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Low Molecular Weight C1q-Precipitins in Hypocomplementemic Vasculitis-Urticaria Syndrome: Partial Purification and Characterization as Immunoglobulin^1,2,

From the Departments of Immunology and Pathology, Rush Medical College and Department of Medicine, Northwestern University, School of Medicine, Chicago, Illinois

Abstract

A lupus-like syndrome involving chronic urticaria with cutaneous vasculitis, systemic symptoms, hypocomplementemia with preferential depletion of C1q, and low m.w. (7S) C1q-precipitins has recently been defined. The C1q-precipitin activity (C1q-p) seems to represent a diagnostic marker of the disease, but its chemical nature is not yet clear. We have partially purified and characterized C1q-p from the serum of two patients with this syndrome and compared its activity with the C1q-precipitating activity of aggregated human -globulin (AHGG), anti-C1q antibodies, and several polynucleotides including DNA and polyinosinic acid. C1q-p was found to partition with IgG during precipitation by ammonium sulfate and low ionic strength buffer as well as during column chromatography on DEAE-cellulose and G-200 Sephadex. Like AHGG, but in complete contrast to the polynucleotides, the C1q-precipitating activity of C1q-p was sensitive to pepsin, trypsin, and acidic conditions, but unaffected by DNAse or RNAse; the C1q-precipitating activity of anti-C1q antibody was not diminished by any of these procedures. Thus, C1q-p consists of -migrating protein of low m.w., and its C1q-precipitating activity is indistinguishable from that of AHGG. These results are consistent with the concept that C1q-p is comprised, at least in part, of IgG that binds C1q via the Fc portion of the molecule.

Footnotes

¹ This work was supported in part by the Hunter Fund.

² Presented in part to the annual meeting of the American Society for Clinical Investigation (Clin. Res., 1978, in press).

³ Holder of the Thomas J. Coogan, Sr. Chair in Immunology established by Marjorie Lindheimer Everett.

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