Bisphenol A diglycidyl ether induces apoptosis in tumour cells independently of peroxisome proliferator-activated receptor-gamma, in caspase-dependent and -independent manners

Peroxisome proliferator-activated receptors (PPARs) are nuclear transcription factors which are involved in many biological processes, such as regulation of cell differentiation, lipid metabolism, inflammation and cell death. PPARs consist of three families, PPAR-alpha, PPAR-delta and PPAR-gamma. Bi...

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Bibliographic Details
Published in:Biochemical journal 2002-03, Vol.362 (Pt 3), p.573-578
Main Authors: Fehlberg, Sebastian, Trautwein, Stefan, Göke, Alexandra, Göke, Rüdiger
Format: Article
Language:English
Subjects:
Apoptosis - drug effects
Apoptosis Regulatory Proteins
Benzhydryl Compounds
Carcinogens - toxicity
Carcinoma
Caspases - metabolism
Cell Survival - drug effects
Colorectal Neoplasms
Epoxy Compounds - toxicity
Humans
Intracellular Membranes - physiology
Jurkat Cells
Membrane Glycoproteins - pharmacology
Membrane Potentials
Mitochondria - drug effects
Mitochondria - physiology
Receptors, Cytoplasmic and Nuclear - genetics
Receptors, Cytoplasmic and Nuclear - physiology
TNF-Related Apoptosis-Inducing Ligand
Transcription Factors - genetics
Transcription Factors - physiology
Tumor Cells, Cultured
Tumor Necrosis Factor-alpha - pharmacology
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Summary:Peroxisome proliferator-activated receptors (PPARs) are nuclear transcription factors which are involved in many biological processes, such as regulation of cell differentiation, lipid metabolism, inflammation and cell death. PPARs consist of three families, PPAR-alpha, PPAR-delta and PPAR-gamma. Bisphenol A diglycidyl ether (BADGE) has been described as a pure antagonist of PPAR-gamma. However, recent data also revealed PPAR-gamma-agonistic activities of BADGE. Here we show that BADGE kills transformed cells by apoptosis and promotes the cytotoxic effects of tumour necrosis factor-related apoptosis-inducing ligand (TRAIL) and indomethacin. The cytotoxic effect of BADGE does not require PPAR-gamma expression and is mediated in caspase-dependent and caspase-independent manners.
ISSN:0264-6021
1470-8728
DOI:10.1042/0264-6021:3620573