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. 1991;45(3):109-15.
doi: 10.1159/000468875.

Inhibition of sarcoplasmic reticulum Ca(2+)-ATPase activity by cadmium, lead and mercury

S Hechtenberg  1 , D Beyersmann
Affiliations

Inhibition of sarcoplasmic reticulum Ca(2+)-ATPase activity by cadmium, lead and mercury

S Hechtenberg et al. Enzyme. 1991.

Abstract

The effect of Cd2+, Pb2+ and Hg2+ on the Ca(2+)-ATPase activity of sarcoplasmic reticulum from rabbit muscle was studied. The concentration of relevant free and complex species for the assay conditions have been computed. As a result, ATP hydrolysis was found to be inhibited with an IC50 value of 950 nmol/l free Cd2+ or 95 nmol/l free Pb2+. Although calculation of the free Hg2+ was not possible, the comparison of the IC50 values for total metal ions show that Hg2+ is the strongest inhibitor of enzyme activity. The inhibition by Cd2+ seems to be independent of substrate concentration, whereas the inhibitory effect of Pb2+ is lowered in the presence of higher MgATP concentrations. Our data illustrate that the three heavy metals are potent inhibitors of the Ca2+ pump. Therefore low concentrations of these metal ions may disturb intracellular Ca2+ homeostasis and act on Ca(2+)-mediated cell functions.

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