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The membrane attack complex of complement and its precursor proteins lack phospholipase activity.

C W Vogel, A Plückthun, E R Podack

    Molecular Immunology
    |April 1, 1983
    PubMed
    Summary

    The membrane attack complex (MAC) of human complement does not possess phospholipase activity. This finding indicates that complement-mediated membrane damage is purely physical, not enhanced by phospholipid breakdown.

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    Area of Science:

    • Immunology
    • Cell Biology
    • Biochemistry

    Background:

    • The membrane attack complex (MAC) is a key component of the human complement system, responsible for cell lysis.
    • Previous hypotheses suggested potential enzymatic activity of MAC components on cell membranes.

    Purpose of the Study:

    • To investigate the presence and extent of phospholipase activity in the human MAC and its precursor proteins.
    • To determine the mechanism of complement-mediated membrane damage.

    Main Methods:

    • Analysis of purified MAC and precursor proteins.
    • Utilized three sensitive biochemical assays to detect phospholipase A1, A2, C, and D activities.

    Main Results:

    • No detectable phospholipase A1, A2, C, or D activity was observed in the MAC or its precursor proteins.

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  • The sensitivity of the assays confirmed the absence of enzymatic activity.

    • Conclusions:

    • Complement-mediated membrane damage is primarily caused by the physical insertion and action of the MAC, not by enzymatic breakdown of phospholipids.
    • The putative serine esterase sites in C6 and C7 do not appear to target phospholipids.