a(MESH:Caspases)
Cleavage of APP by caspases may also contribute to AD pathologies PubMed:21214928
Cleavage of APP by caspases may also contribute to AD pathologies PubMed:21214928
It is also possible that APP betaCTF’s cytotoxic effect is actually mediated by the end products of gamma- and/or caspase-cleavage including APP intracellular domain (AICD), C31 and Jcasp which are cytotoxic (see below) PubMed:21214928
In addition to secretases, caspases (predominantly caspase- 3) can directly cleave APP at position Asp664 (based on the APP695 sequence) within the cytoplasmic tail during apoptosis to release a fragment containing the last 31 amino acids of APP (called C31) PubMed:21214928
Additional gamma-cleavage further generates the fragment (called Jcasp) containing the region between gamma- and caspase-cleavage sites PubMed:21214928
In addition to cleavages involving secretases, APP can be cleaved by caspases independently at its C terminus (Asp664 of APP695), releasing a short tail containing the last 31 amino acids (C31) of APP and a fragment (Jcasp) from between the gamma- and caspase-cleavage sites (Lu et al. 2000) PubMed:22122372
Truncation of Tau by caspases and endopeptidases has been suggested to constitute an important pathogenic step in AD PubMed:29215007
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