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*
Laboratory of Immunology, Department of Clinical Biochemistry, Faculty of Chemical Sciences, National University of Cordoba, Cordoba, Argentina;
Department of Biological Chemistry, Faculty of Pharmacy and Biochemistry, National University of Buenos Aires, Buenos Aires, Argentina; and
Centro de Excelencia en Productos y Procesos de Córdoba (CEPROCOR), Cordoba, Argentina.
Galectins, a family of closely related ß-galactoside-binding
proteins, show specific immunomodulatory properties. We have recently
identified the presence of a galectin-like protein in rat peritoneal
macrophages by means of a cross-reactivity with a polyclonal Ab raised
against a galectin purified from adult chicken liver. Galectin
expression was up-regulated in inflammatory and activated macrophages,
revealing a significant increase in phorbol ester- and formylmethionine
oligopeptide-treated cells. In an attempt to further explore its
functional significance, rat macrophage galectin was purified from
activated macrophages by a single-step affinity chromatography on a
lactosyl-Sepharose matrix. The eluted fraction was resolved as a single
protein band of 
15,000 Da by SDS-PAGE that immunoreacted strongly
with the anti-chicken galectin serum. Gel filtration studies
revealed that the protein behaved like a dimer under native conditions,
and saccharides bearing a ß-D-galactoside
configuration were able to inhibit the hemagglutinating activity
displayed by the purified galectin. In agreement with its isoelectric
point of 4.8, the amino acid analysis showed a definitive acidic
pattern. Internal amino acid sequencing of selected peptides obtained
by proteolytic cleavage revealed that this carbohydrate-binding protein
shares all the absolutely preserved and critical residues found in
other members of the mammalian galectin-1 subfamily. Finally,
biochemical and ultrastructural evidence, obtained by genomic DNA
fragmentation and transmission electron microscopy, are also provided
to show its potential implications in the apoptotic program of T cells.
This effect was quantified by using the terminal deoxynucleotidyl
transferase-mediated dUTP biotin nick end-labeling assay and was found
to be associated to the specific carbohydrate-binding properties of
galectin.
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