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- W2085498526 abstract "Amyloidoses constitute a group of diseases in which soluble proteins aggregate and deposit extracellularly in tissues. Nonhereditary apolipoprotein A-I (apoA-I) amyloid is characterized by deposits of nonvariant protein in atherosclerotic arteries. Despite being common, little is known about the pathogenesis and significance of apoA-I deposition. In this work we investigated by fluorescence and biochemical approaches the impact of a cellular microenvironment associated with chronic inflammation on the folding and pro-amyloidogenic processing of apoA-I. Results showed that mildly acidic pH promotes misfolding, aggregation, and increased binding of apoA-I to extracellular matrix elements, thus favoring protein deposition as amyloid like-complexes. In addition, activated neutrophils and oxidative/proteolytic cleavage of the protein give rise to pro amyloidogenic products. We conclude that, even though apoA-I is not inherently amyloidogenic, it may produce non hereditary amyloidosis as a consequence of the pro-inflammatory microenvironment associated to atherogenesis." @default.
- W2085498526 created "2016-06-24" @default.
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- W2085498526 date "2011-07-19" @default.
- W2085498526 modified "2023-10-07" @default.
- W2085498526 title "Human Apolipoprotein A-I-Derived Amyloid: Its Association with Atherosclerosis" @default.
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- W2085498526 doi "https://doi.org/10.1371/journal.pone.0022532" @default.
- W2085498526 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3139661" @default.
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