C1q solid-phase radioimmunoassay: binding properties of solid-phase C1q and evidence that C1q-binding IgG complexes in systemic lupus erythematosus are not bound to endogenous C1q.
The binding properties of C1q solid-phase radioimmunoassay (C1q SPRIA) were examined, using heat-aggregated IgG (HAG) as the model of immune complexes (IC). The free, liquid-phase C1q, which was added to the C1q-coated tubes prior to the addition of HAG, had little inhibitory effect on binding of HAG to the solid-phase C1q, suggesting that the solid-phase C1q has a higher affinity for HAG than the liquid-phase C1q. On the other hand, more than 60% inhibition was seen when HAG was preincubated with the liquid-phase C1q. These binding properties of HAG to the solid-phase C1q in the presence of the liquid-phase C1q were not essentially altered by the heat inactivation or the addition of EDTA, suggesting that these pretreatments are not essential in C1q SPRIA. Next, in similar kinds of experiments, the binding properties of C1q-binding IgG complexes in SLE sera were investigated. In contrast to HAG, the binding capacity of IgG complexes in SLE sera to the solid-phase C1q was not inhibited by the preincubation with excess liquid-phase C1q. These findings suggest that C1q-binding IgG complexes in SLE sera detected by C1q SPRIA may not be bound to endogenous C1q in the circulation.
D000936:Antigen-Antibody Complex; D001323:Autoantibodies / Q000276:immunology; D003166:Complement Activating Enzymes / Q000032:analysis / Q000276:immunology*; D015922:Complement C1q; D004492:Edetic Acid / Q000494:pharmacology; D006358:Hot Temperature; D006801:Humans; D007074:Immunoglobulin G / Q000276:immunology*; D008180:Lupus Erythematosus, Systemic / Q000276:immunology*; D011863:Radioimmunoassay / Q000379:methods; D012995:Solubility
D000936:Antigen-Antibody Complex; D001323:Autoantibodies; D007074:Immunoglobulin G; D015922:Complement C1q; D004492:Edetic Acid; D003166:Complement Activating Enzymes