Mattson et al.9 demonstrated lysis of human red blood cells (RBC) exposed to amyloid peptide Aβ25-35, a new experimental model for amyloid-beta toxicity. Lysis resulted from pore formation in the RBC membranes and was completely prevented by concurrent exposure to Congo red. We demonstrate that human serum, purified ApoE from human plasma, and recombinant isoforms of ApoE neutralize the Aβ25-35 cytotoxicity: the E2 and E4 isoforms were marginally more effective than E3. Second, we demonstrate that Aβ25-35 forms fibrils in the reaction mixtures using electron-microscopy. Together these results suggest that the RBC model might be useful in preliminary identification of natural and synthetic substances able to protect against amyloid-beta cytotoxic effects due to fibrillar Aβ25-35. Such compounds would be candidate molecules for testing in neuronal systems.
|Number of pages||5|
|Publication status||Published - 2002|
- Apo E
- Red blood cells
ASJC Scopus subject areas
- Pathology and Forensic Medicine