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Glycobiology Advance Access published online on January 12, 2007
Glycobiology, doi:10.1093/glycob/cwm001
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© The Author 2007. Published by Oxford University Press. All rights reserved. For permissions, please e-mail: journals.permissions@oxfordjournals.org

Carbohydrate-recognition domains of galectin-9 are involved in intermolecular interaction with galectin-9 itself and other members of the galectin family

Nobumitsu Miyanishi1, Nozomu Nishi2,5, Hiroko Abe3, Yumiko Kashio4, Rika Shinonaga5, Shin-ichi Nakakita1, Wataru Sumiyoshi1, Akira Yamauchi5,6, Takanori Nakamura2, Mitsuomi Hirashima4,5 and Jun Hirabayashi1,7,*

1 Department of Functional Glycomics, Life Science Research Center
2 Division of Endocrinology, Faculty of Medicine
3 Research Center for Health Technology, National Institute of Advanced Industrial Science and Technology, AIST, 2217-14, Hayashi-machi, Takamatsu, Kagawa 761-0395, JAPAN
4 Division of Immunology, Faculty of Medicine, Kagawa University, 1750-1 Ikenobe, Miki-cho, Kita-gun, Kagawa 761-0793, JAPAN
5 GalPharma Co., Ltd., 2217-44 Hayashi-machi, Takamatsu, Kagawa 761-0301, JAPAN
6 Division of Cell regulation, Faculty of Medicine, Kagawa University, 1750-1 Ikenobe, Miki-cho, Kita-gun, Kagawa 761-0793, JAPAN
7 Research Center for Medical Glycoscience, National Institute of Advanced Industrial Science and Technology, AIST, Central 2, 1-1-1, Umezono, Tsukuba, Ibaraki 305-8568, JAPAN

* To whom correspondence should be addressed: Jun Hirabayashi, Department of Functional Glycomics, Life Science Research Center, Kagawa University, 1750-1 Ikenobe, Miki-cho, Kita-gun, Kagawa 761-0793, JAPAN, TEL: +81-87-891-2409; FAX; +81-87-891-2410; E-mail: glycofun{at}med.kagawa-u.ac.jp

Received on November 8, 2006; revised on December 25, 2006; accepted on January 6, 2007

Galectin-9 (Gal-9) is a tandem-repeat-type member of the galectin family associated with diverse biological processes, such as apoptosis, cell aggregation and eosinophil chemoattraction. Although the detailed sugar-binding specificity of Gal-9 has been elucidated, molecular mechanisms that underlie these functions remain to be investigated. During the course of our binding study by affinity chromatography and surface plasmon resonance (SPR) analysis, we found that human Gal-9 interacts with immobilized Gal-9 in the protein-protein interaction mode. Interestingly, this intermolecular interaction strongly depended on the activity of the carbohydrate recognition domain (CRD), because the addition of potent saccharide inhibitors abolished the binding. The presence of multimers was also confirmed by Ferguson plot analysis of result of polyacrylamide gel electrophoresis and matrix-assisted laser-desorption/ionization time-of-flight (MALDI-TOF) mass spectrometry (MS). Moreover, this intermolecular interaction was observed between Gal-9 and other galectin members, such as Gal-3 and Gal-8, but not Gal-1. Because such properties have not been reported yet, they may explain an unidentified mechanism underlying the diverse functions of Gal-9.

Key words: galectin / interaction / multimer / CRD / cross-interaction


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