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- W2022982095 abstract "beta-Amyloid peptide (Abeta42) is the core protein of amyloid plaque in Alzheimer disease. The intracellular accumulation of Abeta42 in the endosomal/lysosomal system has been under investigation for many years, but the direct link between Abeta42 accumulation and dysfunction of the endosomal/lysosomal system is still largely unknown. Here, we found that both in vitro and in vivo, a major portion of Abeta42 was tightly inserted into and a small portion peripherally associated with the lysosomal membrane, whereas its soluble portion was minimal. We also found that the Abeta42 molecules inserted into the membrane tended to form multiple oligomeric aggregates, whereas Abeta40 peptides formed only dimers. Neutralizing lysosomal pH in differentiated PC12 cells decreased the lysosomal membrane insertion of Abeta42 and moderated Abeta42-induced lysosomal labilization and cytotoxicity. Our findings, thus, suggest that the membrane-inserted portion of Abeta42 accumulated in lysosomes may destabilize the lysosomal membrane and induce neurotoxicity." @default.
- W2022982095 created "2016-06-24" @default.
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- W2022982095 date "2010-06-01" @default.
- W2022982095 modified "2023-10-17" @default.
- W2022982095 title "Membrane Localization of β-Amyloid 1–42 in Lysosomes" @default.
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- W2022982095 doi "https://doi.org/10.1074/jbc.m109.036798" @default.
- W2022982095 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2888410" @default.
- W2022982095 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/20430896" @default.
- W2022982095 hasPublicationYear "2010" @default.
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