Inhibition of CPP32-like proteases prevents granzyme B- and Fas-, but not granzyme A-based cytotoxicity exerted by CTL clones.
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Summary
The results suggest that granzyme B- and Fas-based cytotoxicity exerted by CTL clones converge at the level of CPP32-like protease activation, while granzyme A acts via a different, still undefined, pathway.
- Type
- article
- Published
- 1997-03-01
- Cited by
- 40
- References
- 1
- Access
- Open access
- OpenAlex
- https://openalex.org/W1564737805
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:42132503
Keywords
Granzyme, Perforin, Granzyme B, CTL*, Proteases
References
Cited by
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- Generation of Catalytically Active Granzyme K fromEscherichia coli Inclusion Bodies and Identification of Efficient Granzyme K Inhibitors in Human Plasma*
- Role of TNF Family Ligands in Antitumor Activity of Natural Killer Cells
- Cell death mediated by alloreactive cytotoxic T cells via the granule exocytosis or the Fas pathway is independent of p34cdc2 kinase: Fas dependent killing of cells arrested in the cell cycle
- In Vitro– and Ex Vivo–derived Cytolytic Leukocytes from Granzyme A × B Double Knockout Mice Are Defective in Granule-mediated Apoptosis but not Lysis of Target Cells
- The differential contribution of granzyme A and granzyme B in cytotoxic T lymphocyte‐mediated apoptosis is determined by the quality of target cells
- Granzyme A loading induces rapid cytolysis and a novel form of DNA damage independently of caspase activation.
- Cleavage of FLICE (caspase‐8) by granzyme B during cytotoxic T lymphocyte‐induced apoptosis
- Defects in the Ubiquitin Pathway Induce Caspase-independent Apoptosis Blocked by Bcl-2*
- Zinc-mediated regulation of caspases activity: dose-dependent inhibition or activation of caspase-3 in the human Burkitt lymphoma B cells (Ramos)
- Granzyme B-Induced Cell Death
- Sphingolipids and the immune system.
- Caspase Inhibition Blocks Cell Death and Results in Cell Cycle Arrest in Cytokine-deprived Hematopoietic Cells*
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