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Published on: September 10, 2018
Transferrin neutralization of amyloid beta 25-35 cytotoxicity
Sergio Giunta1, Roberta Galeazzi, M Beatrice Valli
1Laboratorio Analisi Chimico-Cliniche, Microbiologiche e Diagnostica Molecolare, Ospedale Geriatrico INRCA (IRCCS), via della Montagnola 81, 60100 Ancona, Italy. s.giunta@incra.it
Background:
Fibrillar aggregates of amyloid beta 25-35 (Abeta(25-35)) 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 Abeta(1-40/42) aggregates. Transferrin (TF) is investigated in this study.
Methods:
The Mattson red blood cells model was employed to determine whether co-incubation of transferrin and Abeta(25-35) prevented lysis. The formation of fibrillar Abeta(25-35) in the presence of transferrin was investigated using Congo red staining and spectrophotometric studies.
Results:
We found that incubation of 20 muM Abeta(25-35) with physiologic levels of transferrin prevented red blood cells lysis and the formation of macro-aggregates.
Conclusions:
These in vitro results suggest that transferrin may limit fibrillar beta amyloid formation in vivo and cytotoxicity.
