Glycobiology Advance Access published online on July 24, 2003
Glycobiology, doi:10.1093/glycob/cwg102
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© 2003 Oxford University Press
ORIGINAL ARTICLES
1 Department of Endocrinology, Kagawa Medical University, Kagawa 761-0793, Japan The members of the galectin family are associated with diverse cellular events including immune response. We investigated the effects of galectin-8 on neutrophil function. Human galectin-8 induced firm and reversible adhesion of peripheral blood neutrophils, but not eosinophils, to a plastic surface in a lactose-sensitive manner. Other human galectins, galectin-1, -3 and -9, showed low or negligible effects on neutrophil adhesion. Confocal microscopy revealed actin bundle formation in the presence of galectin-8. Cytochalasins inhibited both actin assembly and cell adhesion induced by galectin-8. Affinity purification of galectin-interacting proteins from solubilized neutrophil membrane revealed that N-terminal carbohydrate recognition domain (CRD) of galectin-8 bound promatrix metalloproteinase-9 (proMMP-9), and C-terminal CRD bound integrin
Revised on July 7, 2003
Accepted on July 10, 2003
Galectin-8 modulates neutrophil function via interaction with integrin
M
2 GalPharma Co., Ltd., Kagawa 761-0301, Japan
3 Research Equipment Center, Kagawa Medical University, Kagawa 761-0793, Japan
4 Department of Immunology and Immunopathology, Kagawa Medical University, Kagawa 761-0793, Japan
M/CD11b and proMMP-9. A mutant galectin-8 lacking the carbohydrate-binding activity of N-terminal CRD (galectin-8R69H) retained adhesion-inducing activity but inactivation of C-terminal CRD (galectin-8R233H) abolished the activity. MMP-3-mediated processing of proMMP-9 was accelerated by galectin-8 and this effect was inhibited by lactose. Galectin-1 and -3 did not affect the processing. Superoxide production, an essential event in bactericidal function of neutrophils, was stimulated by galectin-8 to an extent comparable to that induced by fMLP. Galectin-8R69H but not galectin-8R233H could stimulate superoxide production. Taken together, these results suggest that galectin-8 is a novel factor that modulates the neutrophil function related to transendothelial migration and microbial killing.
galectin, inflammation, integrin, matrix metalloproteinase, neutrophil
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