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- Title
Inhibition of tyrosine phosphatases induces apoptosis independent from the CD95 system.
- Authors
Hehner, Steffen P; Hofmann, Thomas G; Dröge, Wulf; Schmitz, M Lienhard
- Abstract
The inhibition of protein tyrosine phosphatases by pervanadate, a potent activator of B- and T-cells through the induction of tyrosine phosphorylation and downstream signaling events in different activation cascades, efficiently induced apoptosis in lymphoid cell lines. Pervanadate-elicited apoptosis could be blocked by the tyrosine kinase inhibitor herbimycin A. This apoptotic process involved the activation of caspases 3, 8 and 9, the induction of mitochondrial permeability transition, the release of cytochrome C and the fragmentation of chromosomal DNA. T-cells lacking the CD95 receptor or caspase-8 and T-cells stably overexpressing a transdominant negative form of the adaptor protein FADD were still susceptible to pervanadate-induced apoptosis, excluding the involvement of the CD95 system or other FADD-dependent death receptors. The apoptotic program initiated by the inhibition of tyrosine phosphatases did not require the presence of the tyrosine kinase p56[sup lck] or phosphatase CD45, whereas Bcl-2 overexpression protected T-cells from pervanadate-induced cytochrome C release, caspase-8 cleavage and apoptosis.
- Subjects
APOPTOSIS; TYROSINE; T cells
- Publication
Cell Death & Differentiation, 1999, Vol 6, Issue 9, p833
- ISSN
1350-9047
- Publication type
Article
- DOI
10.1038/sj.cdd.4400559