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J Biol Chem, Vol. 273, Issue 18, 11205-11211, May 1, 1998
From the 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.
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
,,, and 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
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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