Abstract
Cellular membrane alterations are commonly observed in many diseases, including Alzheimer's disease (AD). Membrane biophysical properties, such as membrane molecular order, membrane fluidity, organization of lipid rafts, and adhesion between membrane and cytoskeleton, play an important role in various cellular activities and functions. While membrane biophysics impacts a broad range of cellular pathways, this review addresses the role of membrane biophysics in amyloid-β peptide aggregation, Aβ-induced oxidative pathways, amyloid precursor protein processing, and cerebral endothelial functions in AD. Understanding the mechanism(s) underlying the effects of cell membrane properties on cellular processes should shed light on the development of new preventive and therapeutic strategies for this devastating disease.
Highlights
Alzheimer’s disease will claim 13.2 million Americans by 2050 if no preventive treatments are found
When amyloid-β peptide (Aβ) is incubated with lipid rafts acquired from rat neuronal cells, cholesterol affects the conversion of the α-helix conformation of Aβ to the β-sheet-rich structure, which is synonymous with toxicity (Zhao et al, 2011)
Another study indicated that treatment of PSwt-1 CHO cells with oleic acid and linoleic acid increased γ-secretase activity and Aβ production (Liu et al, 2004). These studies suggest that modulation of polyunsaturated fatty acids (PUFAs) content in cellular membrane is essential in regulating sAPPα production partially due to their effects on membrane fluidity
Summary
Alzheimer’s disease will claim 13.2 million Americans by 2050 if no preventive treatments are found. Recent studies provide strong evidence that cell membrane composition and cell biophysics play an important role in a number of pathophysiological events in AD (Hicks et al, 2012). Recent research findings show that the influences of membrane lipids and properties have been proven in many cellular pathways and processing implicated in AD, the role of altered lipid composition and membrane properties in the disease has yet to be fully elucidated. Another important area of research investigates which aggregated forms of amyloid-β peptide (Aβ) are involved in the pathogenesis of AD. We summarize the role of biophysical factors in Aβ aggregation and the effects of oxidative stress and Aβ on membrane biophysics, membrane biophysics on amyloid precursor protein (APP) processing, and membrane mechanics in altered endothelial functions and blood brain barrier (BBB)
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