PMID: 9653771Jul 8, 1998Paper

Cationic lipids (lipofectamine) and disturbance of cellular cholesterol and sphingomyelin distribution modulates gamma-secretase activity within amyloid precursor protein in vitro

Prostaglandins & Other Lipid Mediators
B UrmoneitT Dyrks

Abstract

To study beta-amyloid protein generation we expressed different amyloid precursor protein (APP) isoforms in the human neuroblastoma cell line SY5Y (for details see (1)). Treatment with lipofectamine, an cationic lipid for eucaryotic cell transfection, inhibits gamma-secretase activity and stimulates the physiological APP cleavage by alpha-secretase activity. Beside the MDL inhibitor (2), this is the second agent that shows modulation of gamma-secretase activity in vitro. Further, we show that disturbance of cellular cholesterol and sphingomyelin distribution in transfected SY5Y cells results in an overproduction of beta-amyloid protein. This provides experimental evidence that membrane instability influenced the proteolytic activity of gamma-secretase within the APP molecule.

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Citations

Jun 7, 2005·Experimental Brain Research·Kina HöglundKaj Blennow
Aug 25, 2007·Pharmacology & Therapeutics·Mark A Findeis
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Jun 15, 2019·International Journal of Environmental Research and Public Health·Syena SarrafpourAlfred Fonteh

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