Surface alterations of P388 leukemia cells by 2-deoxy-D-glucose
| Autor: | Robert L. Dion, Marjorie W. Myers-Robfogel, Linda S. Cunningham, Vincent H. Bono, Alan C. Sartorelli, Zoe Nakos Canellakis |
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| Rok vydání: | 1979 |
| Předmět: |
Deoxyglucose
In Vitro Techniques Biochemistry chemistry.chemical_compound Mice Glycolipid Lectins Deoxy Sugars Animals Soybean agglutinin Cell Aggregation Pharmacology chemistry.chemical_classification Leukemia Experimental biology Cell Cycle Cell Membrane DNA Neoplasm Galactosyltransferases Molecular biology Cell aggregation Wheat germ agglutinin Sialyltransferases carbohydrates (lipids) Membrane glycoproteins chemistry Concanavalin A biology.protein Glycoprotein 2-Deoxy-D-glucose |
| Zdroj: | Biochemical pharmacology. 28(12) |
| ISSN: | 0006-2952 |
| Popis: | Treatment of P388 murine leukemia cells in vitro with relatively low concentrations of 2-deoxy- d -glucose results in altered plasma membrane architecture, as detected by an increase in the binding of and in the subsequent rate of cellular agglutination by concanavalin A. In contrast, binding of and agglutination by wheat germ agglutinin in 2-deoxy- d -glucose-treated cells are reduced, while these parameters are not changed when soybean agglutinin is employed. These effects of 2-deoxy- d -glucose on surface architecture are not due to partial synchrony of the cell population by the carbohydrate since the DNA content distribution profiles are not altered markedly. The changes detected in the surface membrane appear to be partially due to 2-deoxy- d -glucose incorporation into membrane glycoproteins and glycolipids; in support of this concept, 2-deoxy- d -glucose was found to compete with P388 cells for concanavalin A binding, but did not compete for the binding of either wheat germ or soybean agglutinins. CMP-sialic acid: glycoprotein sialyl transferase and UDP-galactose: glycoprotein galactosyl transferase activities, and the availability of acceptor glycoproteins were measured in 2-deoxy- d -glucose-treated cells. Exposure of cells to this agent decreased sialyl transferase activity and the availability of endogenous acceptor glycoprotein molecules for this enzyme, suggesting that the observed decrease in wheat germ agglutinin binding might be due to decreased sialylation of the cell surface. |
| Databáze: | OpenAIRE |
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