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- W2171403795 abstract "Intracerebral accumulation of amyloid-β (Aβ) leading to Aβ plaque formation, is the main hallmark of Alzheimer's disease and might be caused by defective Aβ-clearance. We previously found primary human astrocytes and microglia able to bind and ingest Aβ1-42 in vitro, which appeared to be limited by Aβ1-42 fibril formation. We now confirm that astrocytic Aβ-uptake depends on size and/or composition of Aβ-aggregates as astrocytes preferably take up oligomeric Aβ over fibrillar Aβ. Upon exposure to either fluorescence-labelled Aβ1-42 oligomers (Aβoligo) or fibrils (Aβfib), a larger (3.7 times more) proportion of astrocytes ingested oligomers compared to fibrils, as determined by flow cytometry. Aβ-internalization was verified using confocal microscopy and live-cell imaging. Neither uptake of Aβoligo nor Aβfib, triggered proinflammatory activation of the astrocytes, as judged by quantification of interleukin-6 and monocyte-chemoattractant protein-1 release. Amyloid-associated proteins, including α1-antichymotrypsin (ACT), serum amyloid P component (SAP), C1q and apolipoproteins E (ApoE) and J (ApoJ) were earlier found to influence Aβ-aggregation. Here, astrocytic uptake of Aβfib increased when added to the cells in combination with SAP and C1q (SAP/C1q), but was unchanged in the presence of ApoE, ApoJ and ACT. Interestingly, ApoJ and ApoE dramatically reduced the number of Aβoligo-positive astrocytes, whereas SAP/C1q slightly reduced Aβoligo uptake. Thus, amyloid-associated proteins, especially ApoJ and ApoE, can alter Aβ-uptake in vitro and hence may influence Aβ clearance and plaque formation in vivo. © 2010 Wiley-Liss, Inc." @default.
- W2171403795 created "2016-06-24" @default.
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- W2171403795 date "2010-05-05" @default.
- W2171403795 modified "2023-10-07" @default.
- W2171403795 title "Astrocytic Aβ1-42 uptake is determined by Aβ-aggregation state and the presence of amyloid-associated proteins" @default.
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- W2171403795 doi "https://doi.org/10.1002/glia.21004" @default.
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