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Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Sci+Rep 2017 ; 7 (ä): ä Nephropedia Template TP
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Amyloid plaque structure and cell surface interactions of ?-amyloid fibrils revealed by electron tomography #MMPMID28240273
Han S; Kollmer M; Markx D; Claus S; Walther P; Fändrich M
Sci Rep 2017[]; 7 (ä): ä PMID28240273show ga
The deposition of amyloid fibrils as plaques is a key feature of several neurodegenerative diseases including in particular Alzheimer?s. This disease is characterized, if not provoked, by amyloid aggregates formed from A? peptide that deposit inside the brain or are toxic to neuronal cells. We here used scanning transmission electron microscopy (STEM) to determine the fibril network structure and interactions of A? fibrils within a cell culture model of Alzheimer?s disease. STEM images taken from the formed A? amyloid deposits revealed three main types of fibril network structures, termed amorphous meshwork, fibril bundle and amyloid star. All three were infiltrated by different types of lipid inclusions from small-sized exosome-like structures (50?100?nm diameter) to large-sized extracellular vesicles (up to 300?nm). The fibrils also presented strong interactions with the surrounding cells such that fibril bundles extended into tubular invaginations of the plasma membrane. Amyloid formation in the cell model was previously found to have an intracellular origin and we show here that it functionally destroys the integrity of the intracellular membranes as it leads to lysosomal leakage. These data provide a mechanistic link to explain why intracellular fibril formation is toxic to the cell.