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Departments of
*
Medicine and Physical Therapy, and
Bioregulatory Function, University of Tokyo School of Medicine, Tokyo, Japan;
Department of Pediatrics, National Mie Hospital, Mie, Japan; and
§
Department of Pathology, Nihon University School of Dentistry, Tokyo, Japan
We examined whether secretory IgA (sIgA), known to mediate
eosinophil stimulation, has an effect on basophil functions. An
immobilized preparation of sIgA, but not of monomeric IgA, induced
histamine release (approximately 15% of total histamine contents) from
human basophils in vitro. sIgA-induced basophil histamine release was
totally dependent on pretreatment with IL-3. IL-5 and
granulocyte-macrophage CSF also primed basophils for sIgA-mediated
release. Exogenous divalent ions, i.e., Ca2+ and
Mg2+, were essential for sIgA-mediated basophil
degranulation, and the degranulation was completed within 45 min. A
newly synthesized lipid mediator, leukotriene C4, was also
liberated from IL-3-primed, sIgA-stimulated basophils. Enzyme digestion
experiments revealed that the (Fc)2·secretory component
portion of sIgA is important for sIgA-mediated basophil activation, but
the functional binding sites of sIgA on basophils were surmised to be
different from Fc
R. These observations reveal the novel finding that
sIgA is able to stimulate basophils as well as eosinophils. Since sIgA
is the most abundant Ig isotype in the secretions from mucosal tissues,
and basophils are active participants in allergic late-phase reactions,
sIgA-mediated basophil mediator release is potentially involved in
exacerbation of the inflammation associated with allergic
disorders.
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