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Cloning and Expression of a G Protein‐Linked Acetylcholine Receptor from Caenorhabditis elegans
Author(s) -
Lee YongSeok,
Park YangSeo,
Chang DeokJin,
Hwang Jung Me,
Min Churl Ki,
Kaang BongKiun,
Cho Nam Jeong
Publication year - 1999
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1046/j.1471-4159.1999.0720058.x
Subject(s) - oxotremorine , muscarinic acetylcholine receptor , muscarinic acetylcholine receptor m2 , muscarinic acetylcholine receptor m5 , biology , muscarinic acetylcholine receptor m3 , muscarinic acetylcholine receptor m1 , acetylcholine , muscarinic acetylcholine receptor m4 , g protein , microbiology and biotechnology , receptor , biochemistry , endocrinology
: We have isolated a cDNA clone from the nematode Caenorhabditis elegans that encodes a protein of greatest sequencesimilarity to muscarinic acetylcholine receptors. This gene codes for apolypeptide of 682 amino acids containing seven putative transmembranedomains. The amino acid identities, excluding a highly variable middle portionof the third intracellular loop, to the human m1‐m5 receptors are 28‐34%. Whenthis cloned receptor was coexpressed with a G protein‐gated inwardlyrectifying K + channel (GIRK1) in Xenopus oocyte, acetylcholine was able to elicit the GIRK current. This acetylcholine‐induced current was substantially inhibited by the muscarinic antagonist atropine in a reversible manner. However, another muscarinic agonist oxotremorine and antagonists scopolamine and pirenzepine had little or negligible effects on this receptor. Taken together, these results suggest that the cloned gene encodes a G protein‐linked acetylcholine receptor that is most similar to but pharmacologically distinct from muscarinic acetylcholine receptors.