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Neuronal nicotinic acetylcholine receptors (nAChRs) were expressed in Xenopus laevis oocytes after nuclear injection of complementary deoxyribonucleic acid (cDNA) expression vectors. The two receptor subtypes alpha 4/n alpha 1 and alpha 3/n alpha 1 were readily distinguishable from one another by ACh sensitivity and desensitization. alpha 3/n alpha 1 receptors showed lower ACh sensitivity and stronger desensitization than alpha 4/n alpha 1 receptors. Furthermore, although the current/voltage relationship was very similar in both receptor subtypes, the voltage dependence of desensitization was found to be strikingly different. As the n alpha 1 subunit was unchanged, the alpha subunits must be responsible for these functional differences. Symmetric hybrid alpha cDNAs, alpha 4:alpha 3 and alpha 3:alpha 4, were constructed and functional receptors were obtained by co-injection with n alpha 1. These hybrid receptors displayed an ACh sensitivity that was mainly defined by the extracellular sequence of the alpha subunit. In contrast, no part of the alpha subunit was found fully to determine desensitization.
Abramson,
Identification of nicotinic receptor ACh-binding subunits.
1990, Pubmed
Abramson,
Identification of nicotinic receptor ACh-binding subunits.
1990,
Pubmed
Ballivet,
Electrophysiology of a chick neuronal nicotinic acetylcholine receptor expressed in Xenopus oocytes after cDNA injection.
1988,
Pubmed
,
Xenbase
Bertrand,
Activation and blocking of neuronal nicotinic acetylcholine receptor reconstituted in Xenopus oocytes.
1990,
Pubmed
,
Xenbase
Bertrand,
DATAC: a multipurpose biological data analysis program based on a mathematical interpreter.
1986,
Pubmed
Boulter,
Functional expression of two neuronal nicotinic acetylcholine receptors from cDNA clones identifies a gene family.
1987,
Pubmed
,
Xenbase
Boyd,
Expression and regulation of neuronal acetylcholine receptor mRNA in chick ciliary ganglia.
1988,
Pubmed
Cachelin,
Desensitization of the acetylcholine receptor of frog end-plates measured in a Vaseline-gap voltage clamp.
1989,
Pubmed
Changeux,
Acetylcholine receptor: an allosteric protein.
1984,
Pubmed
Couturier,
A neuronal nicotinic acetylcholine receptor subunit (alpha 7) is developmentally regulated and forms a homo-oligomeric channel blocked by alpha-BTX.
1990,
Pubmed
,
Xenbase
Couturier,
Alpha 5, alpha 3, and non-alpha 3. Three clustered avian genes encoding neuronal nicotinic acetylcholine receptor-related subunits.
1990,
Pubmed
,
Xenbase
Deneris,
Pharmacological and functional diversity of neuronal nicotinic acetylcholine receptors.
1991,
Pubmed
,
Xenbase
Dunn,
Activation and desensitization of Torpedo acetylcholine receptor: evidence for separate binding sites.
1982,
Pubmed
Hopfield,
Functional modulation of the nicotinic acetylcholine receptor by tyrosine phosphorylation.
1988,
Pubmed
Huganir,
Phosphorylation of the nicotinic acetylcholine receptor regulates its rate of desensitization.
,
Pubmed
Kao,
Identification of the alpha subunit half-cystine specifically labeled by an affinity reagent for the acetylcholine receptor binding site.
1984,
Pubmed
Kao,
Acetylcholine receptor binding site contains a disulfide cross-link between adjacent half-cystinyl residues.
1986,
Pubmed
Mathie,
Rectification of currents activated by nicotinic acetylcholine receptors in rat sympathetic ganglion neurones.
1990,
Pubmed
Nef,
Genes expressed in the brain define three distinct neuronal nicotinic acetylcholine receptors.
1988,
Pubmed
Ochoa,
Desensitization of the nicotinic acetylcholine receptor: molecular mechanisms and effect of modulators.
1989,
Pubmed
Sumikawa,
Change in desensitization of cat muscle acetylcholine receptor caused by coexpression of Torpedo acetylcholine receptor subunits in Xenopus oocytes.
1989,
Pubmed
,
Xenbase
Unwin,
Arrangement of the acetylcholine receptor subunits in the resting and desensitized states, determined by cryoelectron microscopy of crystallized Torpedo postsynaptic membranes.
1988,
Pubmed
