Key result
The purified heart sarcolemma Ca2+-pumping ATPase has high affinity for Ca2+ in the presence of calmodulin and can be reconstituted in liposomes to pump Ca2+ with a 1:1 stoichiometry to ATP.
Population
Purified Ca2+-pumping ATPase of heart sarcolemma
Comparison
Calmodulin, phosphatidylserine, or limited… vs Absence of calmodulin or treatment
Design
Preclinical
Authors
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Characterizes sarcolemmal Ca2+ ATPase in vitro; leaves open its regulation and role in intact cardiomyocytes.
The purified heart sarcolemma Ca2+-pumping ATPase is regulated by calmodulin, phosphatidylserine, and proteolysis, but is not the direct target of cAMP-dependent protein kinase phosphorylation.
Caroni et al. (1983) studied this question. The purified heart sarcolemma Ca2+-pumping ATPase has high affinity for Ca2+ in the presence of calmodulin and can be reconstituted in liposomes to pump Ca2+ with a 1:1 stoichiometry to ATP.
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