Fas Apoptosis Inhibitory Molecule Blocks and Dissolves Pathological Amyloid-β Species

A number of neurodegenerative diseases are associated with the accumulation of misfolded proteins, including Alzheimer's disease (AD). In AD, misfolded proteins such as tau and amyloid-beta (A beta) form pathological insoluble deposits. It is hypothesized that molecules capable of dissolving such protein aggregates might reverse disease progression and improve the lives of afflicted AD patients. Here we report new functions of the highly conserved mammalian protein, Fas Apoptosis Inhibitory Molecule (FAIM). We found that FAIM-deficient Neuro 2A cells accumulate A beta oligomers/fibrils. We further found that recombinant human FAIM prevents the generation of pathologic A beta oligomers and fibrils in a cell-free system, suggesting that FAIM functions without any additional cellular components. More importantly, recombinant human FAIM disaggregates and solubilizes established A beta fibrils. Our results identify a previously unknown, completely novel candidate for understanding and treating irremediable, irreversible, and unrelenting neurodegenerative diseases.

Automated summary

Research has revealed that the mammalian protein FAIM plays a crucial role in preventing and dissolving A beta fibrils in Alzheimer's disease, offering a promising new approach for treating neurodegenerative diseases.