Cell death research shows promise for preventing Alzheimer’s

These Aβ aggregates interact directly with target cells and lead to cell death.

Antonio De Maio, a professor of surgery and neuroscience at the University of California, has been researching for the specific mechanisms behind Aβ-induced toxicity to cells, or cytoxicity.

Preserving cell viability

Cells exposed to stressful conditions respond by expressing heat shock proteins (hsps), whose job is to preserve cell viability. Hsp70, in particular, is a molecular chaperone that plays a major role in protein folding and the solubilisation of misfolded, aggregated polypeptide proteins inside cells.

The researchers were interested in Hsp70 because, according to De Maio, it has also been found outside of cells, potentially coexisting with Aβ peptides.

His team observed that HsP70 did, in fact, reduce oligomerisation of Aβ peptides.

Reduced oligomerisation of Aβ

Significantly, the researchers further inferred that the reduced oligomerisation of Aβ, where individual monomer molecules join to form a longer oligomer, might result in lower cellular toxicity, perhaps by blocking the assembly of Aβ ion channels. And in fact this is what they found, demonstrating a substantial reduction – approximately 70% – of Aβ peptide’s toxicity upon co-exposure to Hsp70.

While extremely promising at this stage, “more investigations of the interface between Hsp70 and Aβ peptides are necessary for any further developments,” De Maio said.