Apolipoprotein E: Structural and Functional Interactions with Amyloid β

Stine, W. Blaine; LaDu, Mary Jo

doi:10.1002/9783527619344.ch10

Cited by 1 publication

(1 citation statement)

References 239 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…These later oligomers induce much higher levels of reactive oxygen species (ROS) in cells than do earlier oligomers [14]. While focusing on Aβ aggregation, these oligomers interact with lipid membrane surfaces through weak electrostatic interactions that promote conformational transition from α-helix structures to β-sheet conformations [15]. Moreover, it has been observed that Aβ alters membrane phospholipid fluidity through its own insertion into lipid bilayers [16].…”

Section: Introductionmentioning

confidence: 99%

Seeding and Growth of β-Amyloid Aggregates upon Interaction with Neuronal Cell Membranes

Ruiz-Arias

Paredes

Biase

et al. 2020

IJMS

View full text Add to dashboard Cite

In recent years, the prevalence of amyloid neurodegenerative diseases such as Alzheimer’s disease (AD) has significantly increased in developed countries due to increased life expectancy. This amyloid disease is characterized by the presence of accumulations and deposits of β-amyloid peptide (Aβ) in neuronal tissue, leading to the formation of oligomers, fibers, and plaques. First, oligomeric intermediates that arise during the aggregation process are currently thought to be primarily responsible for cytotoxicity in cells. This work aims to provide further insights into the mechanisms of cytotoxicity by studying the interaction of Aβ aggregates with Neuro-2a (N2a) neuronal cells and the effects caused by this interaction. For this purpose, we have exploited the advantages of advanced, multidimensional fluorescence microscopy techniques to determine whether different types of Aβ are involved in higher rates of cellular toxicity, and we measured the cellular stress caused by such aggregates by using a fluorogenic intracellular biothiol sensor. Stress provoked by the peptide is evident by N2a cells generating high levels of biothiols as a defense mechanism. In our study, we demonstrate that Aβ aggregates act as seeds for aggregate growth upon interacting with the cellular membrane, which results in cell permeability and damage and induces lysis. In parallel, these damaged cells undergo a significant increase in intracellular biothiol levels.

show abstract

Section: Introductionmentioning

confidence: 99%