Cancer cell sensitization to Fas-mediated apoptosis by sodium butyrate
| Autor: | Nathalie Favre, Nathalie Droin, Sylvie Reveneau, Bernard Bonnotte, Olivier Micheau, Adriano Fontana, Bruno Chauffert, François Martin, Carmen Garrido, Eric Solary |
|---|---|
| Rok vydání: | 1998 |
| Předmět: |
Fas Ligand Protein
Fas-Associated Death Domain Protein bcl-X Protein Apoptosis Butyrate Fas ligand Interferon-gamma chemistry.chemical_compound Bcl-2-associated X protein Proto-Oncogene Proteins In Situ Nick-End Labeling Tumor Cells Cultured Animals Humans Microscopy Phase-Contrast FADD Molecular Biology Adaptor Proteins Signal Transducing bcl-2-Associated X Protein Membrane Glycoproteins biology Tumor Necrosis Factor-alpha Sodium butyrate Cell Biology Flow Cytometry Fas receptor Rats Cell biology Proto-Oncogene Proteins c-bcl-2 chemistry Colonic Neoplasms Cancer cell biology.protein Cancer research Butyric Acid Carrier Proteins |
| Zdroj: | Scopus-Elsevier |
| ISSN: | 1476-5403 1350-9047 |
| DOI: | 10.1038/sj.cdd.4400371 |
| Popis: | Cancer cells often resist Fas-mediated apoptosis even when the Fas receptor is expressed at the cell surface. We show here that human and rat colon cancer cells undergo massive apoptosis when they are exposed to soluble Fas ligand in the presence of sodium butyrate, an agent that induces by itself only a low rate of apoptosis. Sodium butyrate potentiates Fas-dependent apoptosis in seven out of eight colon cancer cell lines. Sodium butyrate does not increase Fas receptor cell surface expression and does not modify cell levels of Bcl-2, Bcl-xL, Bcl-xS and Bax. Sodium butyrate also induces tumor cell sensitization to the apoptotic effect of the combination of TNF-alpha and IFN-gamma, but it does not modify the level of the FADD/Mort1 adaptator molecule, at the connection between Fas- and TNF-dependent apoptosis pathways. Because the clinical toxicity of butyrate is low, its ability to enhance Fas-signal delivery in cancer cells could be of therapeutic interest. |
| Databáze: | OpenAIRE |
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