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Activation of the Classical Pathway of Complement by the C3NeF-Stabilized Cell-Bound Amplification Convertase

From the Department of Nephrology, University Hospital, Leiden, The Netherlands

Abstract

C3 nephritic factor (C3Ne) 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, C3b,Bb(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 10¹² C3b,Bb(C3NeF) complexes/ml. On the other hand, cell-bound C3b,Bb(C3NeF) is capable of both binding ¹²⁵I-C1q and activating ¹²⁵I-C1. This discrepancy between fluid phase and cell-bound C3b,Bb(C3NeF) was found for C3NeF preparations from eight different patients and therefore seems to apply to all C3NeF preparations.

Footnotes

¹ Please address correspondence to: Dr. M. R. Daha, Department of Nephrology, University Hospital, 2333 AA Leiden, The Netherlands.