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  • Title: Interaction of zymosan and of activated properdin with factor D-depleted guinea pig serum: implications for the mechanism of initial C3 cleavage via the alternative complement pathway.
    Author: Brade V, Bentley C, Bitter-Suermann D, Hadding U.
    Journal: Z Immunitatsforsch Immunobiol; 1977 Feb; 152(5):402-14. PubMed ID: 556571.
    Abstract:
    Factor D of the alternative C pathway was specifically removed from guinea pig serum. The resulting serum reagent (RD) supported neither the formation of a C3-cleaving enzyme on zymosan (Z) nor the inactivation of C3 or of factor B in the presence of Z or activated properdin (P). Addition of purified D to RD restored these properties. Studies were limited amounts of purified D were added to RD with Z or P as activating substances, gave the following results: (1) Inactivation of B and of C3 occurs in the presence of minute amounts of D. (2) C3 inactivation is more efficient than B inactivation and proceeds even in the absence of detectable enzymatic B activation. (3) C3 cleavage at any D concentration tested is always accompanied by uptake of C3 fragments onto Z. With respect to initial C3 cleavage via the alternative C pathway these data suggest that the initiating reaction is D-dependent, very efficient in depositing C3 fragments on particulate activating substances such as Z and able to utilize factor B in an apparently uncleaved form.
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