S-Space College of Medicine/School of Medicine (의과대학/대학원) Internal Medicine (내과학전공) Journal Papers (저널논문_내과학전공)
TNF-alpha-mediated apoptosis in chondrocytes sensitized by MG132 or actinomycin D
- Kim, Hyun A.; Song, Yeong W.
- Issue Date
- Biochem. Biophys. Res. Commun. 295 (2005) 937-944
- Annexin A5/pharmacology; *Apoptosis; 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
- 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.
- 0006-291X (Print)
- Files in This Item: There are no files associated with this item.