Transferrin neutralization of amyloid beta 25-35 cytotoxicity.
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.
Giunta
Sergio
S
Laboratorio Analisi Chimico-Cliniche, Microbiologiche e Diagnostica Molecolare, Ospedale Geriatrico INRCA (IRCCS), via della Montagnola 81, 60100 Ancona, Italy. s.giunta@incra.it
Galeazzi
Roberta
R
Valli
M Beatrice
MB
Corder
Elizabeth H
EH
Galeazzi
Luciano
L
D000293:Adolescent; D000328:Adult; D000544:Alzheimer Disease / Q000378:metabolism*; D016229:Amyloid beta-Peptides / Q000378:metabolism / Q000633:toxicity*; D003224:Congo Red; D004347:Drug Interactions; D004912:Erythrocytes / Q000187:drug effects* / Q000378:metabolism; D006461:Hemolysis / Q000187:drug effects; D006801:Humans; D010446:Peptide Fragments / Q000378:metabolism / Q000633:toxicity*; D013053:Spectrophotometry; D014168:Transferrin / Q000494:pharmacology*
D016229:Amyloid beta-Peptides; D010446:Peptide Fragments; D014168:Transferrin; C074636:amyloid beta-protein (25-35); D003224:Congo Red