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1 Laboratory of Muscle Research and Molecular Cardiology, Klinik III für Innere Medizin; 2 Department of Cardiac and Thoracic Surgery; and 3 Department of Anatomy, Universität zu Köln, 50924 Cologne, Germany
The present investigation addresses whether protein
expression and function of sarco(endo)plasmic reticulum
Ca2+-ATPase (SERCA2a) and phospholamban (PLB) correlate in
failing and nonfailing human myocardium. SERCA2a activity and protein expression, PLB phosphorylation, and the force-frequency relationship (FFR) have been determined in right atrium (RA) and left ventricle (LV)
from nonfailing (NF, n = 12) and terminally failing
[dilated cardiomyopathy (DCM), n = 12] human
hearts. Only in LV of DCM hearts was SERCA2a activity significantly
decreased [maximal turnover rate (Vmax) = 196 ± 11 and 396 ± 30 nmol · mg
1 · min1
in LV and RA, respectively], whereas protein expression of
SERCA2a in the different chambers was unchanged in NF (3.9 ± 0.3 and
3.2 ± 0.4 densitometric units in LV and RA, respectively) and DCM hearts (4.8 ± 0.8 and 3.4 ± 0.1 densitometric units in LV and RA,
respectively). Phosphorylation of PLB was higher in LV than in RA in NF
(Ser16: 180.5 ± 19.0 vs. 56.8 ± 6.0 densitometric
units; Thr17: 174.6 ± 11.2 vs. 37.4 ± 8.9 densitometric
units) and DCM hearts (Ser16: 132.0 ± 5.4 vs. 22.4 ± 3.5 densitometric units; Thr17: 131.2 ± 10.9 vs. 9.2 ± 2.4 densitometric units). SERCA2a function, but not protein expression,
correlated well with the functional parameters of the FFR in DCM and NF
human hearts. Regulation of SERCA2a function depends on the
phosphorylation of PLB at Ser16 and Thr17.
However, direct SERCA2a regulation might also be affected by an unknown mechanism.
heart failure; phospholamban phosphorylation; sarco(endo) plasmic reticulum calcium-adenosine 5'-triphosphatase
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