J. Cell Biol., Volume 145, Number 4, May 17, 1999 899-910

Sulfotransferases of Two Specificities Function in the Reconstitution of High Endothelial Cell Ligands for L-selectin

Annette Bistrup,^* Sunil Bhakta,^¶ Jin Kyu Lee,^* Yevgeniy Y. Belov,^* Michael Dee Gunn, Feng-Rong Zuo,^¶ Chiao-Chain Huang, Reiji Kannagi,^§ Steven D. Rosen,^* and Stefan Hemmerich^¶

^* Department of Anatomy and Program in Immunology, and  Cardiovascular Research Institute, University of California, San Francisco, California 94143; ^§ Program in Experimental Pathology, Aichi Cancer Center, Nagoya, Japan;  Clontech Laboratories, Inc., Palo Alto, California 94303; and ^¶ Department of Respiratory Diseases, Roche Bioscience, Palo Alto, California 94304-1397

L-selectin, a lectin-like receptor, mediates rolling of lymphocytes on high endothelial venules (HEVs) in secondary lymphoid organs by interacting with HEV ligands. These ligands consist of a complex of sialomucins, candidates for which are glycosylation- dependent cell adhesion molecule 1 (GlyCAM-1), CD34, and podocalyxin. The ligands must be sialylated, fucosylated, and sulfated for optimal recognition by L-selectin. Our previous structural characterization of GlyCAM-1 has demonstrated two sulfation modifications, Gal-6-sulfate and GlcNAc-6-sulfate in the context of sialyl Lewis x. We now report the cloning of a Gal-6-sulfotransferase and a GlcNAc-6-sulfotransferase, which can modify GlyCAM-1 and CD34. The Gal-6-sulfotransferase shows a wide tissue distribution. In contrast, the GlcNAc-6-sulfotransferase is highly restricted to HEVs, as revealed by Northern analysis and in situ hybridization. Expression of either enzyme in Chinese hamster ovary cells, along with CD34 and fucosyltransferase VII, results in ligand activity, as detected by binding of an L-selectin/IgM chimera. When coexpressed, the two sulfotransferases synergize to produce strongly enhanced chimera binding.

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• Bhakta, S., Bartes, A., Bowman, K. G., Kao, W.-M., Polsky, I., Lee, J. K., Cook, B. N., Bruehl, R. E., Rosen, S. D., Bertozzi, C. R., Hemmerich, S. (2000). Sulfation of N-Acetylglucosamine by Chondroitin 6-Sulfotransferase 2 (GST-5). J. Biol. Chem. 275: 40226-40234 [Abstract] [Full Text]  
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• Gallego, R. G., Blanco, J. L. J., Zuylen, C. W. E. M. T.-v., Gotfredsen, C. H., Voshol, H., Duus, J. O., Schachner, M., Vliegenthart, J. F. G. (2001). Epitope Diversity of N-Glycans from Bovine Peripheral Myelin Glycoprotein P0 Revealed by Mass Spectrometry and Nano Probe Magic Angle Spinning 1H NMR Spectroscopy. J. Biol. Chem. 276: 30834-30844 [Abstract] [Full Text]  
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• Vanderplasschen, A., Markine-Goriaynoff, N., Lomonte, P., Suzuki, M., Hiraoka, N., Yeh, J.-C., Bureau, F., Willems, L., Thiry, E., Fukuda, M., Pastoret, P.-P. (2000). A multipotential beta -1,6-N-acetylglucosaminyl-transferase is encoded by bovine herpesvirus type 4. Proc. Natl. Acad. Sci. USA 97: 5756-5761 [Abstract] [Full Text]  

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