Glycobiology Advance Access originally published online on July 24, 2003
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Glycobiology, 2003, Vol. 13, No. 11 755-763
© 2003 Oxford University Press
Galectin-8 modulates neutrophil function via interaction with integrin 
M
2 Department of Endocrinology, Kagawa Medical University, Kagawa 761-0793, Japan; 3 GalPharma Co., Ltd., Kagawa 761-0301, Japan; 4 Research Equipment Center, Kagawa Medical University, Kagawa 761-0793, Japan; and 5 Department of Immunology and Immunopathology, Kagawa Medical University, Kagawa 761-0793, Japan
Received on March 13, 2003; revised on July 7, 2003; accepted on July 10, 2003
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, galectins-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 
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. Galectins-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.
1 To whom correspondence should be addressed; e-mail: nnishi{at}kms.ac.jp
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