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Calcium at the sarcolemma.

G A Langer

    Journal of Molecular and Cellular Cardiology
    |February 1, 1984
    PubMed
    Summary
    This summary is machine-generated.

    Calcium (Ca) in heart muscle cells is stored on the cell surface, specifically on anionic phospholipids of the sarcolemma. This readily available Ca influences heart contraction by regulating calcium entry and exit.

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    Area of Science:

    • Cardiovascular Physiology
    • Cellular Biology
    • Biochemistry

    Background:

    • Contractile control in mammalian ventricles is influenced by intracellular calcium.
    • The precise mechanisms and cellular localization of calcium involved in rapid contractile regulation require further elucidation.

    Purpose of the Study:

    • To investigate the cellular sites and dynamics of calcium involved in mammalian ventricular contractile control.
    • To determine the relationship between extracellular calcium and intracellular calcium binding sites.

    Main Methods:

    • Experiments involving calcium removal and replacement in arterial perfusate of mammalian ventricles.
    • Analysis of calcium exchange kinetics and binding site characteristics.

    Main Results:

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    • A significant component of calcium crucial for contractile control is bound to rapidly exchangeable cellular sites.
    • These sites are in rapid equilibrium with extracellular calcium and are replenished beat-to-beat.
    • Anionic phospholipids of the sarcolemma are identified as the likely binding sites for this calcium.
    • Sarcolemmal calcium stores regulate transsarcolemmal calcium movement via calcium channels and the Na-Ca exchanger.
    • Increased Na-Ca exchanger activity correlates with enhanced calcium binding to sarcolemmal sites.

    Conclusions:

    • Sarcolemmal-bound calcium plays a critical role in regulating intracellular calcium levels and cardiac contractility.
    • The sarcolemma acts as a dynamic calcium store influencing calcium influx and efflux.
    • The Na-Ca exchanger activity is linked to the modulation of sarcolemmal calcium binding.