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- Title
Inhibition of heat shock protein 27 phosphorylation promotes sensitivity to 5-fluorouracil in colorectal cancer cells.
- Authors
ATSUSHI MATSUNAGA; YOSHIYUKI ISHII; MASASHI TSURUTA; KOJI OKABAYASHI; HIROTOSHI HASEGAWA; YUKO KITAGAWA
- Abstract
The aim of the present study was to investigate whether the inhibition of HSP27 phosphorylation, which affects certain cellular functions, modulates sensitivity to 5-fluorouracil (5-FU) in colorectal cancer cells. Exposure to 5-FU in HCT116 and HCT15 cells expressing high levels of HSP27 with a low 5-FU sensitivity caused a minimal change in HSP27 expression, but induced the upregulation of HSP27 phosphorylation, particularly at Ser78. By contrast, exposure to 5-FU in HT29 cells expressing a low level of HSP27 with a high 5-FU sensitivity marginally increased HSP27 expression, with minimal phosphorylation. Treatment with a selective inhibitor, p38 mitogen-activated protein kinase (MAPK; SB203580), caused the dose-dependent suppression of HSP27 phosphorylation, which was upregulated by 5-FU, reducing the half maximal inhibitory concentration values of 5-FU in the HCT116 and HCT15 cells. However, treatment with SB203580 exhibited no significant effect on cell growth or survival. In conclusion, this study indicated that the inhibition of HSP27 phosphorylation by a selective inhibitor of p38 MAPK promotes 5-FU sensitivity without causing cytotoxicity in colorectal cancer cells.
- Subjects
HEAT shock proteins; PHOSPHORYLATION; FLUOROURACIL; COLON cancer; CANCER cells
- Publication
Oncology Letters, 2014, Vol 8, Issue 6, p2496
- ISSN
1792-1074
- Publication type
Article
- DOI
10.3892/ol.2014.2580