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*
Immunology Department, Fundación Jiménez Díaz, Madrid, Spain; and
Division of Allergy, La Jolla Institute for Allergy and Immunology, San Diego CA 92121
Galectin-3 is an animal lectin, formerly named 
-binding protein
or Mac-2, which has been described to play an important role in some
inflammatory processes by the implication of different cells and the
increase in cell adhesion functions through laminin binding activity.
In this work we analyzed the role of galectin-3 in the modulation of
Th2 cytokines that have an important role in the development of the
inflammatory response. We have found that the addition of galectin-3 to
human eosinophils, the eosinophilic cell line EoL-3, PBMC, and an
Ag-specific T cell line (CD4+) produced a selective
inhibition of IL-5 transcription. No inhibitory effect was found on the
IL-4 mRNA transcription rate. The inhibitory effect on IL-5
transcription was reversed by incubation with lactose and using
specific Ab against galectin-3. Galectin-3 is able to induce inhibition
of the IL-5 released in the supernatants from PBMC stimulated with
phorbol 12,13-dibutyrate and anti-CD3. Similar results were
obtained when a T-specific cell line was stimulated with Ag. Also,
EoL-3 stimulated with anti-CD32 produced IL-5 protein, the
synthesis of which was partially inhibited by galectin-3. The present
results demonstrate that galectin-3 induces a selective down-regulation
of IL-5 expression in different cell types, opening important new
possibilities in the regulation of the allergic reactions.
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