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Related Experiment Videos

Complement receptor is an inhibitor of the complement cascade.

K Iida, V Nussenzweig

    The Journal of Experimental Medicine
    |May 1, 1981
    PubMed
    Summary
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    Complement receptor 1 (CR1) on human erythrocytes inhibits both classical and alternative complement pathways. This glycoprotein protects cells from damage by preventing excessive complement activation when binding C3b- and C4b-coated substrates.

    Area of Science:

    • Immunology
    • Complement System
    • Cell Biology

    Background:

    • Complement receptor 1 (CR1) is a glycoprotein found on human erythrocytes.
    • CR1 is known to bind C3b and C4b, mediating adherence of complement-opsonized particles.
    • The complement system comprises classical and alternative pathways crucial for innate immunity.

    Purpose of the Study:

    • To investigate the inhibitory functions of CR1 beyond its role in adherence.
    • To determine CR1's effect on complement convertases of both classical and alternative pathways.
    • To elucidate CR1's mechanism in protecting cells from complement-mediated damage.

    Main Methods:

    • Biochemical assays to measure CR1's enzymatic inhibitory activity.
    • Radioligand binding studies using 125I-CR1 to assess C4b interaction.

    Related Experiment Videos

  • Functional assays to evaluate CR1's cofactor activity in C4b cleavage.

    • Main Results:

    • CR1 promotes dissociation of the alternative pathway C3 convertase (C3b,Bb) and C3b cleavage.
    • CR1 inactivates classical pathway C3 (EAC142) and C5 convertases, inhibiting C3 consumption and enhancing C4b,2a decay.
    • CR1 is a more potent inhibitor of C4b,2a than C4 binding protein and competes with C2 for binding to C4b.

    Conclusions:

    • CR1 acts as a potent inhibitor of complement cascade amplification enzymes on cell surfaces.
    • CR1 provides a protective mechanism against complement-mediated cellular damage during substrate binding.
    • CR1's dual role in adherence and inhibition highlights its importance in regulating complement activation.