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- W1991666023 abstract "We describe the inhibitory effect of full-length Aβ(1–42) and Aβ(25–35) fragment of amyloid-β peptide on phosphatidylcholine (PtdCho) metabolism in bovine retina capillary pericytes. Cell cultures were incubated with Aβs for 24 h. Peroxidation indices (malondialdehyde and lactate dehydrogenase release) significantly increased after 20–50 μM Aβ(1–42) or Aβ(25–35) treatment. In addition, [Me-3H]choline incorporation into PtdCho strongly decreased while either 3H-choline or 14C-arachidonic acid release from prelabeled cells increased, indicating PtdCho hydrolysis. The effect was very likely due to prooxidant action of both Aβ peptides. Reversed-sequence Aβ(35–25) peptide did not depress 3H-choline incorporation nor stimulate PtdCho breakdown. With addition of Aβs at low concentrations (2–20 μM) to pericytes, marked ultrastructural changes, well connected to metabolic alterations, emerged including shrinkage of cell bodies, retraction of processes, disruption of the intracellular actin network. Cells treated with higher concentrations (50–200 μM) displayed characteristics of necrotic cell death. The data suggest that: (a) Aβ(1–42) and Aβ(25–35) peptides may modulate phospholipid turnover in microvessel pericytes; (b) together with endothelial cells, pericytes could be the target of vascular damage during processes involving amyloid accumulation." @default.
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- W1991666023 date "2001-05-01" @default.
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- W1991666023 title "Amyloid β(1–42) and its β(25–35) fragment induce in vitro phosphatidylcholine hydrolysis in bovine retina capillary pericytes" @default.
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- W1991666023 doi "https://doi.org/10.1016/s0304-3940(01)01749-9" @default.
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