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Clinical & Experimental Allergy

IgE-dependent release of myeloperoxidase by neutrophils from allergic patients


Dr J. Monteseirín, Asunción 27, 3° Izda, 41011 Sevilla, Spain, E-mail:


Background The three forms of IgE receptor: the heterotrimeric high-affinity receptor for IgE (FcεRI), the low-affinity receptor for IgE (FcεRII/CD23) and the Mac-2/IgE-binding protein (εBP), have previously been found on human neutrophils. We have previously shown that specific allergens are able to activate functional responses by neutrophils from allergic patients sensitized to those allergens. Neutrophils are present in the sites of allergic inflammation. The primary (azurophilic) granules of neutrophils contain a variety of enzymes that might potentiate inflammation, such as myeloperoxidase (MPO). It is not known whether specific allergens are able to elicit MPO release by neutrophils from allergic patients.

Methods Neutrophils were challenged in vitro with the specific allergen that produced clinical symptoms in asthmatic patients. Also, the cells were challenged with allergens that the patients were not sensitive to. Neutrophils from normal subjects were also challenged with allergens.

Results The in vitro challenge of neutrophils with allergens that the patients were sensitive to elicited a release of MPO by these cells. The in vitro activation of neutrophils was highly allergen-specific, in such a way that allergens other than those accounting for clinical symptoms did not evoke MPO release, and allergens were ineffective on neutrophils from healthy donors.

Conclusion An IgE-dependent mechanism might promote MPO release by neutrophils at allergic sites.

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