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J. Biol. Chem., Vol. 280, Issue 44, 37178-37182, November 4, 2005

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Sugar-binding Properties of VIP36, an Intracellular Animal Lectin Operating as a Cargo Receptor^*

Yukiko Kamiya¶, Yoshiki Yamaguchi, Noriko Takahashi||, Yoichiro Arata**, Ken-ichi Kasai**, Yoshito Ihara, Ichiro Matsuo, Yukishige Ito, Kazuo Yamamoto¶¶, and Koichi Kato¶||1

From the Graduate School of Pharmaceutical Sciences, Nagoya City University, 3-1 Tanabe-dori, Mizuho-ku, Nagoya 467-8603, Japan, Core Research for Evolutional Science and Technology, Japan Science and Technology Agency, 4-1-8 Honcho, Kawaguchi, 332-1102, Japan, ^¶Institute for Molecular Science, Okazaki National Research Institutes 5-1 Higashiyama Myodaiji, Okazaki, Aichi 444-8787, Japan, ^||GLYENCE Co., Ltd., 1-4-6 Masaki, Naka-ku, Nagoya 460-8690, Japan, ^**Department of Biological Chemistry, Faculty of Pharmaceutical Sciences, Teikyo University, Sagamiko, Kanagawa 199-0195, Japan, Department of Biochemistry and Molecular Biology in Disease, Atomic Bomb Disease Institute, Graduate School of Biomedical Sciences, Nagasaki University, Nagasaki 852-8523, Japan, RIKEN (The Institute of Physical and Chemical Research), 2-1 Hirosawa, Wako-shi, Saitama 351-0198, Japan, and ^¶¶Graduate School of Frontier Sciences, University of Tokyo, 5-1-5 Kashiwanoha, Kashiwa, Chiba 277-8562, Japan

The vesicular integral protein of 36 kDa (VIP36) is an intracellular animal lectin that acts as a putative cargo receptor, which recycles between the Golgi and the endoplasmic reticulum. Although it is known that VIP36 interacts with glycoproteins carrying high mannose-type oligosaccharides, detailed analyses of the sugar-binding specificity that discriminates isomeric oligosaccharide structures have not yet been performed. In the present study, we have analyzed, using the frontal affinity chromatography (FAC) method, the sugar-binding properties of a recombinant carbohydrate recognition domain of VIP36 (VIP36-CRD). For this purpose, a pyridylaminated sugar library, consisting of 21 kinds of oligosaccharides, including isomeric structures, was prepared and subjected to FAC analyses. The FAC data have shown that glucosylation and trimming of the D1 mannosyl branch interfere with the binding of VIP36-CRD. VIP36-CRD exhibits a bell-shaped pH dependence of sugar binding with an optimal pH value of 6.5. By inspection of the specificity and optimal pH value of the sugar binding of VIP36 and its subcellular localization, together with the organellar pH, we suggest that VIP36 binds glycoproteins that retain the intact D1 mannosyl branch in the cis-Golgi network and recycles to the endoplasmic reticulum where, due to higher pH, it releases its cargos, thereby contributing to the quality control of glycoproteins.

Received for publication, May 26, 2005 , and in revised form, August 25, 2005.

^* This work was supported in part by grants-in-aid from the Ministry of Education, Culture, Sports, Science, and Technology of Japan and by Research on Health Sciences focusing on Drug Innovation from the Japan Health Sciences Foundation. 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: Graduate School of Pharmaceutical Sciences, Nagoya City University, 3-1 Tanabe-dori, Mizuho-ku, Nagoya 467-8603, Japan. Tel.: 81-52-836-3447; Fax: 81-52-836-3447; E-mail: kkato{at}phar.nagoya-cu.ac.jp.

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