Functional expression and properties of a nicotinic α9/5-HT3 A chimeric receptor

Miguel Verbitsky; Paola V. Plazas; A. Belén Elgoyhen

doi:10.1097/00001756-200310270-00010

Functional expression and properties of a nicotinic α9/5-HT3 A chimeric receptor

Miguel Verbitsky, Paola V. Plazas, A. Belén Elgoyhen

Research output: Contribution to journal › Article › peer-review

1 Scopus citations

Abstract

We cescribe the functional properties of a nicotinic α9/serotonin subtype 3A (5HT3_A) chimeric receptor expressed in Xenopus laevis oocytes. The chimera preserved ligand-binding properties of α9 and channel properties of 5HT3_A.Thus, it responded to acetylcholine in a concentration-dependent manner with an EC₅₀ of 70 μM but not to serotonin. It was blocked by methyllycaconitine, strychnine, atropine and nicotine, with the same rank order of potency as α9 receptors. The current-voltage relationship of currents through the α9/5HT3_A chimera was similar to that of the 5HT3_A receptors. These results are an evidence of functional coupling between the ligand-binding and the channel domains of the chimeric receptor.

Original language	English (US)
Pages (from-to)	1931-1934
Number of pages	4
Journal	NeuroReport
Volume	14
Issue number	15
DOIs	https://doi.org/10.1097/00001756-200310270-00010
State	Published - Oct 27 2003
Externally published	Yes

Keywords

Hair cells
Ion channels
Nicotinic receptors
Serotonin receptors

ASJC Scopus subject areas

General Neuroscience

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10.1097/00001756-200310270-00010

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abstract = "We cescribe the functional properties of a nicotinic α9/serotonin subtype 3A (5HT3A) chimeric receptor expressed in Xenopus laevis oocytes. The chimera preserved ligand-binding properties of α9 and channel properties of 5HT3A.Thus, it responded to acetylcholine in a concentration-dependent manner with an EC50 of 70 μM but not to serotonin. It was blocked by methyllycaconitine, strychnine, atropine and nicotine, with the same rank order of potency as α9 receptors. The current-voltage relationship of currents through the α9/5HT3A chimera was similar to that of the 5HT3A receptors. These results are an evidence of functional coupling between the ligand-binding and the channel domains of the chimeric receptor.",

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AU - Elgoyhen, A. Belén

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N2 - We cescribe the functional properties of a nicotinic α9/serotonin subtype 3A (5HT3A) chimeric receptor expressed in Xenopus laevis oocytes. The chimera preserved ligand-binding properties of α9 and channel properties of 5HT3A.Thus, it responded to acetylcholine in a concentration-dependent manner with an EC50 of 70 μM but not to serotonin. It was blocked by methyllycaconitine, strychnine, atropine and nicotine, with the same rank order of potency as α9 receptors. The current-voltage relationship of currents through the α9/5HT3A chimera was similar to that of the 5HT3A receptors. These results are an evidence of functional coupling between the ligand-binding and the channel domains of the chimeric receptor.

AB - We cescribe the functional properties of a nicotinic α9/serotonin subtype 3A (5HT3A) chimeric receptor expressed in Xenopus laevis oocytes. The chimera preserved ligand-binding properties of α9 and channel properties of 5HT3A.Thus, it responded to acetylcholine in a concentration-dependent manner with an EC50 of 70 μM but not to serotonin. It was blocked by methyllycaconitine, strychnine, atropine and nicotine, with the same rank order of potency as α9 receptors. The current-voltage relationship of currents through the α9/5HT3A chimera was similar to that of the 5HT3A receptors. These results are an evidence of functional coupling between the ligand-binding and the channel domains of the chimeric receptor.

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KW - Serotonin receptors

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Functional expression and properties of a nicotinic α9/5-HT3 A chimeric receptor

Abstract

Keywords

ASJC Scopus subject areas

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