Glycobiology, 2002, Vol. 12, No. 2 111-118
© 2002 Oxford University Press
Regulation of galectin-9 expression and release in Jurkat T cell line cells
2Department of Immunology and Immunopathology, Kagawa Medical University, 1750-1 Ikenobe, Miki-Cho, Kita-gun, Kagawa 761-0793, Japan; 3Department of Neuroscience, University of Calgary, Calgary, Alberta, Canada; 4Department of Endocrinology, Kagawa Medical University, 1750-1 Ikenobe, Miki-Cho, Kita-gun, Kagawa 761-0793, Japan; and 5Department of Immunology, Mayo Clinic, Rochester, MN 55905
Ecalectin/galectin-9 was recently described as a novel eosinophil chemoattractant highly expressed in immune tissues. We investigated the regulation of galectin-9 expression and release in Jurkat (a T cell line) cells. We demonstrated that medium and long-sized galectin-9 isoforms were constitutively expressed, and phorbol 12-myriastate 13-acetate (PMA) upregulated the level of galectin-9 mRNA in Jurkat cells. Western blotting and flow cytometry analyses revealed that PMA stimulation resulted in the upregulation of both intracellular and surface galectin-9 protein. The stimulated Jurkat cells simultaneously released evident eosinophil chemoattractant activity (ECA). Main ECA was adsorbed by both lactose and anti-galectin-9 antibody affinity column, suggesting that the ECA was ascribed to galectin-9. When Jurkat cells were stimulated with PMA in the presence of a BB94, a matrix metalloproteinase (MMP) inhibitor, but not tissue inhibitor of metalloproteinase-1 (TIMP-1), the release of galectin-9 was suppressed in a dose-dependent manner. We further found that calphostin c, a protein kinase c (PKC) inhibitor, weakly but significantly suppressed the release of galectin-9. The present data suggested that galectin-9 production in Jurkat cells is provoked by the stimulation with PMA and that some MMP and PKC is, at least, partly involved in the release of galectin-9 from Jurkat cells.
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