Activation of the classical pathway of complement by the C3NeF-stabilized cell-bound amplification convertase.
C3 nephritic factor (C3NeF) has been shown to be composed of two heavy and two light chains, like IgG; in addition it shares antigenic determinants with IgG. C3NeF, purified from the sera of eight patients by incorporation of C3NeF into the stabilized fluid phase amplification C3 convertase, C3bBb(C3NeF), followed by its release after decay of convertase function, was investigated for its ability to bind 125I-C1q and to activate 125I-C1. It was found that although fluid phase C3b,Bb(C3NeF) is fully capable of binding 125I-C1q, it is not able to activate 125I-C1 even at concentrations of 1.3 x 10(12) C3bBb(C3NeF) complexs/ml. On the other hand, cell-bound C3bBb(C3NeF) is capable of both binding 125I-C1q and activating 125I-C1. This discrepancy between fluid phase and cell-bound, C3bBb(C3NeF) was found for C3NeF preparations from eight different patients and therefore seems to apply to all C3NeF preparations.
D001665:Binding Sites; D003166:Complement Activating Enzymes / Q000494:pharmacology*; D003167:Complement Activation; D003172:Complement C1; D003178:Complement C3 Nephritic Factor; D050577:Complement C3-C5 Convertases / Q000494:pharmacology*; D003169:Complement Inactivator Proteins; D003171:Complement Pathway, Classical; D004306:Dose-Response Relationship, Immunologic; D006801:Humans; D007457:Iodine Radioisotopes
D003172:Complement C1; D003178:Complement C3 Nephritic Factor; D003169:Complement Inactivator Proteins; D007457:Iodine Radioisotopes; D003166:Complement Activating Enzymes; D050577:Complement C3-C5 Convertases