Frequency-dependent acceleration of relaxation in mammalian heart: a property not relying on phospholamban and SERCA2a phosphorylation

Author:

Valverde Carlos A.,Mundiña-Weilenmann Cecilia,Said Matilde,Ferrero Paola,Vittone Leticia,Salas Margarita,Palomeque Julieta,Petroff Martín Vila,Mattiazzi Alicia

Publisher

Wiley

Subject

Physiology

Reference40 articles.

1. Physical interactions between phospholamban and sarco(endo)plasmic reticulum Ca2+-ATPases are dissociated by elevated Ca2+, but not by phospholamban phosphorylation, vanadate, or thapsigargin, and are enhanced by ATP;Asahi;J Biol Chem,2000

2. CaMKII is responsible for activity-dependent acceleration of relaxation in rat ventricular myocytes;Bassani;Am J Physiol,1995

3. Phospholamban: a major determinant of the cardiac force-frequency relationship;Bluhm;Am J Physiol,2000

4. Robust adenoviral and adeno-associated viral gene transfer to the in vivo murine heart: application to study of phospholamban physiology;Champion;Circulation,2003

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