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

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 wi...

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Detalles Bibliográficos
Autores principales: Verbitsky, M., Plazas, P.V., Elgoyhen, A.B.
Formato: JOUR
Materias:
Hair cells
Ion channels
Nicotinic receptors
Serotonin receptors
acetylcholine
atropine
chimeric protein
cholinergic receptor blocking agent
glycine receptor antagonist
methyllycaconitine
muscarinic receptor blocking agent
nicotine
nicotinic receptor
nicotinic receptor alpha5
nicotinic receptor alpha9
nicotinic receptor blocking agent
receptor subtype
receptor subunit
serotonin
serotonin 3 receptor
serotonin 3a receptor
strychnine
unclassified drug
aconitine
Chrna9 protein, rat
complementary DNA
drug derivative
hybrid protein
nicotinic agent
serotonin antagonist
animal cell
article
concentration response
drug potency
drug receptor binding
electric current
electric potential
female
ligand binding
nonhuman
oocyte
priority journal
Xenopus laevis
animal
biosynthesis
cell membrane potential
drug effect
genetics
metabolism
patch clamp
physiology
rat
Aconitine
Animals
Atropine
DNA, Complementary
Membrane Potentials
Muscarinic Antagonists
Nicotine
Nicotinic Agonists
Nicotinic Antagonists
Oocytes
Patch-Clamp Techniques
Rats
Receptors, Nicotinic
Receptors, Serotonin, 5-HT3
Recombinant Fusion Proteins
Serotonin Antagonists
Strychnine
Acceso en línea:http://hdl.handle.net/20.500.12110/paper_09594965_v14_n15_p1931_Verbitsky
Aporte de:
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires
Descripción
Sumario: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. © 2003 Lippincott Williams & Wilkins.

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