ArticlePflugers Archiv : European journal of physiology2011
Mutant human β4 subunit identified in amyotrophic lateral sclerosis patients impairs nicotinic receptor function.
Article in Pflugers Archiv : European journal of physiology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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8 citing papers in PubMed, 9 citations in OpenAlex.
- Rare Missense Variants of the Human β4 Subunit Alter Nicotinic α3β4 Receptor Plasma Membrane Localisation.Molecules (Basel, Switzerland) · 2023Article
- Genetics of Amyotrophic Lateral Sclerosis.Cold Spring Harbor perspectives in medicine · 2018Review
- Insights Into Nicotinic Receptor Signaling in Nicotine Addiction: Implications for Prevention and Treatment.Current neuropharmacology · 2018Review
- VAChT overexpression increases acetylcholine at the synaptic cleft and accelerates aging of neuromuscular junctions.Skeletal muscle · 2016Article
- Habenular expression of rare missense variants of the β4 nicotinic receptor subunit alters nicotine consumption.Frontiers in human neuroscience · 2014Article
- Functional characterization improves associations between rare non-synonymous variants in CHRNB4 and smoking behavior.PloS one · 2014Article
- Trafficking of alpha4* nicotinic receptors revealed by superecliptic phluorin: effects of a beta4 amyotrophic lateral sclerosis-associated mutation and chronic exposure to nicotine.The Journal of biological chemistry · 2011Article
- Adenosine A2A receptor induces protein kinase A-dependent functional modulation of human (alpha)3(beta)4 nicotinic receptor.The Journal of physiology · 2011Article
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Authors and funding
6 authors at 2 institutions in 1 country.
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Abstract
Recently identified mutations in the genes encoding the neuronal nicotinic ACh receptor (nAChR) subunits in patients affected by sporadic amyotrophic lateral sclerosis (sALS) may represent a factor which enhances disease susceptibility, in particular in association with ambient causes such as cigarette smoking. In this work, we characterize the functional properties of nAChRs containing the β4R349C subunit, the mutation most frequently encountered in sALS patients. The mutation was coexpressed with wild-type α3 or α4 subunits or with mutant α4R487Q subunit, which has been detected in one patient together with β4R349C mutation. None of the functional parameters examined showed differences between α4β4 and α4R487Qβ4 nAChRs. By contrast, β4R349C mutation, independent of the companion α subunit, caused the reduction in potency of both ACh and nicotine, decreased the density of whole-cell current evoked by maximal transmitter concentrations, and altered the kinetics of ACh-evoked whole-cell currents. These data confirm that sALS-associated mutations in nicotinic subunits may markedly perturb cholinergic transmission in individuals bearing the mutations.
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