Oligosaccharide Portion of GM1 Enhances Process Formation by S20Y Neuroblastoma Cells

Schengrund, Cara Lynne; Prouty, Catherine

doi:10.1111/j.1471-4159.1988.tb04867.x

Cited by 26 publications

(21 citation statements)

References 29 publications

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“…60). However, the enhancement of neuritogenesis and cell adherence by the sugar portion of GM 1 has been tentatively ascribed to the presence of a 71-kDa membrane protein in the case of murine cholinergic S20Y neuroblastoma cells (61)(62)(63). Based on the application of the GM 1 -neoganglioprotein and the binding of cells to surfaceimmobilized GM 1 in the absence and presence of galectin-1-specific antibody, as well as the total number of immunologically assessed galectin-1 molecules and glycocytochemically quantitated neoganglioprotein-binding sites, it appears reasonable to conclude that the murine and the human lines differ in their GM 1 receptors.…”

Section: ϫ9mentioning

confidence: 99%

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

Kopitz

Reitzenstein

Burchert

et al. 1998

Journal of Biological Chemistry

262

196

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Cell density-dependent inhibition of growth and neural differentiation in the human neuroblastoma cell line SK-N-MC are associated with a ganglioside sialidasemediated increase of GM 1 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 carbohydratedependent binding revealed a saturable amount of ligand sites approaching 2.6 ؋ 10 6 galectin-1 molecules bound/cell. Presence during cell culture of the sialidase inhibitor 2-deoxy-2,3-dehydro-N-acetylneuraminic acid or of the GM 1 -binding cholera toxin B subunit effected a decrease of the presentation of galectin-1 ligands by 30 -50%. The assumption that GM 1 is a major ligand for galectin-1 was reinforced by the correlation between the number of carbohydrate-dependent 125 I-iodinated GM 1 -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 surfaceimmobilized GM 1 by the antibody. The results open the possibility that the carbohydrate-dependent interaction between ganglioside GM 1 and galectin-1 may relay sialidase-dependent alterations in this cell system.Gangliosides can exert a variety of cellular functions that include the triggering and modulation of transmembrane signaling and the mediation of recognition of receptor molecules in homotypic and heterotypic associations (1-4). Owing to this versatility in regulatory processes, it is fitting that the presentation of gangliosides at the cell surface is subject to control mechanisms that involve biosynthesis, endocytic uptake, recirculation, and lysosomal degradation (5, 6). Moreover, the structure of the oligosaccharide chains of gangliosides can be remodeled in situ by the action of a cell surface sialidase in the course of transformation, differentiation and cell contact formation (7-12). In human neuroblastoma cells (SK-N-MC), the activity of this sialidase was directed toward gangliosides with terminal sialic acids, yielding a shift from higher sialylated species to GM 1 and a conversion of GM 3 to lactosylceramide (13). Such alterations of the ganglioside profile are apparently of profound impact on the behavior of the neuroblastoma cells, because the selective inhibition of the ganglioside sialidase activity by 2-deoxy-2,3-dehydro-N-acetylneuraminic acid (NeuAc2en) 1 led to marked changes in cellular morphology, a complete release from contact inhibition of growth, and a loss of differentiation markers (14,15). Because the underlying molecular events are unknown, we have now addressed questions on the presence and nature of potential receptors for GM 1 and/or lactosylceramide that are generated by the action of the ganglioside sialidase on the surface of neuroblastoma cells.The current literature prompts inves...

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Section: ϫ9mentioning

confidence: 99%

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

Kopitz

Reitzenstein

Burchert

et al. 1998

Journal of Biological Chemistry

262

196

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“…Based on our previous observations (Schengrund and Prouty, 1988;Fueshko and Schengrund, 1990), we hypothesized that GM 1 -binding proteins were present on the surface of S20Y cells. For morphological studies, the aminated oligo-GM 1 was conjugated to iminobiotin, and its interaction with S20Y cells visualized using a streptavidin-alkaline phosphatase complex.…”

Section: Discussionmentioning

confidence: 97%

“…Studies have indicated that the ceramide portion of gangliosides is not essential for all functional interactions. In at least two instances, the addition of the free oligosaccharide moiety to neuroblastoma cells was found to evoke a similar neuritogenic response (Nakajima et al, 1986;Schengrund and Prouty, 1988). Ceramide is not recognized as part of the ligand per se by the toxin.…”

Section: Discussionmentioning

confidence: 99%

Identification of a GM1‐Binding Protein on the Surface of Murine Neuroblastoma Cells

Fueshko

Schengrund

1992

Journal of Neurochemistry

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S20Y murine neuroblastoma cells appear to express a protein component(s) able to adhere specifically to the oligosaccharide portion of GM1 (oligo-GM1). To identify proteins with which the oligo-GM1 becomes closely associated, a radiolabeled (125I), photoactivatable derivative of oligo-GM1 was prepared. This was accomplished by reductive amination of the glucosyl moiety of oligo-GM1 to 1-deoxy-1-aminoglucitol, followed by reaction of the amine with sulfosuccinimidyl 2-(p-azidosalicylamido)ethyl-1,3'-dithiopropionate (SASD). Crosslinking studies using the photoactivatable probe indicated that it came in close proximity to a protein with an apparent molecular mass of approximately 71 kDa. In competition experiments, as little as a 10-fold molar excess of oligo-GM1 resulted in a selective reduction in labeling of this protein; preincubation with a 200-fold molar excess of siayllactose was necessary to observe the same change in the labeling pattern, lending additional support to the hypothesis that the approximately 71-kDa protein specifically associates with oligo-GM1. Cell surface location of the oligo-GM1 binding protein was confirmed using subcellular fractionation and morphological analyses.

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“…The observation that the oligosaccharide portion of GM| could stimulate neuritogenesis by S20Y murine neuroblastoma cells [49] suggested that molecules able to recognize the oligosaccharide portion o f GM| (oIigo-GM|) Recently a glycosidase, sialidase (neur aminidase, N-acetylneuraminosyl glycohydrolase, EC 3.2.1.18), associated with myelin, was postulated to function in the formation Fig. 1.…”

Section: Evidence For Cell Surface Ganglioside-binding Moleculesmentioning

confidence: 99%

“…Addition of the oligosaccharide portion of GQib to GOTO and NB-1 human neuroblastoma cells main tained in vitro resulted in enhanced process formation [20]. Similarly, the oligosaccharide portion of GM) was found to enhance neuritogenesis by S20Y murine neuroblastoma cells [49]. These observations suggest that the morphological changes resulted from the oli gosaccharide portion of the ganglioside inter acting with a cell surface component, since it is unlikely that the free, negatively charged, oligosaccharides could readily cross the plas ma membrane.…”

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confidence: 99%

Evidence that Molecules on the Surface of One Cell Can Adhere to the Oligosaccharide Portion of Gangliosides on the Surface of Another Cell

Schengrund¹

1995

Neurosignals

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While there have been numerous reports concerning the possible role(s) of gangliosides in neuronal development and their efficacy, or lack thereof, as possible therapeutic agents for the treatment of neuronal injury, the molecular mechanisms by which they induce specific cellular effects are not well understood. This review presents evidence for the existence of cell surface molecules able to adhere to the oligosaccharide portion of specific gangliosides and describes methods employed for their study. The identification of such cell surface molecules permits the hypothesis that the binding of the oligosaccharide portion of the ganglioside by its cell surface receptor is responsible for initiating the intracellular reactions that lead to modified cell behavior.

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Oligosaccharide Portion of GM1 Enhances Process Formation by S20Y Neuroblastoma Cells

Cited by 26 publications

References 29 publications

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

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

Identification of a GM1‐Binding Protein on the Surface of Murine Neuroblastoma Cells

Evidence that Molecules on the Surface of One Cell Can Adhere to the Oligosaccharide Portion of Gangliosides on the Surface of Another Cell

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