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TNF-alpha-mediated apoptosis in chondrocytes sensitized by MG132 or actinomycin D
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- Authors
- Issue Date
- 2002
- Publisher
- Elsevier
- Citation
- Biochem. Biophys. Res. Commun. 295 (2005) 937-944
- Keywords
- Annexin A5/pharmacology ; Blotting, Western ; Caspases/antagonists & inhibitors ; Cell Nucleus/metabolism ; Chondrocytes/*metabolism/pathology ; Cysteine Proteinase Inhibitors/pharmacology ; Dactinomycin/metabolism/*pharmacology ; Flow Cytometry ; I-kappa B Proteins/metabolism ; Leupeptins/*pharmacology ; NF-kappa B/metabolism ; Protein Synthesis Inhibitors/pharmacology ; Recombinant Proteins/metabolism ; Signal Transduction ; Time Factors ; Tumor Necrosis Factor-alpha/*metabolism ; Tumor Suppressor Protein p53/metabolism ; Apoptosis
- Abstract
- The mechanism of TNF-alpha-mediated chondrocyte apoptosis in human articular cartilage was investigated. First passage OA chondrocytes were treated with actinomycin D or MG132 in combination with TNF-alpha to facilitate cell death. The patterns of apoptosis-related proteins, NF-kappaB activation, and IkappaB degradation were analyzed. Cell death was increased by 0.2 microg/ml of actinomycin D or 20 microM MG132 in combination with TNF-alpha. Apoptosis potentiated by MG132 was more effectively inhibited by caspase inhibitors than that by actinomycin D. MG132 or actinomycin D both led to a significant increase in p53, but the expressions of the p53 response proteins increased only in MG132 treated chondrocytes. TNF-alpha induced chondrocyte IkappaB phosphorylation was unaffected by either MG132 or actinomycin D. MG132, but not actinomycin D, inhibited the chondrocyte IkappaB degradation induced by TNF-alpha and NF-kappaB activation. Our results suggest that MG132 and actinomycin D exert different influences upon TNF-alpha-mediated chondrocyte apoptotic signaling.
- ISSN
- 0006-291X (Print)
- Language
- English
- URI
- http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=12127985
https://hdl.handle.net/10371/12128
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