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Ras/MAP Kinase pathways are involved in Ras specific apoptosis induced by sodium butyrate
Cited 45 time in
Web of Science
Cited 51 time in Scopus
- Authors
- Issue Date
- 2005-07
- Publisher
- Elsevier BV
- Citation
- Cancer Letters, Vol.225 No.2, pp.199-206
- Abstract
- Histone deacetylase inhibitors such as TSA, SAHA, and NaBu etc. are prospective cancer therapeutics of growing interest. Here, we demonstrated that oncogenic ras-transformed rat liver epithelial (WB-ras) cells were specifically undergone apoptosis by 48 h treatment of NaBu. During this, inhibition of ras proteins, especially farnesylated form of ras, and down-regulation of ERK1/2 were observed, which suggest ras/raf/MEK/ERK down-regulation, while p38 MAP kinase was maintained upregulated. In addition, up-regulation of pro-apoptotic proteins such as p53 and p21(CIPI/WAFI), and down-regulation of cell cycle regulator/anti-apoptotic proteins such as cdk2, -4 and phosphorylated Akt were observed concurrently with an increase in apoptotic cell portion. A phosphatase inhibitor, sodium orthovanadate (SOV), efficiently blocked apoptosis and restored responsible proteins for each phenomenon including ERK1/2 while SB203580, a specific p38 MAP kinase inhibitor, showed minor effect on them. Thus, ras/ERK signaling pathway can be considered in chemotherapeutic strategies of NaBu regardless of its inhibitory action on histone deacetylase. (c) 2004 Elsevier Ireland Ltd. All rights reserved.
- ISSN
- 0304-3835
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