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J. Biol. Chem., Vol. 279, Issue 33, 35001-35008, August 13, 2004

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N-Acetylglucosamine 6-O-Sulfotransferase-1 Regulates Expression of L-Selectin Ligands and Lymphocyte Homing^*

Kenji Uchimura¶, Kenji Kadomatsu, Fathy M. El-Fasakhany, Mark S. Singer, Mineko Izawa||, Reiji Kannagi||, Naoki Takeda**, Steven D. Rosen, and Takashi Muramatsu

From the Department of Biochemistry, Nagoya University Graduate School of Medicine, Nagoya 466-8550, Japan, the Department of Anatomy, Program in Immunology, University of California, San Francisco, California 94143, the ^||Program of Molecular Pathology, Aichi Cancer Center, Research Institute, Nagoya 464-8681, Japan, and the ^**Center for Animal Resources and Development, Kumamoto University, Kumamoto 860-0811, Japan

Lymphocyte homing is initiated by the binding of L-selectin on lymphocytes to its ligands on high endothelial venules (HEV). Sialyl 6-sulfo Lewis X is a major capping group of L-selectin ligands. N-Acetylglucosamine (GlcNAc) 6-sulfation is essential for the ligand activity, and is catalyzed by GlcNAc 6-O-sulfotransferases (GlcNAc6STs) of which GlcNAc6ST-1 and GlcNAc6ST-2 are expressed in HEV. Here, we report that mice deficient in GlcNAc6ST-1 were impaired in the elaboration of sialyl 6-sulfo Lewis X in HEV and that an epitope of L-selectin ligands recognized by the MECA-79 anti-body was greatly reduced or abolished in the abluminal aspect of HEV. Lymphocyte homing to peripheral lymph nodes, mesenteric lymph nodes, and Peyer's patches was significantly reduced in GlcNAc6ST-1 null mice. These results demonstrate that GlcNAc6ST-1 is involved in lymphocyte homing in vivo, and indicate that GlcNAc6ST-1 and -2 play complementary roles. The importance of GlcNAc6ST-1 is particularly high-lighted by its involvement in lymphocyte homing to Peyer's patches where GlcNAc6ST-2 expression is undetectable.

Received for publication, April 22, 2004 , and in revised form, June 1, 2004.

^* This work was supported in part by a grant-in-aid for Priority Area (14082202) from the Ministry of Education, Culture, Sports, Science and Technology of Japan and the Mizutani Foundation for Glycoscience (to T. M.), and National Institutes of Health Grants GM57411 and R37GM23547 (to S. D. R.). 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.

^¶ Research Fellow of the Japan Society for the Promotion of Science.

To whom correspondence should be addressed: Dept. of Biochemistry, Nagoya University Graduate School of Medicine, 65 Tsurumaicho, Showa-ku, Nagoya 466-8550, Japan. Tel.: 81-52-744-2-59; Fax: 81-52-744-2065; E-mail: tmurama{at}med.nagoya-u.ac.jp.

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