{"title":"鞘氨醇抑制大鼠腮腺腺泡细胞毒蕈碱胆碱能受体结合。","authors":"Y Fujita, H Sugiya","doi":"","DOIUrl":null,"url":null,"abstract":"<p><p>1. Sphingosine inhibited the binding of [3H]quinuclidinyl benzilate (QNB), a potent and specific muscarinic antagonist, in dispersed rat parotid acinar cells. 2. The inhibition of [3H]QNB binding was expressed as decrease in affinity without significant change of a number of membrane sites. 3. The effect of sphingosine on the binding was not affected by the chelation of extracellular Ca2+. 4. H-7, an inhibitor of protein kinase C, failed to decrease [3H]QNB binding. 5. Stearylamine, an analogue of sphingosine, was as effective as sphingosine in inhibiting [3H]QNB binding. 6. These results suggest that sphingosine inhibits muscarinic cholinergic receptor binding by a mechanism that is independent on extracellular Ca2+ and protein kinase C.</p>","PeriodicalId":10579,"journal":{"name":"Comparative biochemistry and physiology. C, Comparative pharmacology and toxicology","volume":"103 2","pages":"269-72"},"PeriodicalIF":0.0000,"publicationDate":"1992-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Sphingosine inhibits muscarinic cholinergic receptor binding in rat parotid acinar cells.\",\"authors\":\"Y Fujita, H Sugiya\",\"doi\":\"\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>1. Sphingosine inhibited the binding of [3H]quinuclidinyl benzilate (QNB), a potent and specific muscarinic antagonist, in dispersed rat parotid acinar cells. 2. The inhibition of [3H]QNB binding was expressed as decrease in affinity without significant change of a number of membrane sites. 3. The effect of sphingosine on the binding was not affected by the chelation of extracellular Ca2+. 4. H-7, an inhibitor of protein kinase C, failed to decrease [3H]QNB binding. 5. Stearylamine, an analogue of sphingosine, was as effective as sphingosine in inhibiting [3H]QNB binding. 6. These results suggest that sphingosine inhibits muscarinic cholinergic receptor binding by a mechanism that is independent on extracellular Ca2+ and protein kinase C.</p>\",\"PeriodicalId\":10579,\"journal\":{\"name\":\"Comparative biochemistry and physiology. C, Comparative pharmacology and toxicology\",\"volume\":\"103 2\",\"pages\":\"269-72\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"1992-10-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Comparative biochemistry and physiology. C, Comparative pharmacology and toxicology\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Comparative biochemistry and physiology. C, Comparative pharmacology and toxicology","FirstCategoryId":"1085","ListUrlMain":"","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
Sphingosine inhibits muscarinic cholinergic receptor binding in rat parotid acinar cells.
1. Sphingosine inhibited the binding of [3H]quinuclidinyl benzilate (QNB), a potent and specific muscarinic antagonist, in dispersed rat parotid acinar cells. 2. The inhibition of [3H]QNB binding was expressed as decrease in affinity without significant change of a number of membrane sites. 3. The effect of sphingosine on the binding was not affected by the chelation of extracellular Ca2+. 4. H-7, an inhibitor of protein kinase C, failed to decrease [3H]QNB binding. 5. Stearylamine, an analogue of sphingosine, was as effective as sphingosine in inhibiting [3H]QNB binding. 6. These results suggest that sphingosine inhibits muscarinic cholinergic receptor binding by a mechanism that is independent on extracellular Ca2+ and protein kinase C.