| http://purl.uniprot.org/citations/6096366 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/6096366 | http://www.w3.org/2000/01/rdf-schema#comment | "The cAMP-dependent protein kinase-induced effects on phosphorylase and glycogen synthase activities and glucose production were studied in hepatocytes isolated from fed rats in the presence of the diastereomers of adenosine cyclic 3',5'-phosphorothioate, (Sp)-cAMPS and (Rp)-cAMPS. Incubation of hepatocytes with (Sp)-cAMPS or glucagon, both of which lead to cAMP-dependent protein kinase activation, resulted in a concentration-dependent increase in glycogen phosphorylase activity and a decrease in glycogen synthase activity. Incubation of hepatocytes with the cAMP-dependent protein kinase antagonist, (Rp)-cAMPS, in the absence of an agonist, had no significant effect on phosphorylase or glycogen synthase activities. Incubation of hepatocytes with a half-maximally inhibitory concentration of (Rp)-cAMPS shifted the agonist-induced activation curves for phosphorylase and the agonist-induced inhibition curves for glycogen synthase to 5-fold higher concentrations for both (Sp)-cAMPS and glucagon. Phosphorylase activity was very sensitive to the rapid, concentration-dependent inhibition by (Rp)-cAMPS of agonist-induced activation of cAMP-dependent protein kinase. The effects on phosphorylase activity were observable in 30 s and were concentration-dependent with half-maximal inhibition at 10 microM, similar to that observed for cAMP-dependent protein kinase. In contrast, glycogen synthase activity was less sensitive to (Rp)-cAMPS inhibition of agonist-induced activation of cAMP-dependent protein kinase. The effects on glycogen synthase activity lagged behind those on phosphorylase activity and the concentration dependence did not parallel the cAMP-dependent protein kinase effect, but was shifted to higher concentrations of (Rp)-cAMPS with half-maximal inhibition at 60 microM. Glucose (10 to 40 mM) increased the sensitivity of glycogen synthase to (Rp)-cAMPS inhibition of cAMP-dependent protein kinase over a narrow range of agonist concentration, but had no significant effect throughout most of the agonist-induced activation range. Thus, the diastereomers, (Sp)- and (Rp)-cAMPS, influence glycogen metabolism and the glycogenolytic enzymes through their modulation of cAMP-dependent protein kinase levels."xsd:string |
| http://purl.uniprot.org/citations/6096366 | http://purl.org/dc/terms/identifier | "doi:10.1016/s0021-9258(17)42548-8"xsd:string |
| http://purl.uniprot.org/citations/6096366 | http://purl.uniprot.org/core/author | "Marks J.S."xsd:string |
| http://purl.uniprot.org/citations/6096366 | http://purl.uniprot.org/core/author | "Botelho L.H."xsd:string |
| http://purl.uniprot.org/citations/6096366 | http://purl.uniprot.org/core/author | "Perillo N.L."xsd:string |
| http://purl.uniprot.org/citations/6096366 | http://purl.uniprot.org/core/author | "Rothermel J.D."xsd:string |
| http://purl.uniprot.org/citations/6096366 | http://purl.uniprot.org/core/date | "1984"xsd:gYear |
| http://purl.uniprot.org/citations/6096366 | http://purl.uniprot.org/core/name | "J Biol Chem"xsd:string |
| http://purl.uniprot.org/citations/6096366 | http://purl.uniprot.org/core/pages | "15294-15300"xsd:string |
| http://purl.uniprot.org/citations/6096366 | http://purl.uniprot.org/core/title | "Effects of the specific cAMP antagonist, (Rp)-adenosine cyclic 3',5'-phosphorothioate, on the cAMP-dependent protein kinase-induced activity of hepatic glycogen phosphorylase and glycogen synthase."xsd:string |
| http://purl.uniprot.org/citations/6096366 | http://purl.uniprot.org/core/volume | "259"xsd:string |
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