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Letters to Nature
Nature 335, 355 - 358 (22 September 1988); doi:10.1038/335355a0

Selective coupling with K+ currents of muscarinic acetylcholine receptor subtypes in NG108-15 cells

Kazuhiko Fukuda, Haruhiro Higashida*, Tai Kubo, Akito Maeda, Isamu Akiba, Hideaki Bujo, Masayoshi Mishina & Shosaku Numa

Departments of Medical Chemistry and Molecular Genetics, Kyoto University Faculty of Medicine, Kyoto 606, Japan
*Department of Biophysics, Neuroinformation Research Institute, Kanazawa University School of Medicine, Kanazawa 920, Japan

The primary structures of two muscarinic acetylcholine receptor (mAChR) species, designated as mAChR I and mAChR II, have been elucidated by cloning and sequence analysis of DNAs complementary to the porcine cerebral and cardiac messenger RNAs, respectively1–3. mAChR I and mAChR II expressed in Xenopus oocytes differ from each other both in acetylcholine-induced response and in antagonist binding properties1,4. These results, together with the differential tissue location of the two mAChR mRNAs1,2, have indicated that pharmacologically distinguishable subtypes of the mAChR represent distinct gene products. The primary structures of two additional mammalian mAChR species, designated as mAChR III and mAChR IV, have subsequently been deduced from the nucleotide sequences of the cloned cDNAs or genomic DNAs5–7. We report here that mAChR I and mAChR III expressed in NG108-15 neuroblastoma-glioma hybrid cells, but not mAChR II and mAChR IV, efficiently mediate phosphoinosi-tide hydrolysis, activation of a Ca2+-dependent K+ current and inhibition of the M-current, a voltage-dependent K+ current sensitive to muscarinic agonists.

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