{"title":"arg389 - β -肾上腺素受体- gsalpha融合蛋白的特性:与gly389 - β -肾上腺素受体- gsalpha融合蛋白的比较","authors":"Katharina Wenzel-Seifert, Roland Seifert","doi":"10.3109/713745179","DOIUrl":null,"url":null,"abstract":"<p><p>The human beta1-adrenoceptor (beta1AR) exists in several isoforms and activates adenylyl cyclase (AC) via Gs-proteins. The Arg389-isoform of the beta1AR (beta1AR-R389) expressed in CHW cells is much more efficient than the Gly389 isoform of the beta1AR (beta1AR-G389) at stabilizing the ternary complex and activating AC (Mason et al. 1999). The beta1AR-G389 fused to the Gsalpha splice variants GsalphaL or GsalphaS is efficient at stabilizing the ternary complex and activating AC (Wenzel-Seifert et al. 2002). Here, we show that beta1AR-R389-Gsalpha fusion proteins and beta1AR-G389-Gsalpha fusion proteins are similarly efficient at stabilizing the ternary complex and activating AC. In terms of agonist efficacies and agonist potencies in the [35S]guanosine 5'-O-(3-thiotriphosphate) binding assay, beta1AR-R389-Gsalpha fusion proteins and beta1AR-G389-Gsalpha fusion proteins are similar, too. Our present data fit to an increasing number of clinical studies that failed to detect physiology- or pathology-related functional differences between beta1AR-R389 and beta1AR-G389.</p>","PeriodicalId":20928,"journal":{"name":"Receptors & channels","volume":"9 5","pages":"315-23"},"PeriodicalIF":0.0000,"publicationDate":"2003-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.3109/713745179","citationCount":"10","resultStr":"{\"title\":\"Properties of Arg389-beta1-adrenoceptor-Gsalpha fusion proteins: comparison with Gly389-beta1-adrenoceptor-Gsalpha fusion proteins.\",\"authors\":\"Katharina Wenzel-Seifert, Roland Seifert\",\"doi\":\"10.3109/713745179\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>The human beta1-adrenoceptor (beta1AR) exists in several isoforms and activates adenylyl cyclase (AC) via Gs-proteins. The Arg389-isoform of the beta1AR (beta1AR-R389) expressed in CHW cells is much more efficient than the Gly389 isoform of the beta1AR (beta1AR-G389) at stabilizing the ternary complex and activating AC (Mason et al. 1999). The beta1AR-G389 fused to the Gsalpha splice variants GsalphaL or GsalphaS is efficient at stabilizing the ternary complex and activating AC (Wenzel-Seifert et al. 2002). Here, we show that beta1AR-R389-Gsalpha fusion proteins and beta1AR-G389-Gsalpha fusion proteins are similarly efficient at stabilizing the ternary complex and activating AC. In terms of agonist efficacies and agonist potencies in the [35S]guanosine 5'-O-(3-thiotriphosphate) binding assay, beta1AR-R389-Gsalpha fusion proteins and beta1AR-G389-Gsalpha fusion proteins are similar, too. Our present data fit to an increasing number of clinical studies that failed to detect physiology- or pathology-related functional differences between beta1AR-R389 and beta1AR-G389.</p>\",\"PeriodicalId\":20928,\"journal\":{\"name\":\"Receptors & channels\",\"volume\":\"9 5\",\"pages\":\"315-23\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"2003-01-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://sci-hub-pdf.com/10.3109/713745179\",\"citationCount\":\"10\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Receptors & channels\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://doi.org/10.3109/713745179\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Receptors & channels","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.3109/713745179","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 10
摘要
人β -肾上腺素受体(β - 1ar)存在于多种异构体中，通过gs蛋白激活腺苷酸环化酶(AC)。在CHW细胞中表达的beta1AR的arg389 -异构体(beta1AR- r389)比beta1AR的Gly389异构体(beta1AR- g389)在稳定三元复合物和激活AC方面更有效(Mason et al. 1999)。与Gsalpha剪接变体GsalphaL或gsalphhas融合的beta1AR-G389在稳定三元配合物和激活AC方面是有效的(Wenzel-Seifert et al. 2002)。在本研究中，我们发现beta1AR-R389-Gsalpha融合蛋白和beta1AR-G389-Gsalpha融合蛋白在稳定三元复合物和激活AC方面具有相似的效率。在[35S]鸟苷5'- o -(3-硫代三磷酸)结合实验中，beta1AR-R389-Gsalpha融合蛋白和beta1AR-G389-Gsalpha融合蛋白的激动剂效果和激动剂效力方面也相似。我们目前的数据与越来越多未能检测到beta1AR-R389和beta1AR-G389之间生理或病理相关功能差异的临床研究相吻合。
Properties of Arg389-beta1-adrenoceptor-Gsalpha fusion proteins: comparison with Gly389-beta1-adrenoceptor-Gsalpha fusion proteins.
The human beta1-adrenoceptor (beta1AR) exists in several isoforms and activates adenylyl cyclase (AC) via Gs-proteins. The Arg389-isoform of the beta1AR (beta1AR-R389) expressed in CHW cells is much more efficient than the Gly389 isoform of the beta1AR (beta1AR-G389) at stabilizing the ternary complex and activating AC (Mason et al. 1999). The beta1AR-G389 fused to the Gsalpha splice variants GsalphaL or GsalphaS is efficient at stabilizing the ternary complex and activating AC (Wenzel-Seifert et al. 2002). Here, we show that beta1AR-R389-Gsalpha fusion proteins and beta1AR-G389-Gsalpha fusion proteins are similarly efficient at stabilizing the ternary complex and activating AC. In terms of agonist efficacies and agonist potencies in the [35S]guanosine 5'-O-(3-thiotriphosphate) binding assay, beta1AR-R389-Gsalpha fusion proteins and beta1AR-G389-Gsalpha fusion proteins are similar, too. Our present data fit to an increasing number of clinical studies that failed to detect physiology- or pathology-related functional differences between beta1AR-R389 and beta1AR-G389.
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