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- W2047079596 abstract "Fibrillar aggregates of amyloid β 25–35 (Aβ25–35) form rapidly in vitro able to lyse human red blood cells (RBCs). Human sera, albumin, and apolipoprotein E (ApoE) each limit fibrillation and cytotoxicity. Potentially, these substances protect neurons from Aβ1–40/42 aggregates. Transferrin (TF) is investigated in this study. The Mattson red blood cells model was employed to determine whether co-incubation of transferrin and Aβ25–35 prevented lysis. The formation of fibrillar Aβ25–35 in the presence of transferrin was investigated using Congo red staining and spectrophotometric studies. We found that incubation of 20 μM Aβ25–35 with physiologic levels of transferrin prevented red blood cells lysis and the formation of macro-aggregates. These in vitro results suggest that transferrin may limit fibrillar β amyloid formation in vivo and cytotoxicity." @default.
- W2047079596 created "2016-06-24" @default.
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- W2047079596 date "2004-12-01" @default.
- W2047079596 modified "2023-10-15" @default.
- W2047079596 title "Transferrin neutralization of amyloid β 25–35 cytotoxicity" @default.
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- W2047079596 doi "https://doi.org/10.1016/j.cccn.2004.07.025" @default.
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