α5 subunit is expressed both in the brain and in the periphery. In the brain, it associates with the α4 and β2 subunits to form α4β2α5 receptors. In the periphery, the α5 subunit combines with the α3 and β4 subunits to form the major ganglionic postsynaptic nicotinic receptor subtype. The α3β4α5 receptor regulates a variety of autonomic responses such as control of cardiac rate, blood pressure, and perfusion. In this paradigm, the α5(Asn398) variant may act by regulating autonomic responses that may affect nicotine intake by humans. Here, we have investigated the effect of the α5(Asn398) variant on the function of the α3β4α5 receptor. The wild-type or variant α5 subunits were coexpressed with the α3 and β4 subunits in human embryonic kidney 293 cells. The properties of the receptors were studied using whole-cell and single-channel electrophysiology. The data indicate that the introduction of the α5(Asn398) mutation has little effect on the pharmacology of receptor activation, receptor desensitization, or single-channel properties. We propose that the effect of the α5(Asn398) variant on nicotine use is not mediated by an action on the physiological or pharmacological properties of the α3β4α5 subtype.
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