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Discriminating between 5‐HT 3 A and 5‐HT 3 AB receptors
Author(s) -
Thompson AJ,
Lummis SCR
Publication year - 2013
Publication title -
british journal of pharmacology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.432
H-Index - 211
eISSN - 1476-5381
pISSN - 0007-1188
DOI - 10.1111/bph.12166
Subject(s) - homomeric , receptor , 5 ht receptor , allosteric regulation , protein subunit , chemistry , serotonin , class c gpcr , allosteric modulator , cys loop receptors , affinities , 5 ht1 receptor , biochemistry , agonist , biology , metabotropic receptor , acetylcholine receptor , gene , nicotinic acetylcholine receptor
The 5‐HT3B subunit was first cloned in 1999, and co‐expression with the 5‐HT3A subunit results in heteromeric 5‐HT 3 AB receptors that are functionally distinct from homomeric 5‐HT 3 A receptors. The affinities of competitive ligands at the two receptor subtypes are usually similar, but those of non‐competitive antagonists that bind in the pore often differ. A competitive ligand and allosteric modulator that distinguishes 5‐HT 3 A from 5‐HT 3 AB receptors has recently been described, and the number of non‐competitive antagonists identified with this ability has increased in recent years. In this review, we discuss the differences between 5‐HT 3 A and 5‐HT 3 AB receptors and describe the possible sites of action of compounds that can distinguish between them.