Activation of hepatic microsomal Ca2+-adenosine triphosphatase by Calcium-binding protein regucalcin.

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Abstract
The effect of regucalcin, a calcium-binding protein isolated from rat liver cytosol, on Ca2+-adenosine triphosphatase (ATPase) activity in hepatic microsomes was investigated. Mg2+-ATPase activity was clearly increased by the presence of 50 .mu.M Ca2+. Regucalcin (1.0-4.0 .mu.M) caused a remarkable elevation (about 3-fold) of Ca2+-ATPase activity. Also Mg2+-ATPase activity was increased (about 1.6-fold) by the presence of regucalcin (2.0 and 4.0 .mu.M). Guanosine-5''-O-(3-thiotriphosphate) (GTPrs; 10-5 and 10-4M) and nicotinamide adenine dinucleotide phosphate oxidized form (NADP+; 10-5 to 10-3 M) or reduced form (NADPH; 10-4 and 10-3 M) significantly increased Ca2+-ATPase activity. These increases were not enhanced by the presence of regucalcin (2.0 .mu.M). Of various metal ions, a comparatively low concentration of V5+ (10-5 M) or Cd2+ (10-6 M) significantly increased Ca2+-ATPase activity, while Hg2+, Zn2+, Cu2+ and Mn2+ did not have such an effect. Regucalcin (2.0 .mu.M) did not enhance the effect of V5+ and Cd2+ on Ca2+-ATPase activity. The present finding, that regucalcin activates hepatic microsomal Ca2+-ATPase, suggests a cell physiological role of regucalcin as an activator in the microsomal Ca2+-pump activity. This action of regucalcin may not be influenced by other regulators.