{"title":"β -肾上腺素能受体亚型介导猪脂肪细胞的脂肪分解。β3-肾上腺素能激动剂BRL-37344的研究","authors":"Scott Mills","doi":"10.1016/S0742-8413(00)00086-4","DOIUrl":null,"url":null,"abstract":"<div><p>The β<sub>3</sub>-selective adrenergic receptor ligand BRL 37344 (BRL) was used to differentiate the presence and functional role of β-adrenergic receptor (βAR) subtypes in pig tissues. BRL did not stimulate adenylyl cyclase in membrane preparations or increase lipolysis from pig adipocytes. In contrast to some species, BRL appears to be a poor agonist for the pig βAR and is not a useful β<sub>3</sub>AR ligand. Based on displacement of [<sup>3</sup>H]dihydroalprenolol binding, BRL exhibited a 100-fold selectivity for pig βAR subtypes in adipose and skeletal muscle membranes. The high affinity site was proposed to be the β<sub>2</sub>AR. When used as an antagonist, BRL blockade of the high affinity site did not interfere with isoproterenol-stimulated lipolysis but did inhibit adenylyl cyclase activation. Results indicate that the high affinity βAR (β<sub>2</sub>AR) is not linked to lipolysis, possibly due to intracellular compartmentalization. Therefore, βAR subtypes may have function-specific effects.</p></div>","PeriodicalId":10586,"journal":{"name":"Comparative Biochemistry and Physiology Part C: Pharmacology, Toxicology and Endocrinology","volume":null,"pages":null},"PeriodicalIF":0.0000,"publicationDate":"2000-05-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0742-8413(00)00086-4","citationCount":"12","resultStr":"{\"title\":\"Beta-adrenergic receptor subtypes mediating lipolysis in porcine adipocytes. Studies with BRL-37344, a putative β3-adrenergic agonist\",\"authors\":\"Scott Mills\",\"doi\":\"10.1016/S0742-8413(00)00086-4\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<div><p>The β<sub>3</sub>-selective adrenergic receptor ligand BRL 37344 (BRL) was used to differentiate the presence and functional role of β-adrenergic receptor (βAR) subtypes in pig tissues. BRL did not stimulate adenylyl cyclase in membrane preparations or increase lipolysis from pig adipocytes. In contrast to some species, BRL appears to be a poor agonist for the pig βAR and is not a useful β<sub>3</sub>AR ligand. Based on displacement of [<sup>3</sup>H]dihydroalprenolol binding, BRL exhibited a 100-fold selectivity for pig βAR subtypes in adipose and skeletal muscle membranes. The high affinity site was proposed to be the β<sub>2</sub>AR. When used as an antagonist, BRL blockade of the high affinity site did not interfere with isoproterenol-stimulated lipolysis but did inhibit adenylyl cyclase activation. Results indicate that the high affinity βAR (β<sub>2</sub>AR) is not linked to lipolysis, possibly due to intracellular compartmentalization. Therefore, βAR subtypes may have function-specific effects.</p></div>\",\"PeriodicalId\":10586,\"journal\":{\"name\":\"Comparative Biochemistry and Physiology Part C: Pharmacology, Toxicology and Endocrinology\",\"volume\":null,\"pages\":null},\"PeriodicalIF\":0.0000,\"publicationDate\":\"2000-05-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://sci-hub-pdf.com/10.1016/S0742-8413(00)00086-4\",\"citationCount\":\"12\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Comparative Biochemistry and Physiology Part C: Pharmacology, Toxicology and Endocrinology\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://www.sciencedirect.com/science/article/pii/S0742841300000864\",\"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 Part C: Pharmacology, Toxicology and Endocrinology","FirstCategoryId":"1085","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/S0742841300000864","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
Beta-adrenergic receptor subtypes mediating lipolysis in porcine adipocytes. Studies with BRL-37344, a putative β3-adrenergic agonist
The β3-selective adrenergic receptor ligand BRL 37344 (BRL) was used to differentiate the presence and functional role of β-adrenergic receptor (βAR) subtypes in pig tissues. BRL did not stimulate adenylyl cyclase in membrane preparations or increase lipolysis from pig adipocytes. In contrast to some species, BRL appears to be a poor agonist for the pig βAR and is not a useful β3AR ligand. Based on displacement of [3H]dihydroalprenolol binding, BRL exhibited a 100-fold selectivity for pig βAR subtypes in adipose and skeletal muscle membranes. The high affinity site was proposed to be the β2AR. When used as an antagonist, BRL blockade of the high affinity site did not interfere with isoproterenol-stimulated lipolysis but did inhibit adenylyl cyclase activation. Results indicate that the high affinity βAR (β2AR) is not linked to lipolysis, possibly due to intracellular compartmentalization. Therefore, βAR subtypes may have function-specific effects.
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