Heat-shock protein 27 is phosphorylated in gemcitabine-resistant pancreatic cancer cells

Kumiko Taba, Yasuhiro Kuramitsu, Shomei Ryozawa, Kanako Yoshida, Toshiyuki Tanaka, Shin Ichiro Maehara, Yoshihiro Maehara, Isao Sakaida, Kazuyuki Nakamura

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32 Citations (Scopus)

Abstract

Background: Gemcitabine (2′-deoxy-2′-difluorodeoxycytidine: Gemzar) (GEM) appears to be the only effective anticancer drug for pancreatic cancer, but it has little impact on outcome due to a high level of inherent and acquired tumor resistance. Our previous proteomic study demonstrated that the expression of three spots of heat-shock protein 27 (HSP27) was increased in GEM-resistant pancreatic cancer cells and could play a role in determining the sensitivity of pancreatic cancer to GEM. Materials and Methods and Results: In the present study, using one-dimensional and two-dimensional Western blotting, we elucidated that these three spots of HSP27 were phosphorylated in GEM-resistant pancreatic cancer cell line, KLM1-R. Conclusion: Phosphorylated HSP27 may play an important role in the resistance to GEM, and it could also be a possible biomarker for predicting the response of pancreatic cancer patients to treatment with GEM.

Original languageEnglish
Pages (from-to)2539-2543
Number of pages5
JournalAnticancer research
Volume30
Issue number7
Publication statusPublished - Jul 1 2010

All Science Journal Classification (ASJC) codes

  • Oncology
  • Cancer Research

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    Taba, K., Kuramitsu, Y., Ryozawa, S., Yoshida, K., Tanaka, T., Maehara, S. I., Maehara, Y., Sakaida, I., & Nakamura, K. (2010). Heat-shock protein 27 is phosphorylated in gemcitabine-resistant pancreatic cancer cells. Anticancer research, 30(7), 2539-2543.