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• W2011309091 abstract "Inhibitor 1 (I-1) is a protein inhibitor of protein phosphatase 1 (PP1), the predominating Ser/Thr phosphatase in the heart. Non-phosphorylated I-1 is inactive, whereas I-1 phosphorylated by protein kinase A (PKA) at Thr35 is a potent PP1 inhibitor. The phosphatases that dephosphorylate I-1Thr35 and thus deactivate I-1 in the heart are not established. Here we overexpressed I-1 in neonatal rat cardiac myocytes with recombinant adenovirus and determined phosphorylation of I-1, and one of the major target proteins of PKA/PP1 in the heart, phospholamban (PLB), by Western blot with phospho-specific antibodies. Incubation with the calcineurin inhibitor cyclosporine A or okadaic acid, used at a concentration preferentially inhibiting phosphatase 2A (PP2A), increased significantly I-1Thr35 (∼2- to 6-fold) and PLB Ser16 phosphorylation (∼2-fold). The results indicate that calcineurin and PP2A act to maintain a low basal level of phosphorylated (active) I-1 in living cardiac myocytes. Calcineurin may constitute a cross-talk between calcium- and cAMP-dependent pathways." @default.
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• W2011309091 date "2006-08-01" @default.
• W2011309091 modified "2023-10-17" @default.
• W2011309091 title "Role of calcineurin and protein phosphatase-2A in the regulation of phosphatase inhibitor-1 in cardiac myocytes" @default.
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• W2011309091 doi "https://doi.org/10.1016/j.bbrc.2006.05.182" @default.
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