IgA-induced chemokinesis of human polymorphonuclear neutrophils: requirement of their Fc-alpha receptor.
(1987) Molecular Immunology — Vol. 24, n° 6, p. 551-559 (1987)
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- The influence of purified human immunoglobulins on the migration of human neutrophils (PMN) was measured in a 48-well micro chemotaxis chamber, with results expressed as percentages of maximal formyl-methionyl-leucyl-phenylalanine (FMLP)-stimulated chemotaxis. Both monomeric and polymeric IgA, of both subclasses, in monoclonal and polyclonal form, as well as secretory IgA and Fc-alpha, but not Fab-alpha fragments, enhanced PMN migration when present either in the lower or in both compartments of the chamber (chemokinesis) at concns as low as 0.1 mg/ml. IgM and IgE had no such effect. In contrast, IgG was chemotactic at low concn (0.1 mg/ml). Both monomeric and polymeric IgA decreased the maximally induced FMLP-chemotaxis, but IgA increased chemotaxis induced by suboptimal levels of FMLP. Binding of 3[H]-FMLP to PMN was not affected. Cytofluorographic analysis revealed that, under the conditions of the assay, IgA did bind to 93% of PMN. Thus, the various forms of IgA have a dual effect on human PMN mobility: (1) increase PMN random migration (chemokinesis); and (2) decrease the maximal FMLP-induced chemotaxis. Our data support the requirement of binding of IgA to the Fc-alpha receptor of PMN for expression of these activities. This effect of IgA on PMN mobility may be relevant in IgA deficiency states.
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Sibille, Y., Merill, W. W., Chatelain, B., & Vaerman, J.-P. (1987). IgA-induced chemokinesis of human polymorphonuclear neutrophils: requirement of their Fc-alpha receptor. Molecular Immunology, 24(6), 551-559. https://doi.org/10.1016/0161-5890(87)90035-6 (Original work published 1987)