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Originally published In Press as doi:10.1074/jbc.M009995200 on February 15, 2001

J. Biol. Chem., Vol. 276, Issue 19, 16271-16278, May 11, 2001
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Human Corneal GlcNAc 6-O-Sulfotransferase and Mouse Intestinal GlcNAc 6-O-Sulfotransferase Both Produce Keratan Sulfate*

Tomoya O. Akama, Jun NakayamaDagger , Kohji Nishida§, Nobuyoshi Hiraoka, Misa Suzuki, Joseph McAuliffe, Ole Hindsgaul, Minoru Fukuda, and Michiko N. Fukuda

From the Glycobiology Program, The Burnham Institute, La Jolla, California 92037, the Dagger  Institute of Organ Transplants, Reconstructive Medicine, and Tissue Engineering, Shinshu University Graduate School of Medicine, Matsumoto 390-8621, Japan, and the § Department of Ophthalmology, Osaka University Medical School, Osaka 565-0871, Japan

Human corneal N-acetylglucosamine 6-O-sulfotransferase (hCGn6ST) has been identified by the positional candidate approach as the gene responsible for macular corneal dystrophy (MCD). Because of its high homology to carbohydrate sulfotransferases and the presence of mutations of this gene in MCD patients who lack sulfated keratan sulfate in the cornea and serum, hCGn6ST protein is thought to be a sulfotransferase that catalyzes sulfation of GlcNAc in keratan sulfate. In this report, we analyzed the enzymatic activity of hCGn6ST by expressing it in cultured cells. A lysate prepared from HeLa cells transfected with an intact form of hCGn6ST cDNA or culture medium from cells transfected with a secreted form of hCGn6ST cDNA showed an activity of transferring sulfate to C-6 of GlcNAc of synthetic oligosaccharide substrates in vitro. When hCGn6ST was expressed together with human keratan sulfate Gal-6-sulfotransferase (hKSG6ST), HeLa cells produced highly sulfated carbohydrate detected by an anti-keratan sulfate antibody 5D4. These results indicate that hCGn6ST transfers sulfate to C-6 of GlcNAc in keratan sulfate. Amino acid substitutions in hCGn6ST identical to changes resulting from missense mutations found in MCD patients abolished enzymatic activity. Moreover, mouse intestinal GlcNAc 6-O-sulfotransferase had the same activity as hCGn6ST. This observation suggests that mouse intestinal GlcNAc 6-O-sulfotransferase is the orthologue of hCGn6ST and functions as a sulfotransferase to produce keratan sulfate in the cornea.

* This work was supported by National Institutes of Health Grant CA71932 (to M. N. F.) and a Grant-in-aid for Scientific Research (10178104) from the Ministry of Education, Science, Sports, and Culture of Japan (J. N.).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

To whom correspondence should be addressed. Tel.: 858-646-3143; Fax: 858-646-3193; E-mail: michiko@burnham-inst.org.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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