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Originally published In Press as doi:10.1074/jbc.M105135200 on July 12, 2001

J. Biol. Chem., Vol. 276, Issue 38, 35917-35923, September 21, 2001
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Negative Regulation of Neuroblastoma Cell Growth by Carbohydrate-dependent Surface Binding of Galectin-1 and Functional Divergence from Galectin-3*

Jürgen KopitzDagger , Carolina von ReitzensteinDagger , Sabine André§, Herbert Kaltner§, Johannes UhlDagger , Volker Ehemann, Michael CantzDagger ||, and Hans-Joachim Gabius§

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

The cell density-dependent growth inhibition of human SK-N-MC neuroblastoma cells is initiated by increased ganglioside sialidase activity leading to elevated cell surface presentation of ganglioside GM1, a ligand of galectin-1. We herein show that the extent of the cell surface expression of the galectin coincides with marked increases of the sialidase activity. Reverse transcriptase-polymerase chain reaction analysis excludes a regulation at the transcriptional level. Exposure of cells to purified galectin-1 reveals its carbohydrate-dependent activity to reduce cell proliferation. Assays to detect DNA fragmentation biochemically and cytometrically and to block caspases render it unlikely that galectin-1 acts as a classical proapoptotic factor on these cells. Because the chimeric galectin-3 shares binding sites and binding parameters with galectin-1 for these cells, we tested whether this galectin will elicit the same response as the homodimeric cross-linking galectin-1. Evidently, galectin-3 fails to affect cell growth by itself but interferes with galectin-1 upon coincubation. Its proteolytically truncated variant, the C-terminal lectin domain with impaired capacity to form aggregates when surface bound, has only weak binding properties. Thus, the way in which the galectin-1 interacts topologically with an apparently common set of ligands relative to galectin-3 is crucial for eliciting post-binding events. We conclude that galectin-1 is a probable effector in the sialidase-dependent growth control in this system. Moreover, the experiments with galectin-3 reveal functional divergence, most probably based on different topologies of presentation of homologous carbohydrate-binding sites.

* This work was supported by funds from the Wilhelm Sander-Stiftung (Munich) (to H.-J. G.).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: University of Heidelberg, Inst. für Pathochemie und Neurochemie, Im Neuenheimer Feld 220, D-69120 Heidelberg, Germany. Fax: 49-6221-564228; E-mail: michael_cantz@med.uni-heidelberg.de.

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