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. 1988 Aug;64(4):703–708.

Binding, internalization and degradation of soluble aggregates of human secretory IgA by resident rat peritoneal macrophages.

A Gorter 1, P S Hiemstra 1, N Klar-Mohamad 1, L A van Es 1, M R Daha 1
PMCID: PMC1384994  PMID: 3169844

Abstract

In the present study the in vitro binding, internalization and degradation of IgA immune complexes (IC) by phagocytes was studied. As a model for IgA IC, heat-aggregated human secretory IgA (AsIgA) was prepared and resident rat peritoneal macrophages (PM phi) were used as a source of phagocytes. First, binding of 125I-AsIgA to rat PM phi was investigated. Binding of 125I-AsIgA to PM phi at 4 degrees was saturable and reached plateau values after 2 hr. At 37 degrees, degradation of membrane-bound 125I-AsIgA into trichloroacetic acid (TCA)-soluble fragments occurred. Parallel experiments with unlabelled AsIgA and 125I-labelled anti-human IgA revealed that degradation of AsIgA was preceded by internalization of AsIgA. The specificity of binding of 125I-AsIgA to PM phi was investigated using human IgG, human serum IgA, human myeloma IgA1, human sIgA and the glycoproteins asialofetuin and ovalbumin. The binding of 125I-AsIgA to rat PM phi was inhibited in the presence of sIgA and asialofetuin. In contrast IgG and ovalbumin had no effect. These results suggest that receptors with a specificity for galactose on the rat PM phi are involved in the binding of AsIgA.

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Selected References

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