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An endogenous protease activating plasma inactive renin.

B J Leckie

    Clinical Science and Molecular Medicine. Supplement
    |December 1, 1978
    PubMed
    Summary
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    Acid activation of inactive renin in human plasma is a serine protease process. Protease inhibitors like Trasylol blocked this activation, indicating a key role for serine proteases in renin regulation.

    Area of Science:

    • Biochemistry
    • Physiology
    • Enzymology

    Background:

    • Plasma inactive renin requires activation to become enzymatically active.
    • Understanding the mechanisms of renin activation is crucial for regulating blood pressure and fluid balance.

    Purpose of the Study:

    • To investigate the molecular mechanisms underlying the acid-activation of plasma inactive renin.
    • To identify the type of enzyme involved in this activation process.

    Main Methods:

    • Utilized protease inhibitors Trasylol and soyabean trypsin inhibitor to block enzyme activity.
    • Assessed the effect of N-Ethylmaleimide and o-phenathroline on acid-induced renin activation.
    • Studied inactive renin activation in human plasma under acidic conditions.

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    Main Results:

    • Trasylol and soyabean trypsin inhibitor effectively prevented acid-induced activation of plasma inactive renin.
    • N-Ethylmaleimide showed partial inhibition of acid-activation.
    • o-phenathroline did not affect the acid-activation process.

    Conclusions:

    • Acid-activation of inactive renin in human plasma is mediated by a serine protease.
    • Serine proteases play a significant role in the activation pathway of plasma inactive renin.