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10.1074/jbc.M115.691840 http://scihub22266oqcxt.onion/10.1074/jbc.M115.691840 C5016693!5016693!27458018     free     free     free Deprecated: Implicit conversion from float 227.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 227.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 227.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 227.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       J+Biol+Chem 2016 ; 291 (37): 19590-606 Nephropedia Template TP {{tp|p=27458018|t=2016. Amyloid-?(1?42) Aggregation Initiates Its Cellular Uptake and Cytotoxicity * |pdf=|usr=}}{{27458018}} gab.com Text Amyloid- (1 42) Aggregation Initiates Its Cellular Uptake and Cytotoxicity * JO: J Biol Chem http://www.kidney.de/pget.php?&tw=1&pmid=27458018 #FOAvip The accumulation of amyloid ? peptide(1?42) (A?(1?42)) in extracellular plaques is one of the pathological hallmarks of Alzheimer disease (AD). Several studies have suggested that cellular reuptake of A?(1?42) may be a crucial step in its cytotoxicity, but the uptake mechanism is not yet understood. A? may be present in an aggregated form prior to cellular uptake. Alternatively, monomeric peptide may enter the endocytic pathway and conditions in the endocytic compartments may induce the aggregation process. Our study aims to answer the question whether aggregate formation is a prerequisite or a consequence of A? endocytosis. We visualized aggregate formation of fluorescently labeled A?(1?42) and tracked its internalization by human neuroblastoma cells and neurons. ?-Sheet-rich A?(1?42) aggregates entered the cells at low nanomolar concentration of A?(1?42). In contrast, monomer uptake faced a concentration threshold and occurred only at concentrations and time scales that allowed A?(1?42) aggregates to form. By uncoupling membrane binding from internalization, we found that A?(1?42) monomers bound rapidly to the plasma membrane and formed aggregates there. These structures were subsequently taken up and accumulated in endocytic vesicles. This process correlated with metabolic inhibition. Our data therefore imply that the formation of ?-sheet-rich aggregates is a prerequisite for A?(1?42) uptake and cytotoxicity. Twit Text FOAVip Amyloid- (1 42) Aggregation Initiates Its Cellular Uptake and Cytotoxicity * ????J Biol Chem http://www.kidney.de/pget.php?&tw=1&pmid=27458018 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=27458018 #FOAvip English Wikipedia <ref>{{Cite pmid|27458018}}</ref> Amyloid-?(1?42) Aggregation Initiates Its Cellular Uptake and Cytotoxicity * #MMPMID27458018 Jin S; Kedia N; Illes-Toth E; Haralampiev I; Prisner S; Herrmann A; Wanker EE; Bieschke J J Biol Chem 2016[Sep]; 291 (37): 19590-606 PMID27458018show ga The accumulation of amyloid ? peptide(1?42) (A?(1?42)) in extracellular plaques is one of the pathological hallmarks of Alzheimer disease (AD). Several studies have suggested that cellular reuptake of A?(1?42) may be a crucial step in its cytotoxicity, but the uptake mechanism is not yet understood. A? may be present in an aggregated form prior to cellular uptake. Alternatively, monomeric peptide may enter the endocytic pathway and conditions in the endocytic compartments may induce the aggregation process. Our study aims to answer the question whether aggregate formation is a prerequisite or a consequence of A? endocytosis. We visualized aggregate formation of fluorescently labeled A?(1?42) and tracked its internalization by human neuroblastoma cells and neurons. ?-Sheet-rich A?(1?42) aggregates entered the cells at low nanomolar concentration of A?(1?42). In contrast, monomer uptake faced a concentration threshold and occurred only at concentrations and time scales that allowed A?(1?42) aggregates to form. By uncoupling membrane binding from internalization, we found that A?(1?42) monomers bound rapidly to the plasma membrane and formed aggregates there. These structures were subsequently taken up and accumulated in endocytic vesicles. This process correlated with metabolic inhibition. Our data therefore imply that the formation of ?-sheet-rich aggregates is a prerequisite for A?(1?42) uptake and cytotoxicity. äAmyloid-?(1?42) Aggregation Initiates Its Cellular Uptake and Cytotoxi(epmc).pdf DeepDyve Pubget Overpricing