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Originally published In Press as doi:10.1074/jbc.M001117200 on March 20, 2000

J. Biol. Chem., Vol. 275, Issue 22, 16730-16737, June 2, 2000
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Expression of a Specific Glycosyltransferase Enzyme Regulates T Cell Death Mediated by Galectin-1*

Marisa GalvanDagger §, Shigeru Tsuboi, Minoru Fukuda, and Linda G. BaumDagger ||

From the Dagger  Department of Pathology and Laboratory Medicine, UCLA School of Medicine, Los Angeles, California 90095 and  The Glycobiology Program, The Burnham Institute, La Jolla, California 92037

Galectin-1 induces apoptosis of immature thymocytes and activated T cells, suggesting that galectin-1 regulates cell death in the thymus during selection and in the periphery following an immune response. Although it is known that galectin-1 recognizes lactosamine (Gal-GlcNAc) as a minimal ligand, this disaccharide is ubiquitously expressed on a variety of cell surface glycoproteins. Thus, susceptibility to galectin-1 may be regulated by the presentation of lactosamine on specific oligosaccharide structures created by specific glycosyltransferase enzymes. The core 2 beta -1,6-N-acetylglucosaminyltransferase (core 2 GnT) creates a branched structure on O-glycans that can be elongated to present multiple lactosamine sequences. In the thymus, the core 2 GnT is expressed in galectin-1-sensitive thymocyte subsets. In the periphery, an oligosaccharide epitope created by the core 2 GnT is expressed on galectin-1-sensitive activated T-cells. In this report, we demonstrate that expression of the core 2 GnT was necessary and sufficient for galectin-1-induced death of murine T cell lines. In addition, overexpression of the core 2 GnT in mice increased the susceptibility of double positive thymocytes to galectin-1. These data demonstrate that expression of a specific glycosyltransferase can control susceptibility to galectin-1, suggesting that developmentally regulated glycosyltransferase expression may be a mechanism to modulate cell death during T cell development and function.

* This work was supported in part by National Institutes of Health Grants R37CA33000 (to M. F.) and R01AI40118 (to L. G. B.), Grant RPG-97-049-01 from the American Cancer Society (to L. G. B.), and a Glycoscience Research Award from Neose Technologies (to L. G. B.). Work performed in the Flow Cytometry Core Laboratory was supported in part by the Jonsson Comprehensive Cancer Center Core Grant NIH-CA16042.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.

§ Supported by National Institutes of Health Grant CA09120-21.

|| To whom correspondence should be addressed: Dept. of Pathology and Laboratory Medicine, UCLA School of Medicine, 10833 Le Conte Ave., Los Angeles, CA 90095. Tel.: 310-206-5985; Fax: 310-206-0657; E-mail: lbaum@mednet.ucla.edu.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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