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Effects of granulocyte neutral proteases on complement components.

U Johnson, K Ohlsson, I Olsson

    Scandinavian Journal of Immunology
    |January 1, 1976
    PubMed
    Summary
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    Human granulocyte collagenase and elastase enzymes can cleave complement components C3 and C5. Elastase generates a C5b-like fragment, while collagenase only affects C3, impacting immune responses.

    Area of Science:

    • Biochemistry
    • Immunology
    • Protease research

    Background:

    • Human granulocytes release collagenase and elastase.
    • Complement components C3 and C5 are crucial in immune responses.
    • Protease inhibitors like alpha1-antitrypsin and alpha2-macroglobulin regulate enzyme activity.

    Purpose of the Study:

    • To investigate the proteolytic effects of human granulocyte collagenase and elastase on complement components C3 and C5.
    • To determine the impact of these enzymes on C3 and C5 conversion in serum and purified systems.
    • To understand the conditions under which proteolysis occurs in the presence of protease inhibitors.

    Main Methods:

    • Analysis of C3 conversion using crossed immunoelectrophoresis (Ganrot's method).
    • Detection of C5 conversion using immunoelectrophoresis (Scheidegger's method).

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  • Investigation of enzyme activity in both purified complement components and human serum.

    • Main Results:

    • Collagenase converted C3 to C3b but did not affect C5.
    • Elastase converted C3 to C3b and generated a C5b-like fragment from C5.
    • Proteolysis was only detected when the enzyme to inhibitor molar ratio exceeded 1 in serum.

    Conclusions:

    • Human granulocyte collagenase and elastase exhibit distinct cleavage specificities for complement components C3 and C5.
    • Elastase's ability to cleave C5 suggests a potential role in complement-mediated inflammation.
    • Protease inhibitors significantly modulate the activity of these granulocyte enzymes against complement components in serum.