The Effect of Calmodulin on the Phosphoprotein Intermediate of Mg2+-dependent Ca2+-stimulated Adenosine Triphosphatase in Human Erythrocyte Membranes

Overview

Journal Biochem J

Specialty Biochemistry

Date 1981 Feb 15

PMID 6458281

Citations 1

Authors

D A Jeffery

B D Roufogalis

S Katz

Affiliations

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Abstract

The effect of calmodulin on the formation and decomposition of the Ca2+-dependent phosphoprotein intermediate of the (Mg2+ + Ca2+)-dependent ATPase in erythrocyte membranes was investigated. In the presence of 60 microM-Ca2+ and 25 microM-MgCl2, calmodulin (0.5-1.5 microgram) did not alter the steady-state concentration of the phosphoprotein, but increased its rate of decomposition. Higher calmodulin concentrations significantly decreased the steady-state concentration of phosphoprotein. Calmodulin (0.5-1.7 microgram) increased Ca2+-transport ATPase activity by increasing the turnover rate of its phosphoprotein intermediate. Increasing the MgCl2 concentration from 25 microM to 250 microM increased the (Mg2+ + Ca2+)-dependent ATPase activity, but decreased the concentration of the phosphoprotein intermediate. Similarly to calmodulin, MgCl2 increased the turnover rate of the Ca2+-transport ATPase complex (about 3-fold). At the higher MgCl2 concentration calmodulin did not further affect the decomposition of the phosphoprotein intermediate. It was concluded that both calmodulin and MgCl2 increase the turnover of the Ca2+-pump by enhancing the decomposition of the Ca2+-dependent phosphoprotein intermediate.

Citing Articles

Effects of Ca2+, Mg2+ and calmodulin on the formation and decomposition of the phosphorylated intermediate of the erythrocyte Ca2+-stimulated ATPase.

Allen B, Katz S, Roufogalis B Biochem J. 1987; 244(3):617-23.

PMID: 2965571 PMC: 1148041. DOI: 10.1042/bj2440617.

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