Phosphorylation of phospholamban and troponin I in beta-adrenergic-induced acceleration of cardiac relaxation.

@article{Li2000PhosphorylationOP,
  title={Phosphorylation of phospholamban and troponin I in beta-adrenergic-induced acceleration of cardiac relaxation.},
  author={Lin Li and Jaime Desantiago and Gavin Chu and Evangelia G Kranias and Donald M. Bers},
  journal={American journal of physiology. Heart and circulatory physiology},
  year={2000},
  volume={278 3},
  pages={H769-79}
}
Activation of cAMP-dependent protein kinase A (PKA) in ventricular myocytes by isoproterenol (Iso) causes phosphorylation of both phospholamban (PLB) and troponin I (TnI) and accelerates relaxation by up to twofold. Because PLB phosphorylation increases sarcoplasmic reticulum (SR) Ca pumping and TnI phosphorylation increases the rate of Ca dissociation from the myofilaments, both factors could contribute to the acceleration of relaxation seen with PKA activation. To compare quantitatively the… CONTINUE READING

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Characteristics of L-type Ca21 channel and b-adrenergic stimulation in wild-type and phospholamban-deficient mouse cardiac myocytes (Abstract)

  • H. Masaki, Y. Sato, W. Luo, E. G. Kranias, A. Yatani
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