Literature summary extracted from
Lee, J.O.; Kim, J.Y.; Rhee, D.K.; Pyo, S.
Streptococcus pneumoniae ClpP protease induces apoptosis via caspase-independent pathway in human neuroblastoma cells: cytoplasmic relocalization of p53 (2013), Toxicon, 70, 142-152.
Application
EC Number |
Application |
Comment |
Organism |
---|
3.4.21.92 |
medicine |
treatment with ClpP inhibits cell growth and induces apoptosis in SK-N-SH neuroblastoma cells. Treatment results in hypodiploid DNA contents, increased Bax/Bcl-2 ratio and induction of reactive oxygen species production. The release of cytochrome c from mitochondria into the cytosol, is not observed in ClpP-treated cells. Pretreatment with Z-Val-Ala-Asp-fluoromethylketone, a broad spectrum caspase inhibitor, cannot rescue apoptotic cells from ClpP toxicity. Caspase-3 and -8 activation and cleavage of PARP are not detected. Caspase independent apoptosis-inducing factor is released from mitochondria and translocated to the nucleus in response to ClpP. ClpP treatment results in the increase of p53 activity, and cytoplasmic p53 levels are increased by ClpP |
Streptococcus pneumoniae |
Cloned(Commentary)
EC Number |
Cloned (Comment) |
Organism |
---|
3.4.21.92 |
expression in Escherichia coli |
Streptococcus pneumoniae |
Localization
EC Number |
Localization |
Comment |
Organism |
GeneOntology No. |
Textmining |
---|
Organism
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
3.4.21.92 |
Streptococcus pneumoniae |
- |
- |
- |
Source Tissue
EC Number |
Source Tissue |
Comment |
Organism |
Textmining |
---|
Synonyms
EC Number |
Synonyms |
Comment |
Organism |
---|
3.4.21.92 |
ClpP |
- |
Streptococcus pneumoniae |