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Involvement of caspases in proteolytic cleavage of Alzheimer's amyloid-beta precursor protein and amyloidogenic A beta peptide formation.

Cell | Apr 30, 1999

The amyloid-beta precursor protein (APP) is directly and efficiently cleaved by caspases during apoptosis, resulting in elevated amyloid-beta (A beta) peptide formation. The predominant site of caspase-mediated proteolysis is within the cytoplasmic tail of APP, and cleavage at this site occurs in hippocampal neurons in vivo following acute excitotoxic or ischemic brain injury. Caspase-3 is the predominant caspase involved in APP cleavage, consistent with its marked elevation in dying neurons of Alzheimer's disease brains and colocalization of its APP cleavage product with A beta in senile plaques. Caspases thus appear to play a dual role in proteolytic processing of APP and the resulting propensity for A beta peptide formation, as well as in the ultimate apoptotic death of neurons in Alzheimer's disease.

Pubmed ID: 10319819 RIS Download

Mesh terms: Acute Disease | Alzheimer Disease | Amyloid Precursor Protein Secretases | Amyloid beta-Peptides | Amyloid beta-Protein Precursor | Amyloidosis | Animals | Apoptosis | Aspartic Acid | Aspartic Acid Endopeptidases | Brain Diseases | Camptothecin | Caspase 3 | Caspases | Cysteine Proteinase Inhibitors | Endopeptidases | Enzyme Inhibitors | Enzyme Precursors | Excitatory Amino Acid Agonists | Hippocampus | Humans | In Situ Nick-End Labeling | Kainic Acid | Leukemia, Erythroblastic, Acute | Male | Mice | Mice, Inbred C57BL | Mutation | Neurons | Oligopeptides | Rabbits | Rats | Rats, Wistar | Sweden | Tumor Cells, Cultured