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1 Institut für Pharmakologie und Toxikologie, Westfälische Wilhelms-Universität, D-48149 Münster, Germany; and 2 Department of Laboratories, Denver Health Medical Center, Denver, Colorado 80204
Compared with isolated electrically driven
neonatal ventricular preparations, the total time of contraction, the
time to peak tension, and the time of relaxation were decreased to
~50% in adult ventricular preparations. The expression of
sarco(endo)plasmic reticulum
Ca2+-ATPase (SERCA) was increased
to 133% at the protein level and to 154% at the mRNA level in adult
vs. neonatal ventricular preparations, whereas phospholamban was
unchanged at both the protein and mRNA levels. Moreover,
Ca2+ uptake was increased to 180%
in adult vs. neonatal ventricular preparations. Phospholamban
phosphorylation was enhanced in adult vs. neonatal ventricular
preparations. In adult ventricular preparations, phosphatase activity
was reduced to 53% of neonatal preparations, the protein levels of the
immunologically detectable catalytic subunits of protein phosphatase
types 1 and 2A were reduced to 28 and 61% of neonatal preparations,
respectively, and the mRNA levels of type 1
, 1
, 1
, 2A
, and
2A
phosphatase isoforms were decreased to 69, 68, 54, 67, and 63%,
respectively. We conclude that in the adult rat heart, the shortened
time parameters of contraction can be explained by an elevated
expression of SERCA. In addition, an increased phosphorylation state of
phospholamban due to reduced phosphatase activity may be involved.
phospholamban; sarco(endo)plasmic reticulum calcium-adenosinetriphosphatase; calsequestrin; contractility
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