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, Yoshihiko Maehara, Isao Sakaida, Kazuyuki Nakamura

Research output: Contribution to journalArticle

27 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

Fingerprint

gemcitabine
HSP27 Heat-Shock Proteins
Pancreatic Neoplasms
Proteomics
Biomarkers
Western Blotting

All Science Journal Classification (ASJC) codes

  • Oncology
  • Cancer Research

Cite this

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

Heat-shock protein 27 is phosphorylated in gemcitabine-resistant pancreatic cancer cells. / Taba, Kumiko; Kuramitsu, Yasuhiro; Ryozawa, Shomei; Yoshida, Kanako; Tanaka, Toshiyuki; Maehara, Shin Ichiro; Maehara, Yoshihiko; Sakaida, Isao; Nakamura, Kazuyuki.

In: Anticancer Research, Vol. 30, No. 7, 01.07.2010, p. 2539-2543.

Research output: Contribution to journalArticle

Taba, K, Kuramitsu, Y, Ryozawa, S, Yoshida, K, Tanaka, T, Maehara, SI, Maehara, Y, Sakaida, I & Nakamura, K 2010, 'Heat-shock protein 27 is phosphorylated in gemcitabine-resistant pancreatic cancer cells', Anticancer Research, vol. 30, no. 7, pp. 2539-2543.
Taba K, Kuramitsu Y, Ryozawa S, Yoshida K, Tanaka T, Maehara SI et al. Heat-shock protein 27 is phosphorylated in gemcitabine-resistant pancreatic cancer cells. Anticancer Research. 2010 Jul 1;30(7):2539-2543.
Taba, Kumiko ; Kuramitsu, Yasuhiro ; Ryozawa, Shomei ; Yoshida, Kanako ; Tanaka, Toshiyuki ; Maehara, Shin Ichiro ; Maehara, Yoshihiko ; Sakaida, Isao ; Nakamura, Kazuyuki. / Heat-shock protein 27 is phosphorylated in gemcitabine-resistant pancreatic cancer cells. In: Anticancer Research. 2010 ; Vol. 30, No. 7. pp. 2539-2543.
@article{6c0f02081c204c468931dc784179c9b0,
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 Yoshihiko Maehara and Isao Sakaida and Kazuyuki Nakamura",
year = "2010",
month = "7",
day = "1",
language = "English",
volume = "30",
pages = "2539--2543",
journal = "Anticancer Research",
issn = "0250-7005",
publisher = "International Institute of Anticancer Research",
number = "7",

}

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, Yoshihiko

AU - Sakaida, Isao

AU - Nakamura, Kazuyuki

PY - 2010/7/1

Y1 - 2010/7/1

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.

UR - http://www.scopus.com/inward/record.url?scp=77955832992&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=77955832992&partnerID=8YFLogxK

M3 - Article

VL - 30

SP - 2539

EP - 2543

JO - Anticancer Research

JF - Anticancer Research

SN - 0250-7005

IS - 7

ER -