2001
DOI: 10.1016/s0006-8993(00)03322-9
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Acidic pH promotes the formation of toxic fibrils from β-amyloid peptide

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Cited by 121 publications
(100 citation statements)
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“…It has been suggested that the acidic lysosomal environment can promote formation of Aβ oligomers and protofibrils 39 and that intralysosomally accumulated Aβ damages lysosomal membranes, resulting in the leak of acid hydrolases into the cytosol and apoptotic death as described in our previous study. 34 In support of these results, we showed that the prevention of intralysosomal Aβ (Aβ 1-42 and oligomeric Aβ) accumulation by macroautophagy inhibition rescued the cells.…”
Section: Discussionsupporting
confidence: 60%
See 1 more Smart Citation
“…It has been suggested that the acidic lysosomal environment can promote formation of Aβ oligomers and protofibrils 39 and that intralysosomally accumulated Aβ damages lysosomal membranes, resulting in the leak of acid hydrolases into the cytosol and apoptotic death as described in our previous study. 34 In support of these results, we showed that the prevention of intralysosomal Aβ (Aβ 1-42 and oligomeric Aβ) accumulation by macroautophagy inhibition rescued the cells.…”
Section: Discussionsupporting
confidence: 60%
“…Aβ aggregation is pH-dependent, and oligomerization seems to be more rapid at a low pH. 39 To investigate if Aβ oligomerization takes place inside the lysosomes, or if Aβ oligomers are delivered through autophagy, we increased lysosomal pH with NH 4 Cl and exposed cells to hyperoxia for 3 d. No significant changes in the number of cells with Aβ oligomer-containing lysosomes were found after NH 4 Cl treatment, although a slight decrease (approximately 10%) was noted. These results suggest that, under hyperoxia, the majority of intralysosomal Aβ oligomers were taken up through autophagic pathway.…”
Section: Resultsmentioning
confidence: 99%
“…Molecular dynamic simulations have been employed to study the mechanism of how these mitigators interact and disassemble fibrils (80,83,84). Recently, Yassmine et al showed through simulation the disassembly of Aβ [16][17][18][19][20][21][22] protofibrils by N-methylated inhibitors (85). They reported that Nmethylated inhibitors interact with the protofibril by both lateral and longitudinal association, thereby disrupting the β-sheet extension and its lateral association into layers.…”
Section: Discussionmentioning
confidence: 99%
“…Aggregation Pathways-Amyloid fibril formation can be provoked by changes in solvent pH or polarity (53)(54)(55) and therefore may not reflect the ability to form such fibrils under normal physiological conditions. To ensure that the fibrils formed from mutant elastin-like polypeptides were not an artifact of the purification process (EP:K to Y), or a consequence only of heatinduced aggregation (EP:K to A), we assessed fibril formation under physiological conditions from an initial solution containing monomeric species.…”
Section: Mutant Elastin-like Polypeptides Have Multiple Possiblementioning
confidence: 99%