Activation of B cell apoptotic pathways in the course of Francisella tularensis infection
Language English Country England, Great Britain Media print-electronic
Document type Journal Article, Research Support, Non-U.S. Gov't
PubMed
20600796
DOI
10.1016/j.micpath.2010.06.003
PII: S0882-4010(10)00105-1
Knihovny.cz E-resources
- MeSH
- Apoptosis * MeSH
- B-Lymphocytes microbiology MeSH
- Cell Line MeSH
- Cytochromes c metabolism MeSH
- Francisella tularensis pathogenicity MeSH
- Caspase 3 biosynthesis MeSH
- Caspase 8 biosynthesis MeSH
- Caspase 9 biosynthesis MeSH
- Humans MeSH
- Membrane Potential, Mitochondrial MeSH
- Mitochondria enzymology physiology MeSH
- BH3 Interacting Domain Death Agonist Protein biosynthesis MeSH
- Check Tag
- Humans MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- BID protein, human MeSH Browser
- CASP8 protein, human MeSH Browser
- Cytochromes c MeSH
- Caspase 3 MeSH
- Caspase 8 MeSH
- Caspase 9 MeSH
- BH3 Interacting Domain Death Agonist Protein MeSH
Francisella tularensis is a facultative intracellular, gram-negative bacterium that induces apoptosis in macrophages and B cells. Here we show apoptotic pathways that are activated in the Ramos human B cell line in the course of F. tularensis infection. Live bacteria F. tularensis FSC200 activate caspases 8, 9 and 3, as well as Bid; release cytochrome c and apoptosis-inducing factor from mitochondria; and induce depolarization of mitochondrial membrane potential in the Ramos cell line, thus leading these cells to apoptosis. Unlike live bacteria, killed F. tularensis FSC200 bacteria activated only caspase 3, and did not cause apoptosis of Ramos cells as measured by annexin V. Killed bacteria also caused accumulation of anti-apoptotic protein Bclx(L) in mitochondrial membranes. Thus, live F. tularensis activates both caspase pathways (receptor-mediated and intrinsic) as well as caspase-independent mitochondrial death.
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