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Pressure effects on sarcoplasmic reticulum.

S Varga, N Mullner, S Pikula

    The Journal of Biological Chemistry
    |October 25, 1986
    PubMed
    Summary
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    High pressure irreversibly damages sarcoplasmic reticulum Ca2+-ATPase (calcium adenosine triphosphatase) enzyme activity and structure. Enzyme conformation and protective agents like glycerol influence pressure sensitivity.

    Area of Science:

    • Biochemistry
    • Biophysics
    • Membrane Protein Chemistry

    Background:

    • Sarcoplasmic reticulum Ca2+-ATPase (calcium adenosine triphosphatase) is crucial for muscle contraction.
    • Understanding pressure effects on enzymes is vital for various biological and industrial applications.

    Purpose of the Study:

    • To investigate the irreversible effects of hydrostatic pressure on Ca2+-ATPase activity and structure.
    • To determine how enzyme conformation and protective agents influence pressure sensitivity.

    Main Methods:

    • Exposure of sarcoplasmic reticulum vesicles to pressures ranging from 800 to 2000 atmospheres.
    • Assays for Ca2+ transport and Ca2+-stimulated ATPase activity.
    • Analysis of enzyme structure through tryptic digestion, SH group exposure, and conformational studies.

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    Main Results:

    • Pressures above 800 atm irreversibly inhibit Ca2+-ATPase activity and Ca2+ transport.
    • Pressure causes structural damage, including crystal disruption, increased proteolysis, and altered conformational responses.
    • Enzyme conformation (E1/E2 states) and protective agents (e.g., glycerol, sucrose, 1M KCl) significantly affect pressure resistance.

    Conclusions:

    • High pressure induces irreversible inactivation and structural damage to Ca2+-ATPase.
    • Enzyme conformation plays a critical role in pressure sensitivity.
    • Osmolytes and high salt concentrations can stabilize the enzyme against pressure-induced denaturation.