Effects of onium derivatives on Na-, Cl-, and K-dependent acetylcholine receptors

• Published in: Japanese journal of physiology Vol. 30; no. 5; p. 729
• Main Authors: Matsumoto, M, Sasaki, K, Somei, K, Sato, M
• Format: Journal Article
• Language: English
• Published: Japan 1980
• Subjects: Acetylcholine - pharmacology; Animals; Aplysia - physiology; Choline - pharmacology; Decamethonium Compounds - pharmacology; Ganglia - physiology; Hexamethonium Compounds - pharmacology; In Vitro Techniques; Membrane Potentials - drug effects; Neostigmine - pharmacology; Neural Conduction - drug effects; Nicotine - pharmacology; Receptors, Cholinergic - physiology
• ISSN: 0021-521X; 1881-1396
• DOI: 10.2170/jjphysiol.30.729

Various types of acetylcholine (ACh) receptor in the pleural or abdominal ganglion cells of Aplysia were classified into three types depending on the ion species involved in the electrogenesis of their responses. The Na-dependent receptor was designated the DNa-type since the response was a depolarization (D) produced by an increase in permeability, mainly toward Na+, although other ions were partially involved. Similarly, the Cl- or K-dependent receptor was designated the HCl- or HK-type since the response was a hyperpolarization (H) produced by an exclusive increase in permeability toward Cl- or K+. ACh-induced responses were evaluated by an increase in membrane conductance. The DNa-type receptor could be readily activated by tetramethylammonium (TMA) and choline, but not by decamethonium (Deca). Instead, it was blocked competitively either by hexamethonium (Hexa) or by Deca. The HCl-type receptor could be readily activated by TMA, choline, and Deca. Hexa did not block this type of receptor. The HK-type receptor was neither activated nor blocked by TMA, choline, Hexa, and Deca. The above findings suggested that there is a certain structural similarity in the ACh-binding site between DNa-type and HCl-type receptors, although the ion species involved in the electrogenesis of each response were totally different. The structure of the ACh-binding site at the HK-type receptor seemed considerably different from that of either DNa-type or HCl-type.