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J. Biol. Chem., Vol. 282, Issue 29, 21081-21089, July 20, 2007

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Recognition Mechanism of Galectin-4 for Cholesterol 3-Sulfate^*

Hiroko Ideo, Akira Seko, and Katsuko Yamashita¹

From the Innovative Research Initiatives, Tokyo Institute of Technology, 4259 Nagatsuta-cho, Midori-ku, Yokohama 226-8503 and Core Research for Evolutional Science and Technology, Japan Science and Technology Agency, 4-1-8 Honcho, Kawaguchi, Saitama 332-0012, Japan

Galectin-4 binds to glycosphingolipids carrying 3-O-sulfated Gal residues, and it co-localizes on the cell surface of human colonic adenocarcinoma cells with glycosphingolipids carrying SO^–₃3Gal13(GalNAc) residues (Ideo, H., Seko, A., and Yamashita, K. (2005) J. Biol. Chem. 280, 4730–4737). In the present study, it was found that galectin-4 also binds to cholesterol 3-sulfate, which has no -galactoside moiety. This characteristic of galectin-4 is unique within the galectin family. The site-directed mutated galectin-4-R45A had diminished binding ability toward cholesterol 3-sulfate, suggesting that Arg⁴⁵ of galectin-4 is indispensable for cholesterol 3-sulfate recognition. Gel filtration and chemical cross-linking experiments revealed that some galectin-4 exists as dimers, and this multivalency seemed to enhance its avidity for cholesterol 3-sulfate binding. Cholesterol 3-sulfate and sulfatide co-existed with galectin-4 in detergent-insoluble fractions of porcine esophagus and intestine, respectively. These results suggested that not only sulfated glycosphingolipids but also cholesterol 3-sulfate are endogenous ligands for galectin-4 in vivo.

Received for publication, May 8, 2007

^* Part of this work was supported by Grant-in-aid for Scientific Research on Priority Area(s) 14082208 from the Ministry of Education, Culture, Sports, Science, and Technology of Japan. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

¹ To whom correspondence should be addressed: Tokyo Institute of Technology, Innovative Research Initiatives, 4259 Nagatsuta-cho, Midori-ku, Yokohama 226-8503, Japan. Tel./Fax: 81-45-921-4308; E-mail: kyamashi{at}bio.titech.ac.jp.

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