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  • Title: Activation of human monocytes via their sIgA receptors.
    Author: Padeh S, Jaffe CL, Passwell JH.
    Journal: Immunology; 1991 Feb; 72(2):188-93. PubMed ID: 2016119.
    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 or 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.
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