| http://purl.uniprot.org/citations/22105697 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/22105697 | http://www.w3.org/2000/01/rdf-schema#comment | "Adenosine A(1) receptor (A(1)R)-induced translocation of PKCε to transverse (t) tubular membranes in isolated rat cardiomyocytes is associated with a reduction in β(1)-adrenergic-stimulated contractile function. The PKCε-mediated activation of protein kinase D (PKD) by endothelin-1 is inhibited by β(1)-adrenergic stimulated protein kinase A (PKA) suggesting a similar mechanism of A(1)R signal transduction modulation by adrenergic agonists may exist in the heart. We have investigated the influence of β(1)-adrenergic stimulation on PKCε translocation elicited by A(1)R. Immunofluorescence imaging and Western blotting with PKCε and β-COP antibodies were used to quantify the co-localization of PKCε and t-tubular structures in isolated rat cardiomyocytes. The A(1)R agonist CCPA increased the co-localization of PKCε and t-tubules as detected by imaging. The β(1)-adrenergic receptor agonist isoproterenol (ISO) inhibited this effect of CCPA. Forskolin, a potent activator of PKA, mimicked, and H89, a pharmacological PKA inhibitor, and PKI, a membrane-permeable PKA peptide PKA inhibitor, attenuated the negative effect of ISO on the A(1)R-mediated PKCε translocation. Western blotting with isolated intact hearts revealed an increase in PKCε/β-COP co-localization induced by A(1)R. This increase was attenuated by the A(1)R antagonist DPCPX and ISO. The ISO-induced attenuation was reversed by H89. It is concluded that adrenergic stimulation inhibits A(1)R-induced PKCε translocation to the PKCε anchor site RACK2 constituent of a coatomer containing β-COP and associated with the t-tubular structures of the heart. In that this translocation has been previously associated with the antiadrenergic property of A(1)R, it is apparent that the interactive effects of adenosine and β(1)-adrenergic agonists on function are complex in the heart."xsd:string |
| http://purl.uniprot.org/citations/22105697 | http://purl.org/dc/terms/identifier | "doi:10.1002/jcp.24008"xsd:string |
| http://purl.uniprot.org/citations/22105697 | http://purl.uniprot.org/core/author | "Komatsu S."xsd:string |
| http://purl.uniprot.org/citations/22105697 | http://purl.uniprot.org/core/author | "Fenton R.A."xsd:string |
| http://purl.uniprot.org/citations/22105697 | http://purl.uniprot.org/core/author | "Ikebe M."xsd:string |
| http://purl.uniprot.org/citations/22105697 | http://purl.uniprot.org/core/author | "Dobson J.G. Jr."xsd:string |
| http://purl.uniprot.org/citations/22105697 | http://purl.uniprot.org/core/author | "Shea L.G."xsd:string |
| http://purl.uniprot.org/citations/22105697 | http://purl.uniprot.org/core/date | "2012"xsd:gYear |
| http://purl.uniprot.org/citations/22105697 | http://purl.uniprot.org/core/name | "J Cell Physiol"xsd:string |
| http://purl.uniprot.org/citations/22105697 | http://purl.uniprot.org/core/pages | "3201-3207"xsd:string |
| http://purl.uniprot.org/citations/22105697 | http://purl.uniprot.org/core/title | "Crosstalk between adenosine A1 and beta1-adrenergic receptors regulates translocation of PKCepsilon in isolated rat cardiomyocytes."xsd:string |
| http://purl.uniprot.org/citations/22105697 | http://purl.uniprot.org/core/volume | "227"xsd:string |
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