We investigated whether the toxicity of oligomeric amyloid-beta peptide (Abeta1-42) upon differentiated human neuroblastoma SH-SY5Y cells, can be affected by changes of membrane lipid composition. An immunostaining technique, using lipids extracted from the cells and separated by thin layer chromatography, suggested that Abeta preferentially binds to phosphatidylethanolamine (PE), one of the major lipids in the cell extract. For this reason, we utilized treatments with putative inhibitors of phosphatidylethanolamine biosynthesis (choline, phosphocholine, R59949) to decrease its proportion in the cell membrane; choline treatment (2.5 mM, 24 h) showed the best performance, reducing phosphatidylethanolamine content from 5.7 to 3.3 μg phosphorous/mg protein. Either the extent of Abeta binding or its toxicity decreased onto choline-treated cells. These data may open the possibility to develop future strategies aiming to reduce Abeta toxicity in Alzheimer disease.

Cazzaniga, E., Bulbarelli, A., Lonati, E., Orlando, A., Re, F., Gregori, M., et al. (2011). Abeta peptide toxicity is reduced after treatments decreasing phosphatidylethanolamine content in differentiated neuroblastoma cells. NEUROCHEMICAL RESEARCH, 36(5), 863-869 [10.1007/s11064-011-0415-4].

Abeta peptide toxicity is reduced after treatments decreasing phosphatidylethanolamine content in differentiated neuroblastoma cells

CAZZANIGA, EMANUELA
;
BULBARELLI, ALESSANDRA;LONATI, ELENA RITA;ORLANDO, ANTONINA;RE, FRANCESCA;GREGORI, MARIA;MASSERINI, MASSIMO ERNESTO
2011

Abstract

We investigated whether the toxicity of oligomeric amyloid-beta peptide (Abeta1-42) upon differentiated human neuroblastoma SH-SY5Y cells, can be affected by changes of membrane lipid composition. An immunostaining technique, using lipids extracted from the cells and separated by thin layer chromatography, suggested that Abeta preferentially binds to phosphatidylethanolamine (PE), one of the major lipids in the cell extract. For this reason, we utilized treatments with putative inhibitors of phosphatidylethanolamine biosynthesis (choline, phosphocholine, R59949) to decrease its proportion in the cell membrane; choline treatment (2.5 mM, 24 h) showed the best performance, reducing phosphatidylethanolamine content from 5.7 to 3.3 μg phosphorous/mg protein. Either the extent of Abeta binding or its toxicity decreased onto choline-treated cells. These data may open the possibility to develop future strategies aiming to reduce Abeta toxicity in Alzheimer disease.
Articolo in rivista - Articolo scientifico
Amyloid-beta peptide (1-42); Neuroblastoma SH-SY5Y; Phosphatidylcholine; Phosphatidylethanolamine
English
2011
36
5
863
869
none
Cazzaniga, E., Bulbarelli, A., Lonati, E., Orlando, A., Re, F., Gregori, M., et al. (2011). Abeta peptide toxicity is reduced after treatments decreasing phosphatidylethanolamine content in differentiated neuroblastoma cells. NEUROCHEMICAL RESEARCH, 36(5), 863-869 [10.1007/s11064-011-0415-4].
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/10281/21957
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