Binding of IgA to erythrocytes from patients with IgA nephropathy

Clinical Immunology and Immunopathology
S MatsudaJ Mestecky

Abstract

Primate erythrocytes (RBCs) may be involved in the transport and processing of C3b-containing immune complexes (IC). Compared to RBCs from healthy controls, increased amounts of IgA were detectable on RBCs from 7 of 17 patients with IgA nephropathy (IgA NP). There was no difference in the amount of IgG or IgM. The highest amount of RBC-bound IgA corresponded to 6 ng IgA/10(8) cells. The mechanisms involved in the binding of IgA to RBCs were investigated in vitro. Isolated IgA1 or IgA2 did not bind to RCBs from a patient with IgA deficiency. In contrast, incubation of RBCs with a polyethyleneglycol (PEG) precipitate of serum from a patient with IgA NP which contained IgA-IC resulted in IgA1 binding. However, this binding was not inhibited by monoclonal anti-CR1 or by an excess of IgG or IgM. Factor I did not cause release of IgA from RBCs from patients with IgA NP. Heat-aggregated IgA1 also bound to RBCs and this binding was not affected by the presence of complement. We conclude that minute amounts of IgA-IC are bound to RBCs by a complement- and Fc receptor-independent mechanism. The quantity of IgA-IC associated with RBC is so small that it is unlikely to represent an important in vivo route of IgA-IC transport or processing.

References

Oct 22, 1965·Science·T Borsos, H J Rapp

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Citations

Mar 22, 2001·Clinical and Experimental Allergy : Journal of the British Society for Allergy and Clinical Immunology·P GriffinA D Curran
Jan 1, 1992·Digestive Diseases and Sciences·B LavöR Hällgren
Oct 28, 2008·Médecine sciences : M/S·Vincent AudardDil Sahali
Jul 1, 1991·American Journal of Kidney Diseases : the Official Journal of the National Kidney Foundation·D RoccatelloR Mosso

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