Microglia convert aggregated amyloid-β into neurotoxic forms through the shedding of microvesicles

• Published in: Cell death and differentiation Vol. 21; no. 4; pp. 582 - 593
• Main Authors: Joshi, P, Turola, E, Ruiz, A, Bergami, A, Libera, D D, Benussi, L, Giussani, P, Magnani, G, Comi, G, Legname, G, Ghidoni, R, Furlan, R, Matteoli, M, Verderio, C
• Format: Journal Article
• Language: English
• Published: London Nature Publishing Group UK 01.04.2014; Nature Publishing Group
• Subjects: 631/378/1689/1283; 631/378/2596/1953; 692/420; Alzheimer Disease - metabolism; Alzheimer Disease - pathology; Amyloid beta-Peptides - chemistry; Amyloid beta-Peptides - toxicity; Animals; Apoptosis; Biochemistry; Biomedical and Life Sciences; Cell Biology; Cell Cycle Analysis; Cell Survival - drug effects; Cells, Cultured; Excitatory Amino Acid Antagonists - pharmacology; Female; Humans; Interleukin-1beta - metabolism; Life Sciences; Male; Microglia - drug effects; Microglia - metabolism; Neurons - cytology; Neurons - drug effects; Neurons - metabolism; Original Paper; Peptide Fragments - chemistry; Peptide Fragments - toxicity; PrPC Proteins - metabolism; Rats; Solubility; Stem Cells; Transport Vesicles - chemistry; Transport Vesicles - metabolism; Tumor Necrosis Factor-alpha - metabolism; Alzheimer’s disease; microglia; extracellular microvesicles; Abeta 1–42; bioactive lipids; prion protein

Alzheimer’s disease (AD) is characterized by extracellular amyloid- β (A β ) deposition, which activates microglia, induces neuroinflammation and drives neurodegeneration. Recent evidence indicates that soluble pre-fibrillar A β species, rather than insoluble fibrils, are the most toxic forms of A β...