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Glycobiology, 2002, Vol. 12, No. 3 199-208
© 2002 Oxford University Press

High-affinity binding of recombinant human galectin-4 to SO3–->3Galß1->3GalNAc pyranoside

Hiroko Ideo2, Akira Seko2,3, Takashi Ohkura2,3, Khushi L. Matta4 and Katsuko Yamashita1,2,3

2CREST (Core Research for Evolutional Science and Technology) of the Japan Science and Technology Corporation, 2-3, Kanda-Surugadai, Chiyoda-ku, Tokyo 101-0062, Japan; 3Department of Biochemistry, Sasaki Institute, 2-2, Kanda-Surugadai, Chiyoda-ku, Tokyo 101-0062; and 4Department of Gynecologic Oncology, Roswell Park Memorial Cancer Institute, Buffalo, New York, USA

Galectin-4 is a member of galectin family and has two carbohydrate recognition domains. Although galectin-4 has been thought to function in cell adhesion, its precise carbohydrate binding specificity has not yet been clarified. We studied the carbohydrate binding specificity of galectin-4 comparatively with that of galectin-3, using surface plasmon resonance, galectin-3- or -4-Sepharose column chromatography and the inhibition assay of their binding to immobilized asialofetuin. Galectin-3 broadly recognized lactose, type 1, type 2, and core 1. The substitution at the C-2 and C-3 position of ß-galactose in these oligosaccharides with {alpha}-fucose, {alpha}-GalNAc, {alpha}-Neu5Ac, or sulfate increased the binding ability for galectin-3, whereas the substitution at the C-4 or C-6 position diminished the affinity. In contrast, galectin-4 had quite weak affinity to lactose, type 1, and type 2 (Kd {cong} 8 x 10–4 M). Galectin-4 showed weak binding ability to core 1 and C-2' or -3'-substituted lactose, type 1, and type 2 with {alpha}-fucose, {alpha}-GalNAc, or sulfate (Kd : 5 x 10–5 ~ 3 x 10–4 M). Interestingly, the Kd value, 3.4 x 10–6 M, of SO3–->3Galß1->3GalNAc-O-Bn to galectin-4 at 25°C was two orders of magnitude lower than that of core 1-O-Bn. 3'-Sialylated core 1 had very weak affinity to galectin-4, suggesting that 3'-O-sulfation of core 1 is critical for the recognition. These results suggest that galectin-4 has a unique carbohydrate binding specificity and interacts with O-linked sulfoglycans.

1 To whom correspondence should be addressed at the Department of Biochemistry, Sasaki Institute


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