The prion protein and cellular cholesterol homeostasis
Citation: Diomede L et al. The prion protein and cellular cholesterol homeostasis. Neurobiol Lipids Vol. 1, 3 (30 Nov 2002). Available at: http://neurobiologyoflipids.org/content/1/3/
Abstract: The amount of lipids in cell membranes seems to regulate the interaction of the prion protein with cells and the propagation of prions. We investigated how the synthetic human prion peptide PrP 106-126 affected the chemico-physical and biochemical properties of nerve and HL60 cells. PrP 106-126 rapidly increased cell membrane microviscosity, inhibited cellular cholesterol release and increased membrane cholesterol content. PrP also inhibited cellular 3-hydroxy-3-methylglutaryl-coenzyme A reductase activity. These findings indicate that PrP 106-126 alters cellular cholesterol homeostasis and may help clarify how changes in membrane lipid composition are involved in the progression of prion encephalopathies.
Authors: Luisa Diomede and colleagues
Authors Institution: Department of Molecular Biochemistry and Pharmacology and Department of Neurochemistry, Istituto di Ricerche Farmacologiche Mario Negri Via Eritrea 62, 20157 Milano, Italy; email: diomede[at]marionegri.it
Key words: Prion protein; PrP 106-126; 3-hydroxy-3-methylglutaryl-coenzyme A (HMG CoA) reductase; membrane fluidity; cell homeoviscosity; etiology; lipids; learning; memory; lipoprotein; receptor; LTP; neurodegeneration marker; oxidative stress; PHF NFT tau phosphorylation; phospholipids; synaptic plasticity; disease; therapy; nutrition; cytoskeleton; Down syndrome; prions; scrapie
Abstract: The amount of lipids in cell membranes seems to regulate the interaction of the prion protein with cells and the propagation of prions. We investigated how the synthetic human prion peptide PrP 106-126 affected the chemico-physical and biochemical properties of nerve and HL60 cells. PrP 106-126 rapidly increased cell membrane microviscosity, inhibited cellular cholesterol release and increased membrane cholesterol content. PrP also inhibited cellular 3-hydroxy-3-methylglutaryl-coenzyme A reductase activity. These findings indicate that PrP 106-126 alters cellular cholesterol homeostasis and may help clarify how changes in membrane lipid composition are involved in the progression of prion encephalopathies.
Authors: Luisa Diomede and colleagues
Authors Institution: Department of Molecular Biochemistry and Pharmacology and Department of Neurochemistry, Istituto di Ricerche Farmacologiche Mario Negri Via Eritrea 62, 20157 Milano, Italy; email: diomede[at]marionegri.it
Key words: Prion protein; PrP 106-126; 3-hydroxy-3-methylglutaryl-coenzyme A (HMG CoA) reductase; membrane fluidity; cell homeoviscosity; etiology; lipids; learning; memory; lipoprotein; receptor; LTP; neurodegeneration marker; oxidative stress; PHF NFT tau phosphorylation; phospholipids; synaptic plasticity; disease; therapy; nutrition; cytoskeleton; Down syndrome; prions; scrapie
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