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Related Experiment Videos

Evidence that a nicked C4b, C4b', is a functionally active C4b derivative.

M Yamazaki, C Ichihara, S Nagasawa

    FEBS Letters
    |November 10, 1986
    PubMed
    Summary

    Factor I inactivates the complement system

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    Area of Science:

    • Immunology
    • Biochemistry

    Background:

    • The classical pathway of the complement system is regulated by Factor I-catalyzed C4b cleavage.
    • This cleavage occurs in two steps, producing an intermediate C4b' and then C4c and C4d.

    Purpose of the Study:

    • To determine which cleavage step inactivates C4b's function in C3 convertase assembly.

    Main Methods:

    • Purification of C4b'.
    • Assessment of C4b's ability to assemble C3 convertase with C2 using size exclusion high-performance liquid chromatography.

    Main Results:

    • C4b' retains the ability to assemble C3 convertase with C2.
    • The second cleavage step, C4b' to C4c and C4d, is the primary inactivation step.

    Conclusions:

    • The cleavage of C4b' into C4c and C4d is the critical step for inactivating C4b function in C3 convertase assembly.
    • This finding clarifies the regulatory mechanism of the classical complement pathway.

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