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Literature summary for 3.4.21.92 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.
    View publication on PubMed

Application

Application Comment Organism
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)

Cloned (Comment) Organism
expression in Escherichia coli Streptococcus pneumoniae

Localization

Localization Comment Organism GeneOntology No. Textmining

Organism

Organism UniProt Comment Textmining
Streptococcus pneumoniae
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining

Synonyms

Synonyms Comment Organism
ClpP
-
Streptococcus pneumoniae