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  • Title: Properties of Arg389-beta1-adrenoceptor-Gsalpha fusion proteins: comparison with Gly389-beta1-adrenoceptor-Gsalpha fusion proteins.
    Author: Wenzel-Seifert K, Seifert R.
    Journal: Recept Channels; 2003; 9(5):315-23. PubMed ID: 14527875.
    Abstract:
    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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