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• W2036390167 abstract "Abstract Receptors for the Fc region of IgG (FcγRIIIa, FcγRIIc) and IgM (FcμR) were previously described on NK cells. In this work the expression of Fc receptors for IgA (FcαR) on humanNK cells and the signaling events were investigated. The FcαR was demonstrated by flow cytometry using secretory IgA (sIgA) and anti‐human IgA antibody. The percentage of NK cells (CD3 – CD56 + CD16 + ) expressing FcαR ranged between 55.7% and 95.7%, with a mean ± SD of 75.2±11.8. The association constant and the number of 125 I‐labeled sIgA ( 125 I‐sIgA) molecules bound per cell, calculated by Scatchard analysis, were 2×10 7 M –1 and 1.7×10 4 , respectively. The binding specificity was proved by inhibition experiments. Cold sIgA but not IgA Fab fragments were able to inhibit 125 I‐sIgA binding in a concentration‐dependent manner. Binding of sIgA to NK cells was neither inhibited by anti‐mannose receptor antibody, nor by L ‐fucose, D ‐galactose, D ‐glucose, D ‐mannose or N‐acetyl‐ D ‐glucosamine. Pretreatment of NK cells with polymeric IgA inhibited their capacity to kill 51 Cr‐labeled K562 target cells by 34.8%, whereas with monomeric IgA only by 13.1%. Ligand‐induced clustering of the FcαR resulted in activation of tyrosine kinases Lck, Syk and phosphatidylinositol 3‐kinase. The present studies support the concept that human NK cells bind preferentially sIgA and polymeric IgA with moderate affinity via FcαR, which is different from the FcαRI/CD89 and other carbohydrate‐recognizing receptors like mannose receptor/CD206. This novel structure mediates signal transduction and cell killing." @default.
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• W2036390167 date "2003-07-07" @default.
• W2036390167 modified "2023-10-17" @default.
• W2036390167 title "Human NK cells express Fc receptors for IgA which mediate signal transduction and target cell killing" @default.
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• W2036390167 doi "https://doi.org/10.1002/eji.200323534" @default.
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