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Calmodulin and the plasma membrane calcium pump.

F F Vincenzi, T R Hinds, B U Raess

    Annals of the New York Academy of Sciences
    |January 1, 1980
    PubMed
    Summary
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    Calmodulin (CaM) regulates the plasma membrane calcium pump in red blood cells (RBCs). Data suggest CaM acts as a subunit of the calcium pump ATPase in vivo.

    Area of Science:

    • Biochemistry
    • Cell Biology
    • Membrane Transport

    Background:

    • The plasma membrane calcium pump (Ca2+ + Mg2+)-ATPase is crucial for maintaining calcium homeostasis.
    • Calmodulin (CaM) is a known calcium-binding protein that regulates various cellular processes.
    • Understanding CaM's role in calcium pump regulation is vital for cellular physiology.

    Purpose of the Study:

    • To investigate the role of Calmodulin (CaM) in the regulation of the red blood cell (RBC) plasma membrane calcium pump.
    • To determine if CaM functions as a subunit of the (Ca2+ + Mg2+)-ATPase in vivo.

    Main Methods:

    • Studied CaM binding to isolated RBC membranes under varying calcium concentrations.
    • Assessed the responsiveness of the (Ca2+ + Mg2+)-ATPase to CaM.

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  • Utilized kinetic analysis and computational modeling based on estimated intracellular calcium and CaM levels.

    • Main Results:

    • Ca2+ loading of RBCs enhances CaM binding to membranes, decreasing ATPase responsiveness to CaM.
    • CaM activation of the (Ca2+ + Mg2+)-ATPase in vitro is not instantaneous, suggesting slow binding kinetics.
    • CaM binding to membranes shows calcium dependence, similar to ATPase activation, and persists at high calcium levels.

    Conclusions:

    • Data support the interpretation that CaM participates in regulating the plasma membrane calcium pump.
    • Calculations suggest CaM occupies most pump sites in vivo, indicating it functions as a subunit of the Ca2+ pump ATPase.