Activation of human monocytes via their sIgA receptors

S. Padeh, C. L. Jaffe, J. H. Passwell

Research output: Contribution to journalArticlepeer-review

Abstract

We have studied the interaction of secretory immunoglobulin A (sIgA) derived from human breast milk with human monocytes. The presence of specific sIgA receptors on the monocyte membrane was confirmed by dose-dependent inhibition of E-sIgA rosette formation and by the binding of iodinated sIgA to monocyte monolayers. Binding was dependent on both the number of monocytes, as well as the amount of [125I]sIgA, and could be inhibited by unlabelled sIgA. Incubation of monocyte monolayers in the presence of increasing concentrations of secretory IgA and F(ab')2 anti-IgA resulted in a dose-dependent increase of the oxidative burst, as measured by H2O2 production. Neither sIgA of anti-IgA alone, nor incubation of IgG with anti-IgA, had any effect on the oxidative burst. These studies indicate that human monocytes have a receptor for sIgA and that specific activation of the monocytes occurs via these receptors.

Original languageEnglish
Pages (from-to)188-193
Number of pages6
JournalImmunology
Volume72
Issue number2
StatePublished - 1991
Externally publishedYes

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