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Departments of Immunology and Internal Medicine, Mayo Clinic and Mayo Foundation, Rochester, MN 55905; and
Departments of Immunology and Immunopathology, Kagawa Medical School, Kagawa, Japan
Ecalectin, produced by Ag-stimulated T lymphocytes, is a potent
eosinophil-specific chemoattractant in vitro as well as in vivo and
thus is implicated in allergic responses. Ecalectin differs
structurally from other known eosinophil chemoattractants (ECAs);
ecalectin belongs to the galectin family defined by their affinity for
-galactosides and by their conserved carbohydrate recognition
domains. These characteristic features suggest that ecalectin has
unique activities associated with allergic inflammation besides ECA
activity. Conversely, ecalectin may mediate ECA activity by binding to
a receptor of a known ECA via affinity for the -galactosides present
on this receptor. In this study, we have tested whether ecalectin
mediates ECA activity by binding to a receptor of a known ECA, and we
have assessed its effects on eosinophils. Ecalectin did not mediate ECA
activity by binding to the IL-5R or to CCR3. Also, the ECA activity of
ecalectin was mainly chemokinetic. In addition, ecalectin induced
concentration-dependent eosinophil aggregation, a marker for eosinophil
activation. Ecalectin induced concentration-dependent superoxide
production from eosinophils but did not induce degranulation; usually
these two events are coupled in eosinophil activation. Moreover,
ecalectin directly prolonged eosinophil survival in vitro and did not
trigger eosinophils to secrete cytokines that prolong eosinophil
survival. These results demonstrate that ecalectin has several unique
effects on eosinophils. Therefore, we conclude that ecalectin is a
novel eosinophil-activating factor. Presumably, these effects allow
ecalectin to play a distinctive role in allergic
inflammation.
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