p(FPLX:Caspase)

Entity

Name

Caspase

Namespace

FPLX

Namespace Version

20180917

Namespace URL

https://raw.githubusercontent.com/sorgerlab/famplex/e8ae9926ff95266032cb74f77973c84939bffbeb/export/famplex.belns

A study in cultured mouse neuroblastoma cells showed that N-terminal mutant Huntingtin inhibited the 20S proteasome catalytic activity, in turn causing impaired proteasomal degradation of p53, subsequent loss of mitochondrial membrane potential, release of cytochrome c, caspase activation, and apoptosis (Jana et al., 2001) (Figure 2). PubMed:14556719

Recent data suggest that caspases are involved in the accumulation of tau pathology [10, 25, 26], and reductions in CHIP have been shown to cause caspase activation and increased caspase-cleaved tau levels [19]. PubMed:25374103

These results indicate that CHIP is involved in degradation of caspases and caspase-cleaved tau. PubMed:25374103

Recent data suggest that caspases are involved in the accumulation of tau pathology [10, 25, 26], and reductions in CHIP have been shown to cause caspase activation and increased caspase-cleaved tau levels [19]. PubMed:25374103

Human brain tau can be degraded by the proteases, such as cathepsin-D, amino peptidases, human high temperature requirement serine protease A1 (HTRA1), thrombin, caspases, and calpains (Chesser et al. 2013; Kenessey et al. 1997) PubMed:29626319

It has been reported that tau is degraded by several major cellular degradation systems, including calpain, caspases, lysosomes, and proteasomes. PubMed:22908190

Recent data suggest that caspases are involved in the accumulation of tau pathology [10, 25, 26], and reductions in CHIP have been shown to cause caspase activation and increased caspase-cleaved tau levels [19]. PubMed:25374103

Recent data suggest that caspases are involved in the accumulation of tau pathology [10, 25, 26], and reductions in CHIP have been shown to cause caspase activation and increased caspase-cleaved tau levels [19]. PubMed:25374103

This fragment was proposed to be generated by caspases (although not caspase 3). PubMed:26631930