毒蕈碱乙酰胆碱受体
氟烷
毒蕈碱乙酰胆碱受体M5
药理学
麻醉剂
乙酰胆碱
受体
毒蕈碱乙酰胆碱受体M4
爪蟾
毒蕈碱乙酰胆碱受体M3
内分泌学
细胞生物学
医学
内科学
生物
生物化学
麻醉
基因
出处
期刊:Anesthesiology
[Ovid Technologies (Wolters Kluwer)]
日期:1995-01-01
卷期号:82 (1): 174-182
被引量:63
标识
DOI:10.1097/00000542-199501000-00022
摘要
Background Interactions between volatile anesthetics and muscarinic acetylcholine receptors have been studied primarily in binding assays or in functional systems derived from tissues or cells, often containing multiple receptor subtypes. Because interactions with muscarinic signaling systems may explain some effects and side effects of anesthetics and form a model for anesthetic-protein interactions in general, the author studied anesthetic inhibition of muscarinic signaling in an isolated system. Methods mRNA encoding the m1 muscarinic receptor subtype was prepared in vitro and expressed in Xenopus oocytes. Effects of halothane on methylcholine-induced intracellular Ca2+ release was measured. Angiotensin II receptors were expressed to evaluate anesthetic effects on intracellular signaling. Results m1 Receptors expressed in oocytes were functional, and could be inhibited by atropine and pirenzepine. Halothane depressed m1 muscarinic signaling in a dose-dependent manner: half-maximal inhibition of 10(-7) M methylcholine was obtained with 0.3 mM halothane. The effect was reversible and could be overcome by high concentrations of muscarinic agonist. Angiotensin II signaling was unaffected by 0.34 mM halothane. Conclusions m1 Muscarinic signaling is inhibited by halothane, and lack of halothane effect on angiotensin signaling indicates that the intracellular signaling systems of Xenopus oocytes are unaffected. Therefore, the most likely site of halothane action is the receptor and/or G protein. Oocytes provide a versatile system for detailed investigation into the molecular mechanism of anesthetic-protein interactions.
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