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Alcohol and Alcoholism Advance Access published online on June 2, 2006
Alcohol and Alcoholism, doi:10.1093/alcalc/agl044
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© The Author 2006. Published by Oxford University Press on behalf of the Medical Council on Alcohol. All rights reserved
Received March 6, 2006
Revised April 28, 2006
Accepted May 4, 2006

Article

GLYCOSYLATION IS ALTERED BY ETHANOL IN RAT HIPPOCAMPAL CULTURED NEURONS

AITANA BRAZA-BOÏLS 1, MÓNICA TOMÁS 1, MARÍA PILAR MARÍN 1, LUIS MEGÍAS 2, MARÍA SANCHO-TELLO 1, EUGENIO FORNAS 1, and JAIME RENAU-PIQUERAS 1 *

1 Section of Cell Biology and Pathology, Center for Investigation, Hospital La Fe, Valencia, Spain
2 Department of Human Anatomy and Embryology. University of Granada, Spain

* To whom correspondence should be addressed.
JAIME RENAU-PIQUERAS, E-mail: renau_jai{at}gva.es


  Abstract

Aims: Glycoproteins, such as adhesion molecules and growth factors, participate in the regulation of nervous system development. Ethanol affects the synthesis, intracellular transport, distribution, and secretion of N-glycoproteins in different cell types, including astrocytes and hepatocytes, suggesting alterations in the glycosylation process. We analysed the effect of exposure to low doses of ethanol (30 mm, 7 days) on glycosylation in cultured hippocampal neurons. Methods: Neurons were incubated for short (5 min) and long (90 min) periods with the radioactively labelled carbohydrate precursors 2-deoxy-glucose, N-acetyl-D-mannosamine and mannose. The uptake and metabolism of these precursors, as well as the radioactivity distribution in protein gels, were analysed. The levels of the glucose transporters GLUT1 and GLUT3 were also determined. Results: Ethanol exposure reduces the synthesis of proteins, DNA and RNA and decreased the uptake of mannose, but not of 2-deoxy-glucose and N-acetyl-D-mannosamine, and it increased the protein levels of both glucose transporters. Moreover, it altered the carbohydrate moiety of several proteins. Finally, alcohol treatment results in an increment of cell surface glycoconjugates containing terminal non-reduced mannose. Conclusions: Alcohol-induced alterations in glycosylation of proteins in neurons could be a key mechanism involved in the teratogenic effects of alcohol exposure on brain development.

The first two authors contributed equally to this study.
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