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

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 terminu...

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Veröffentlicht in:Nature medicine 2000-04, Vol.6 (4), p.397
Hauptverfasser: Lu, Daniel C, Rabizadeh, Shahrooz, Chandra, Sreeganga, Shayya, Rana F, Ellerby, Lisa M, Ye, Xin, Salvesen, Guy S, Koo, Edward H, Bredesen, Dale E
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Sprache:eng
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Zusammenfassung: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.
ISSN:1078-8956
1546-170X
DOI:10.1038/74656