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TNF-α Mediates Eosinophil Cationic Protein-induced Apoptosis in BEAS-2B Cells
- Source :
- BMC Cell Biology, BMC Cell Biology, Vol 11, Iss 1, p 6 (2010)
- Publisher :
- Springer Nature
-
Abstract
- BackgroundEosinophilic granulocytes are important for the human immune system. Many cationic proteins with cytotoxic activities, such as eosinophil cationic protein (ECP) and eosinophil-derived neurotoxin (EDN), are released from activated eosinophils. ECP, with low RNase activity, is widely used as a biomarker for asthma. ECP inhibits cell viability and induces apoptosis to cells. However, the specific pathway underlying the mechanisms of ECP-induced cytotoxicity remains unclear. This study investigated ECP-induced apoptosis in bronchial epithelial BEAS-2B cells and elucidated the specific pathway during apoptosis.ResultsTo address the mechanisms involved in ECP-induced apoptosis in human BEAS-2B cells, investigation was carried out using chromatin condensation, cleavage of poly (ADP-ribose) polymerase (PARP), sub-G1 distribution in cell cycle, annexin V labeling, and general or specific caspase inhibitors. Caspase-8-dependent apoptosis was demonstrated by cleavage of caspase-8 after recombinant ECP treatment, accompanied with elevated level of tumor necrosis factor alpha (TNF-α). Moreover, ECP-induced apoptosis was effectively inhibited in the presence of neutralizing anti-TNF-α antibody.ConclusionIn conclusion, our results have demonstrated that ECP increased TNF-α production in BEAS-2B cells and triggered apoptosis by caspase-8 activation through mitochondria-independent pathway.
- Subjects :
- education
Eosinophil-derived neurotoxin
Apoptosis
Eosinophil-Derived Neurotoxin
Biology
Caspase 8
Antibodies
fluids and secretions
Annexin
Cell Line, Tumor
Research article
Cytotoxic T cell
Humans
lcsh:QH573-671
Annexin A5
Eosinophil cationic protein
lcsh:Cytology
Tumor Necrosis Factor-alpha
Eosinophil Cationic Protein
G1 Phase
Cell Biology
Molecular biology
Recombinant Proteins
Cell biology
Eosinophils
Tumor necrosis factor alpha
Poly(ADP-ribose) Polymerases
Subjects
Details
- Language :
- English
- ISSN :
- 14712121
- Volume :
- 11
- Issue :
- 1
- Database :
- OpenAIRE
- Journal :
- BMC Cell Biology
- Accession number :
- edsair.doi.dedup.....d1cce776ca841504cd7931af5a0d9979
- Full Text :
- https://doi.org/10.1186/1471-2121-11-6