Binding of IgA to erythrocytes from XXXX with @entity8 .

@entity1 @entity5727 @entity8 @entity3432 @entity7110 @entity4417 @entity7491 @entity970 @entity968
Primate erythrocytes (RBCs) may be involved in the transport and processing of @entity4417 -containing @entity7110 ( @entity7110 ). Compared to RBCs from healthy controls, increased amounts of IgA were detectable on RBCs from 7 of 17 @entity1 with @entity8 ( @entity8 ). 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 @entity5727 or IgA2 did not bind to RCBs from a @entity1 with @entity7491 . In contrast, incubation of RBCs with a @entity968 ( @entity970 ) precipitate of serum from a @entity1 with @entity8 which contained @entity7110 resulted in @entity5727 binding. However, this binding was not inhibited by monoclonal anti- @entity3432 or by an excess of IgG or IgM. Factor I did not cause release of IgA from RBCs from @entity1 with @entity8 . Heat-aggregated @entity5727 also bound to RBCs and this binding was not affected by the presence of complement. We conclude that minute amounts of @entity7110 are bound to RBCs by a complement- and Fc receptor-independent mechanism. The quantity of @entity7110 associated with RBC is so small that it is unlikely to represent an important in vivo route of @entity7110 transport or processing.
