| http://purl.uniprot.org/citations/16840718 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/16840718 | http://www.w3.org/2000/01/rdf-schema#comment | "Previous studies in transgenic mice and with isolated ryanodine receptors (RyR) have indicated that Ca2+-calmodulin-dependent protein kinase II (CaMKII) can phosphorylate RyR and activate local diastolic sarcoplasmic reticulum (SR) Ca2+ release events (Ca2+ sparks) and RyR channel opening. Here we use relatively controlled physiological conditions in saponin-permeabilized wild type (WT) and phospholamban knockout (PLB-KO) mouse ventricular myocytes to test whether exogenous preactivated CaMKII or endogenous CaMKII can enhance resting Ca2+ sparks. PLB-KO mice were used to preclude ancillary effects of CaMKII mediated by phospholamban phosphorylation. In both WT and PLB-KO myocytes, Ca2+ spark frequency was increased by both preactivated exogenous CaMKII and endogenous CaMKII. This effect was abolished by CaMKII inhibitor peptides. In contrast, protein kinase A catalytic subunit also enhanced Ca2+ spark frequency in WT, but had no effect in PLB-KO. Both endogenous and exogenous CaMKII increased SR Ca2+ content in WT (presumably via PLB phosphorylation), but not in PLB-KO. Exogenous calmodulin decreased Ca2+ spark frequency in both WT and PLB-KO (K0.5 approximately 100 nmol/L). Endogenous CaMKII (at 500 nmol/L [Ca2+]) phosphorylated RyR as completely in <4 minutes as the maximum achieved by preactivated exogenous CaMKII. After CaMKII activation Ca2+ sparks were longer in duration, and more frequent propagating SR Ca2+ release events were observed. We conclude that CaMKII-dependent phosphorylation of RyR by endogenous associated CaMKII (but not PKA-dependent phosphorylation) increases resting SR Ca2+ release or leak. Moreover, this may explain the enhanced SR diastolic Ca2+ leak and certain triggered arrhythmias seen in heart failure."xsd:string |
| http://purl.uniprot.org/citations/16840718 | http://purl.org/dc/terms/identifier | "doi:10.1161/01.res.0000236756.06252.13"xsd:string |
| http://purl.uniprot.org/citations/16840718 | http://purl.uniprot.org/core/author | "Zhang T."xsd:string |
| http://purl.uniprot.org/citations/16840718 | http://purl.uniprot.org/core/author | "Guo T."xsd:string |
| http://purl.uniprot.org/citations/16840718 | http://purl.uniprot.org/core/author | "Bers D.M."xsd:string |
| http://purl.uniprot.org/citations/16840718 | http://purl.uniprot.org/core/author | "Mestril R."xsd:string |
| http://purl.uniprot.org/citations/16840718 | http://purl.uniprot.org/core/date | "2006"xsd:gYear |
| http://purl.uniprot.org/citations/16840718 | http://purl.uniprot.org/core/name | "Circ Res"xsd:string |
| http://purl.uniprot.org/citations/16840718 | http://purl.uniprot.org/core/pages | "398-406"xsd:string |
| http://purl.uniprot.org/citations/16840718 | http://purl.uniprot.org/core/title | "Ca2+/Calmodulin-dependent protein kinase II phosphorylation of ryanodine receptor does affect calcium sparks in mouse ventricular myocytes."xsd:string |
| http://purl.uniprot.org/citations/16840718 | http://purl.uniprot.org/core/volume | "99"xsd:string |
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