Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

A second cytotoxic proteolytic peptide derived from amyloid beta-protein precursor.

Lu D.C., Rabizadeh S., Chandra S., Shayya R.F., Ellerby L.M., Ye X., Salvesen G.S., Koo E.H., Bredesen D.E.

The amyloid beta-protein precursor gives rise to the amyloid beta-protein, the principal constituent of senile plaques and a cytotoxic fragment involved in the pathogenesis of Alzheimer disease. Here we show that amyloid beta-protein precursor was proteolytically cleaved by caspases in the C terminus to generate a second unrelated peptide, called C31. The resultant C31 peptide was a potent inducer of apoptosis. Both caspase-cleaved amyloid beta-protein precursor and activated caspase-9 were present in brains of Alzheimer disease patients but not in control brains. These findings indicate the possibility that caspase cleavage of amyloid beta-protein precursor with the generation of C31 may be involved in the neuronal death associated with Alzheimer disease.

Nat. Med. 6:397-404(2000) [PubMed] [Europe PMC]