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J Biol Chem, Vol. 273, Issue 18, 11205-11211, May 1, 1998

Galectin-1 Is a Major Receptor for Ganglioside GM₁, a Product of the Growth-controlling Activity of a Cell Surface Ganglioside Sialidase, on Human Neuroblastoma Cells in Culture

Jürgen Kopitz, Carolina von Reitzenstein, Maria Burchert^§, Michael Cantz, and Hans-Joachim Gabius^§

From the  Institut für Pathochemie und Neurochemie, Klinikum der Ruprecht-Karls-Universität, Im Neuenheimer Feld 220, D-69120 Heidelberg, Germany and the ^§ Institut für Physiologische Chemie, Tierärztliche Fakultät, Ludwig-Maximilians-Universität, Veterinärstrasse 13, D-80539 München, Germany

Cell density-dependent inhibition of growth and neural differentiation in the human neuroblastoma cell line SK-N-MC are associated with a ganglioside sialidase-mediated increase of GM₁ and lactosylceramide at the cell surface. Because these glycolipids expose galactose residues, we have initiated the study of the potential role of galectins in such cellular events. Using specific antibodies, galectin-1 but not galectin-3 was found to be present at the cell surface. Assessment of carbohydrate-dependent binding revealed a saturable amount of ligand sites approaching 2.6 × 10⁶ galectin-1 molecules bound/cell. Presence during cell culture of the sialidase inhibitor 2-deoxy-2,3-dehydro-N-acetylneuraminic acid or of the GM₁-binding cholera toxin B subunit effected a decrease of the presentation of galectin-1 ligands by 30-50%. The assumption that GM₁ is a major ligand for galectin-1 was reinforced by the correlation between the number of carbohydrate-dependent ¹²⁵I-iodinated GM₁-neoganglioprotein binding sites and the amount of immunoreactive surface galectin-1, the marked sensitivity of probe binding to the presence of anti-galectin-1 antibody, and the inhibition of cell adhesion to surface-immobilized GM₁ by the antibody. The results open the possibility that the carbohydrate-dependent interaction between ganglioside GM₁ and galectin-1 may relay sialidase-dependent alterations in this cell system.

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Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.

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