The cAMP binding protein Epac regulates cardiac myofilament function The effects of Epac activation on myofilament Ca 2 sensitivity and on cTnI and cMyBP-C phosphorylation were independent of PKA and were blocked by protein kinase C (PKC) and Ca 2 calmodulin kinase II (CaMKII) inhibitors. Altogether these findings identify Epac as a new regulator of myofilament function. calmodulin kinase II contraction exchange protein activated by cyclic AMP sarcomeric proteins protein kinase C - Université de Montpellier Accéder directement au contenu
Article Dans Une Revue Proceedings of the National Academy of Sciences of the United States of America Année : 2009

The cAMP binding protein Epac regulates cardiac myofilament function The effects of Epac activation on myofilament Ca 2 sensitivity and on cTnI and cMyBP-C phosphorylation were independent of PKA and were blocked by protein kinase C (PKC) and Ca 2 calmodulin kinase II (CaMKII) inhibitors. Altogether these findings identify Epac as a new regulator of myofilament function. calmodulin kinase II contraction exchange protein activated by cyclic AMP sarcomeric proteins protein kinase C

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hal-01824357 , version 1 (27-06-2018)

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Olivier Cazorla, Alexandre Lucas, Florence Poirier, Alain Lacampagne, F. Lezoualc'H, et al.. The cAMP binding protein Epac regulates cardiac myofilament function The effects of Epac activation on myofilament Ca 2 sensitivity and on cTnI and cMyBP-C phosphorylation were independent of PKA and were blocked by protein kinase C (PKC) and Ca 2 calmodulin kinase II (CaMKII) inhibitors. Altogether these findings identify Epac as a new regulator of myofilament function. calmodulin kinase II contraction exchange protein activated by cyclic AMP sarcomeric proteins protein kinase C. Proceedings of the National Academy of Sciences of the United States of America, 2009, 106 (33), pp.14144 - 14149. ⟨10.1073/pnas.0812536106⟩. ⟨hal-01824357⟩
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