Activation of the apoptotic protease CPP32 by cytotoxic T-cell-derived granzyme B View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1995-10

AUTHORS

A J Darmon, D W Nicholson, R C Bleackley

ABSTRACT

Cytotoxic T lymphocyte (CTL)-mediated cytotoxicity represents the body's major defence against virus-infected and tumorigenic cells, and contributes to transplant rejection and autoimmune disease. During killing, CTL granules are exocytosed, releasing their contents into the intercellular space between the target cell and the effector. Perforin facilitates the entry of cytotoxic cell serine proteases, the granzymes, into the target cell, where they induce apoptotic death by an unknown pathway. Granzyme B is essential for the induction of DNA fragmentation and apoptosis in target cells, yet its substrate is unknown. Identification of the intracellular substrate for granzyme B is therefore the key to understanding the mechanism of CTL-mediated killing. Here we show that granzyme B cleaves and activates CPP32, the precursor of the protease responsible for cleavage of poly(ADP-ribose) polymerase. More... »

PAGES

446

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/377446a0

DOI

http://dx.doi.org/10.1038/377446a0

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1016593213

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/7566124


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