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J. Biol. Chem., Vol. 280, Issue 25, 23876-23883, June 24, 2005

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A Non-sulfated Form of the HNK-1 Carbohydrate Is Expressed in Mouse Kidney^*

Hideki Tagawa, Yasuhiko Kizuka, Tomoko Ikeda, Satsuki Itoh¶, Nana Kawasaki¶, Hidetake Kurihara||, Maristela Lika Onozato**, Akihiro Tojo**, Tatsuo Sakai||, Toshisuke Kawasaki, and Shogo Oka

From the Department of Biological Chemistry and Core Research for Evolutional Science and Technology, Japan Science and Technology Corporation, Graduate School of Pharmaceutical Sciences, Kyoto University, Kyoto 606-8501, Japan, the ^¶Division of Biological Chemistry and Biologicals, National Institute of Health Sciences, Tokyo 158-8501, Japan, the ^||Department of Anatomy, Juntendo University School of Medicine, Tokyo 113-8421, Japan, and the ^**Division of Nephrology and Endocrinology, University of Tokyo, Tokyo 113-8655, Japan

The HNK-1 carbohydrate, which is recognized by anti-HNK-1 antibody, is well known to be expressed predominantly in the nervous system. The characteristic structural feature of the HNK-1 carbohydrate is 3-sulfo-glucuronyl residues attached to lactosamine structures (Gal1-4GlcNAc) on glycoproteins and glycolipids. The biosynthesis of the HNK-1 carbohydrate is regulated mainly by two glucuronyltransferases (GlcAT-P and GlcAT-S) and a sulfotransferase. In this study, we found that GlcAT-S mRNA was expressed at higher levels in the kidney than in the brain, but that both GlcAT-P and HNK-1 sulfotransferase mRNAs, which were expressed at high levels in the brain, were not detected in the kidney. These results suggested that the HNK-1 carbohydrate without sulfate (non-sulfated HNK-1 carbohydrate) is expressed in the kidney. We substantiated this hypothesis using two different monoclonal antibodies: one (anti-HNK-1 antibody) requires sulfate on glucuronyl residues for its binding, and the other (antibody M6749) does not. Western blot analyses of mouse kidney revealed that two major bands (80 and 140 kDa) were detected with antibody M6749, but not with anti-HNK-1 antibody. The 80- and 140-kDa band materials were identified as meprin and CD13/aminopeptidase N, respectively. We also confirmed the presence of the non-sulfated HNK-1 carbohydrate on N-linked oligosaccharides by multistage tandem mass spectrometry. Immunofluorescence staining with antibody M6749 revealed that the non-sulfated HNK-1 carbohydrate was expressed predominantly on the apical membranes of the proximal tubules in the cortex and was also detected in the thin ascending limb in the inner medulla. This is the first study indicating the presence of the non-sulfated HNK-1 carbohydrate being synthesized by GlcAT-S in the kidney. The results presented here constitute novel knowledge concerning the function of the HNK-1 carbohydrate.

Received for publication, February 15, 2005 , and in revised form, April 20, 2005.

^* This work was supported in part by Grant-in-aid for Creative Scientific Research 16GS0313 (to S. O.) and Grant-in-aid for Scientific Research on Priority Areas A-14082203 (to T. K.) from the Ministry of Education, Culture, Sports, 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.

The on-line version of this article (available at http://www.jbc.org) contains Supplemental Fig. 1.

To whom correspondence should be addressed: Dept. of Biological Chemistry, Graduate School of Pharmaceutical Sciences, Kyoto University, Shimoadachi-cho, Sankyo-ku, Kyoto 606-8501, Japan. Tel.: 81-75-753-4562; Fax: 81-75-753-4605; E-mail: shogo{at}pharm.kyoto-u.ac.jp.

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