Different sensitivities to agonist of muscarinic acetylcholine receptor subtypes

Hideaki Bujo; Junichi Nakai; Tai Kubo; Kazuhiko Fukuda; Isamu Akiba; Akito Maeda; Masayoshi Mishina; Shosaku Numa

doi:10.1016/0014-5793(88)80346-6

Different sensitivities to agonist of muscarinic acetylcholine receptor subtypes

Hideaki Bujo, Junichi Nakai, Tai Kubo, Kazuhiko Fukuda, Isamu Akiba, Akito Maeda, Masayoshi Mishina, Shosaku Numa

Research output: Contribution to journal › Article

30 Citations (Scopus)

Abstract

Muscarinic acetylcholine receptor (mAChR) III expressed in Xenopus oocytes, like mAChR I, mediates activation of a Ca²⁺-dependent Cl^- current, whereas mAChR IV, like mAChR II, principally induces activation of Na⁺ and K⁺ currents in a Ca²⁺-independent manner. mAChR III has a sensitivity to agonist of about one order of magnitude higher than that of mAChR I in mediating the Ca²⁺-dependent current response in Xenopus oocytes and in stimulating phosphoinositide hydrolysis in NG108-15 neuroblastoma-glioma hybrid cells. The agonist-binding affinity of mAChR III is also about one order of magnitude higher than that of mAChR I.

Original language	English
Pages (from-to)	95-100
Number of pages	6
Journal	FEBS Letters
Volume	240
Issue number	1-2
DOIs	https://doi.org/10.1016/0014-5793(88)80346-6
Publication status	Published - 1988 Nov 21
Externally published	Yes

Keywords

Agonist-binding affinity
Ca-dependent Cl current
K current
Muscarinic acetylcholine receptor subtype
Na current
Phosphoinositide hydrolysis
Sensitivity to agonist

ASJC Scopus subject areas

Biophysics
Structural Biology
Biochemistry
Molecular Biology
Genetics
Cell Biology

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Bujo, H., Nakai, J., Kubo, T., Fukuda, K., Akiba, I., Maeda, A., Mishina, M., & Numa, S. (1988). Different sensitivities to agonist of muscarinic acetylcholine receptor subtypes. FEBS Letters, 240(1-2), 95-100. https://doi.org/10.1016/0014-5793(88)80346-6

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abstract = "Muscarinic acetylcholine receptor (mAChR) III expressed in Xenopus oocytes, like mAChR I, mediates activation of a Ca2+-dependent Cl- current, whereas mAChR IV, like mAChR II, principally induces activation of Na+ and K+ currents in a Ca2+-independent manner. mAChR III has a sensitivity to agonist of about one order of magnitude higher than that of mAChR I in mediating the Ca2+-dependent current response in Xenopus oocytes and in stimulating phosphoinositide hydrolysis in NG108-15 neuroblastoma-glioma hybrid cells. The agonist-binding affinity of mAChR III is also about one order of magnitude higher than that of mAChR I.",

keywords = "Agonist-binding affinity, Ca-dependent Cl current, K current, Muscarinic acetylcholine receptor subtype, Na current, Phosphoinositide hydrolysis, Sensitivity to agonist",

author = "Hideaki Bujo and Junichi Nakai and Tai Kubo and Kazuhiko Fukuda and Isamu Akiba and Akito Maeda and Masayoshi Mishina and Shosaku Numa",

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AU - Bujo, Hideaki

AU - Nakai, Junichi

AU - Kubo, Tai

AU - Fukuda, Kazuhiko

AU - Akiba, Isamu

AU - Maeda, Akito

AU - Mishina, Masayoshi

AU - Numa, Shosaku

PY - 1988/11/21

Y1 - 1988/11/21

N2 - Muscarinic acetylcholine receptor (mAChR) III expressed in Xenopus oocytes, like mAChR I, mediates activation of a Ca2+-dependent Cl- current, whereas mAChR IV, like mAChR II, principally induces activation of Na+ and K+ currents in a Ca2+-independent manner. mAChR III has a sensitivity to agonist of about one order of magnitude higher than that of mAChR I in mediating the Ca2+-dependent current response in Xenopus oocytes and in stimulating phosphoinositide hydrolysis in NG108-15 neuroblastoma-glioma hybrid cells. The agonist-binding affinity of mAChR III is also about one order of magnitude higher than that of mAChR I.

AB - Muscarinic acetylcholine receptor (mAChR) III expressed in Xenopus oocytes, like mAChR I, mediates activation of a Ca2+-dependent Cl- current, whereas mAChR IV, like mAChR II, principally induces activation of Na+ and K+ currents in a Ca2+-independent manner. mAChR III has a sensitivity to agonist of about one order of magnitude higher than that of mAChR I in mediating the Ca2+-dependent current response in Xenopus oocytes and in stimulating phosphoinositide hydrolysis in NG108-15 neuroblastoma-glioma hybrid cells. The agonist-binding affinity of mAChR III is also about one order of magnitude higher than that of mAChR I.

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