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CUTTING EDGE |
Department of Medicine, Harvard Thorndike Laboratories, Charles A. Dana Research Institute, Beth Israel Deaconess Medical Center, Harvard Medical School, Boston, Massachusetts 02215
IL-4 release is important in promoting Th2-mediated allergic and
parasitic immune responses. Although human eosinophils are
potential sources of IL-4, physiologic mechanisms to elicit its release
have not been established. By flow cytometry and microscopy,
eosinophils from normal donors uniformly contained
preformed IL-4. In contrast to cytolytic IL-4 release from calcium
ionophore-activated eosinophils, eotaxin and RANTES, but
not IFN-
, elicited IL-4 release by noncytotoxic mechanisms. With a
dual Ab capture and detection immunofluorescent microscopic assay, IL-4
was released at discrete cell surface sites. IL-5 enhanced
eotaxin-induced IL-4 release, which was mediated by G protein-coupled
CCR3 receptors, detectable as early as 5 min and maximum within 1
h. IL-4 release was not diminished by transcription or protein
synthesis inhibitors, but was suppressed by brefeldin A, an inhibitor
of vesicle formation. Thus, CCR3-mediated signaling can rapidly
mobilize IL-4 stored preformed in human eosinophils for
release by vesicular transport to contribute to immune
responses.
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