{"title":"进一步证明经典α1A-和克隆α1c-肾上腺素受体是同一亚型","authors":"Carmen Pimoule, Salomon Z. Langer, David Graham","doi":"10.1016/0922-4106(95)90015-2","DOIUrl":null,"url":null,"abstract":"<div><p>We compared the inactivation of [<sup>3</sup>H]prazosin binding sites in membrane preparations of cell-lines expressing the cloned <em>α</em><sub>1b</sub>, <em>α</em><sub>1c</sub> and <em>α</em><sub>1d</sub>-adrenoceptors after pretreatment with the alkylating agents, 10 μM chlorethylclonidine or 10 nM SZL-49 (1-(4-amino-6,7-dimethoxy-2-quinazolinyl)-4-(2-bicyclo[2.2.2]octa-2,5-diene-Z-carbonyl)-piperazine). The cloned <em>α</em><sub>1b</sub>-adrenoceptor exhibited a similar inactivation profile to that of the classical <em>α</em><sub>1B</sub>-adrenoceptor of rat liver in that chlorethylclonidine in contrast to SZL-49 produced a marked degree of inactivation. A similarity between the cloned <em>α</em><sub>1c</sub>-adrenoceptor and the classical <em>α</em><sub>1A</sub>-adrenoceptor of rat submaxillary gland was also noted in that both subtypes were highly sensitive to SZL-49 but relatively insensitive to chlorethylclonidine. The cloned <em>α</em><sub>1d</sub>-adrenoceptor displayed a unique profile in that both chlorethylclonidine and SZL-49 produced a marked inactivation of this subtype. The similarity of the alkylation-inactivation profiles between the cloned <em>α</em><sub>1c</sub> and classical <em>α</em><sub>1A</sub>-adrenoceptors support the recent proposal that these two <em>α</em><sub>1</sub>-adrenoceptors in fact correspond to the same subtype.</p></div>","PeriodicalId":100502,"journal":{"name":"European Journal of Pharmacology: Molecular Pharmacology","volume":"290 1","pages":"Pages 49-53"},"PeriodicalIF":0.0000,"publicationDate":"1995-06-23","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0922-4106(95)90015-2","citationCount":"12","resultStr":"{\"title\":\"Further evidence that the classical α1A- and cloned α1c-adrenoceptors are the same subtype\",\"authors\":\"Carmen Pimoule, Salomon Z. Langer, David Graham\",\"doi\":\"10.1016/0922-4106(95)90015-2\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<div><p>We compared the inactivation of [<sup>3</sup>H]prazosin binding sites in membrane preparations of cell-lines expressing the cloned <em>α</em><sub>1b</sub>, <em>α</em><sub>1c</sub> and <em>α</em><sub>1d</sub>-adrenoceptors after pretreatment with the alkylating agents, 10 μM chlorethylclonidine or 10 nM SZL-49 (1-(4-amino-6,7-dimethoxy-2-quinazolinyl)-4-(2-bicyclo[2.2.2]octa-2,5-diene-Z-carbonyl)-piperazine). The cloned <em>α</em><sub>1b</sub>-adrenoceptor exhibited a similar inactivation profile to that of the classical <em>α</em><sub>1B</sub>-adrenoceptor of rat liver in that chlorethylclonidine in contrast to SZL-49 produced a marked degree of inactivation. A similarity between the cloned <em>α</em><sub>1c</sub>-adrenoceptor and the classical <em>α</em><sub>1A</sub>-adrenoceptor of rat submaxillary gland was also noted in that both subtypes were highly sensitive to SZL-49 but relatively insensitive to chlorethylclonidine. The cloned <em>α</em><sub>1d</sub>-adrenoceptor displayed a unique profile in that both chlorethylclonidine and SZL-49 produced a marked inactivation of this subtype. The similarity of the alkylation-inactivation profiles between the cloned <em>α</em><sub>1c</sub> and classical <em>α</em><sub>1A</sub>-adrenoceptors support the recent proposal that these two <em>α</em><sub>1</sub>-adrenoceptors in fact correspond to the same subtype.</p></div>\",\"PeriodicalId\":100502,\"journal\":{\"name\":\"European Journal of Pharmacology: Molecular Pharmacology\",\"volume\":\"290 1\",\"pages\":\"Pages 49-53\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"1995-06-23\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://sci-hub-pdf.com/10.1016/0922-4106(95)90015-2\",\"citationCount\":\"12\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"European Journal of Pharmacology: Molecular Pharmacology\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://www.sciencedirect.com/science/article/pii/0922410695900152\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"European Journal of Pharmacology: Molecular Pharmacology","FirstCategoryId":"1085","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/0922410695900152","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
Further evidence that the classical α1A- and cloned α1c-adrenoceptors are the same subtype
We compared the inactivation of [3H]prazosin binding sites in membrane preparations of cell-lines expressing the cloned α1b, α1c and α1d-adrenoceptors after pretreatment with the alkylating agents, 10 μM chlorethylclonidine or 10 nM SZL-49 (1-(4-amino-6,7-dimethoxy-2-quinazolinyl)-4-(2-bicyclo[2.2.2]octa-2,5-diene-Z-carbonyl)-piperazine). The cloned α1b-adrenoceptor exhibited a similar inactivation profile to that of the classical α1B-adrenoceptor of rat liver in that chlorethylclonidine in contrast to SZL-49 produced a marked degree of inactivation. A similarity between the cloned α1c-adrenoceptor and the classical α1A-adrenoceptor of rat submaxillary gland was also noted in that both subtypes were highly sensitive to SZL-49 but relatively insensitive to chlorethylclonidine. The cloned α1d-adrenoceptor displayed a unique profile in that both chlorethylclonidine and SZL-49 produced a marked inactivation of this subtype. The similarity of the alkylation-inactivation profiles between the cloned α1c and classical α1A-adrenoceptors support the recent proposal that these two α1-adrenoceptors in fact correspond to the same subtype.