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Regulation of SERCA2 activity by PDE3A in human myocardium: Phosphorylation-dependent interaction of PDE3A1 with SERCA2.

J Biol Chem.. 2015-01; 
Ahmad F, Shen W, Vandeput F, Szabo-Fresnais N, Krall J, Degerman E, Goetz F, Klussmann E, Movsesian M, Manganiello V. NIH, United States
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摘要

PDE3 regulates cAMP-mediated signaling in the heart, and PDE3 inhibitors augment contractility in patients with heart failure. Studies in mice showed that PDE3A, not PDE3B, is the subfamily responsible for these inotropic effects, and that murine PDE3A1 associates with SERCA2, PLB and AKAP18 in a multi-protein signalosome in human SR. Immunohistochemical staining demonstrated that PDE3A co-localizes in Z-bands of human cardiac myocytes with desmin, SERCA2, PLB and AKAP18. In human SR fractions, cAMP increased PLB phosphorylation and SERCA2 activity; this was potentiated by PDE3 inhibition but not by PDE4 inhibition. During gel-filtration chromatography of solubilized SR membranes, PDE3 activity was recovered in... More

关键词

A-kinase anchoring protein (AKAP); Cyclic Nucleotide Phosphodiesterase; PDE3A; Phospholamban; SERCA2; cyclic AMP (cAMP); immunohistochemistry; protein kinase A (PKA); subcellular fractionation