Cloning and functional characterization of a Caenorhabditis elegans muscarinic acetylcholine receptor

Citation
Jm. Hwang et al., Cloning and functional characterization of a Caenorhabditis elegans muscarinic acetylcholine receptor, RECEPT CHAN, 6(6), 1999, pp. 415-424
Citations number
26
Language
INGLESE
art.tipo
Article
Categorie Soggetti
Cell & Developmental Biology
Journal title
RECEPTORS & CHANNELS
ISSN journal
1060-6823 → ACNP
Volume
6
Issue
6
Year of publication
1999
Pages
415 - 424
Database
ISI
SICI code
1060-6823(1999)6:6<415:CAFCOA>2.0.ZU;2-8
Abstract
A cDNA clone encoding a muscarinic acetylcholine receptor (mAChR) has been isolated from the nematode Caenorhabditis elegans, The nematode mAChR, cons isted of 585 amino acids, displays a high degree of amino acid sequence hom ology to other invertebrate and vertebrate mAChRs, Excluding a highly varia ble middle portion of the third intracellular loop, the C. elegans mAChR sh ares about 51% amino acid sequence identity with a Drosophila mAChR and 42- 44% identity with human m1-m5 mAChR subtypes, Comparison of the cDNA sequen ce with the corresponding genomic sequence reveals that the C. elegans mACh R gene contains ten introns, eight of them in the coding region. Pharmacolo gical profiles of the C. elegans mAChR expressed in Chinese hamster ovary ( CHO) cells were shown to be similar to those of mammalian counterparts, ind icating that ligand binding domains of the receptor have been conserved dur ing evolution. When this cloned receptor was expressed in Xenopus oocytes, acetylcholine evoked a transient Cl- current. Furthermore, activation of th e receptor with oxotremorine, acetylcholine or carbachol resulted in the st imulation of phosphatidylinositol metabolism in CHO cells, suggesting that the receptor is coupled to phospholipase C activation.