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

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

Surgery

Research output: Contribution to journal › Article › peer-review

39 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 language	English
Pages (from-to)	2539-2543
Number of pages	5
Journal	Anticancer research
Volume	30
Issue number	7
Publication status	Published - Jul 2010

All Science Journal Classification (ASJC) codes

Oncology
Cancer Research

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

Cite this

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title = "Heat-shock protein 27 is phosphorylated in gemcitabine-resistant pancreatic cancer cells",

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.",

author = "Kumiko Taba and Yasuhiro Kuramitsu and Shomei Ryozawa and Kanako Yoshida and Toshiyuki Tanaka and Maehara, {Shin Ichiro} and Yoshihiro Maehara and Isao Sakaida and Kazuyuki Nakamura",

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language = "English",

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pages = "2539--2543",

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TY - JOUR

T1 - Heat-shock protein 27 is phosphorylated in gemcitabine-resistant pancreatic cancer cells

AU - Taba, Kumiko

AU - Kuramitsu, Yasuhiro

AU - Ryozawa, Shomei

AU - Yoshida, Kanako

AU - Tanaka, Toshiyuki

AU - Maehara, Shin Ichiro

AU - Maehara, Yoshihiro

AU - Sakaida, Isao

AU - Nakamura, Kazuyuki

PY - 2010/7

Y1 - 2010/7

N2 - 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.

AB - 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.

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SN - 0250-7005

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JO - Anticancer research

JF - Anticancer research

IS - 7

ER -

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

Abstract

All Science Journal Classification (ASJC) codes

UN SDGs

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