NDLI: Oxidized LDL lipids increase ß-amyloid production by SH-SY5Y cells through glutathione depletion and lipid raft formation.

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Oxidized LDL lipids increase ß-amyloid production by SH-SY5Y cells through glutathione depletion and lipid raft formation.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Dias, Irundika H. K. Mistry, Jayna Fell, Shaun Reis, Ana Spickett, Corinne M. Polidori, Maria C. Lip, Gregory Y. H. Griffiths, Helen R.
Description	Country affiliation: United kingdom Author Affiliation: Dias IH ( Life and Health Sciences and Aston Research Centre for Healthy Ageing, Aston University, Birmingham, West Midlands B4 7ET, UK.); Mistry J ( Life and Health Sciences and Aston Research Centre for Healthy Ageing, Aston University, Birmingham, West Midlands B4 7ET, UK.); Fell S ( Life and Health Sciences and Aston Research Centre for Healthy Ageing, Aston University, Birmingham, West Midlands B4 7ET, UK.); Reis A ( Life and Health Sciences and Aston Research Centre for Healthy Ageing, Aston University, Birmingham, West Midlands B4 7ET, UK.); Spickett CM ( Life and Health Sciences and Aston Research Centre for Healthy Ageing, Aston University, Birmingham, West Midlands B4 7ET, UK.); Polidori MC ( Institute of Geriatrics, University of Cologne, Cologne, Germany.); Lip GY ( Centre for Cardiovascular Sciences, City Hospital Birmingham, Birmingham B18 7QH, UK.); Griffiths HR ( Life and Health Sciences and Aston Research Centre for Healthy Ageing, Aston University, Birmingham, West Midlands B4 7ET, UK. Electronic address: helen.griffiths@aston.ac.uk.)
Abstract	Elevated total cholesterol in midlife has been associated with increased risk of dementia in later life. We have previously shown that low-density lipoprotein (LDL) is more oxidized in the plasma of dementia patients, although total cholesterol levels are not different from those of age-matched controls. ß-Amyloid (Aß) peptide, which accumulates in Alzheimer disease (AD), arises from the initial cleavage of amyloid precursor protein by ß-secretase-1 (BACE1). BACE1 activity is regulated by membrane lipids and raft formation. Given the evidence for altered lipid metabolism in AD, we have investigated a mechanism for enhanced Aß production by SH-SY5Y neuronal-like cells exposed to oxidized LDL (oxLDL). The viability of SH-SY5Y cells exposed to 4µg oxLDL and 25µM 27-hydroxycholesterol (27OH-C) was decreased significantly. Lipids, but not proteins, extracted from oxLDL were more cytotoxic than oxLDL. In parallel, the ratio of reduced glutathione (GSH) to oxidized glutathione was decreased at sublethal concentrations of lipids extracted from native and oxLDL. GSH loss was associated with an increase in acid sphingomyelinase (ASMase) activity and lipid raft formation, which could be inhibited by the ASMase inhibitor desipramine. 27OH-C and total lipids from LDL and oxLDL independently increased Aß production by SH-SY5Y cells, and Aß accumulation could be inhibited by desipramine and by N-acetylcysteine. These data suggest a mechanism whereby oxLDL lipids and 27OH-C can drive Aß production by GSH depletion, ASMase-driven membrane remodeling, and BACE1 activation in neuronal cells.
File Format	HTM / HTML
ISSN	08915849
e-ISSN	18734596
DOI	10.1016/j.freeradbiomed.2014.07.012
Journal	Free Radical Biology and Medicine
Volume Number	75
Language	English
Publisher	Elsevier
Publisher Date	2014-10-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Discipline Free radicals biology Amyloid Beta-peptides Biosynthesis Cholesterol, Ldl Metabolism Glutathione Lipoproteins, Ldl Pharmacology Membrane Microdomains Acetylcysteine Alzheimer Disease Pathology Amyloid Precursor Protein Secretases Secretion Aspartic Acid Endopeptidases Cell Line, Tumor Cell Survival Drug Effects Desipramine Enzyme Activation Enzyme Inhibitors Free Radical Scavengers Chemistry Glutathione Disulfide Hydroxycholesterols Lipid Metabolism Blood Oxidation-reduction Sphingomyelin Phosphodiesterase Antagonists & Inhibitors Research Support, Non-u.s. Gov't
Content Type	Text
Resource Type	Article
Subject	Physiology (medical) Biochemistry

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