This preclinical study demonstrates that the SR Ca2+-ATPase is directly involved in passive monovalent cation exchange.
Hypothesis-generating for SR Ca2+-ATPase in monovalent cation exchange; leaves open physiological relevance in intact cardiomyocytes.
A specific inhibitor of SERCA-pumps, thapsigargin (TG) was used to demonstrate the direct involvement of the SR Ca(2+)-ATPase in passive K+/Na+ exchange. The K(+)-potential variations across vesicle membranes were measured in the absence of ATP with a fluorescent probe: 3,3'-dipropylthiodicarbocyanine iodide. Addition of EGTA dissipates the K(+)-potential whereas the presence of TG abolishes this effect. Our data prove that the Ca(2+)-ATPase translocates monovalent cations at a rate similar to the E2-->E1 conformational change.
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Jesus et al. (1995) studied this question.
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