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J Biol Chem, Vol. 273, Issue 27, 16976-16984, July 3, 1998
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From the A 1.6-kilobase pair cDNA was isolated from a
human T-cell-derived expression library that encodes a novel eosinophil
chemoattractant (designated ecalectin) expressed during allergic and
parasitic responses. Based on its deduced amino acid sequence,
ecalectin is a 36-kDa protein consisting of 323 amino acids. Although
ecalectin lacks a hydrophobic signal peptide, it is secreted from
mammalian cells. Ecalectin is not related to any known cytokine or
chemokine but rather is a variant of human galectin-9, a member of the
large family of animal lectins that have affinity for Department of Bacterial Infection, Institute
of Medical Science, University of Tokyo, Tokyo 108, Japan,
¶ Faculty of Applied Biological Science, Hiroshima University,
Higashi-Hiroshima 739, Japan, the Department of Immunology and
Immunopathology, Kagawa Medical School, Kagawa 761-07, Japan, and the
** Department of Medicine, Harvard Medical School, and Division of
Rheumatology, Immunology, and Allergy, Brigham and Women's Hospital,
Boston, Massachusetts 02115
-galactosides. Recombinant ecalectin, expressed in COS cells and insect cells, exhibited potent eosinophil chemoattractant activity and attracted eosinophils in vitro and in vivo in a
dose-dependent manner but not neutrophils, lymphocytes, or
monocytes. The finding that the ecalectin transcript is present in
abundance in various lymphatic tissues and that its expression
increases substantially in antigen-activated peripheral blood
mononuclear cells suggests that ecalectin is an important
T-cell-derived regulator of eosinophil recruitment in tissues during
inflammatory reactions. We believe that this is the first report of the
expression of an immunoregulatory galectin expressed by a T-cell line
that is selective for eosinophils.
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