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

Anticancer Res. 2010 Jul;30(7):2539-43.

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Antimetabolites, Antineoplastic / pharmacology*
  • Blotting, Western
  • Cell Line, Tumor
  • Deoxycytidine / analogs & derivatives*
  • Deoxycytidine / pharmacology
  • Drug Resistance, Neoplasm
  • Electrophoresis, Gel, Two-Dimensional
  • Gemcitabine
  • HSP27 Heat-Shock Proteins / metabolism*
  • Humans
  • Pancreatic Neoplasms / drug therapy*
  • Pancreatic Neoplasms / metabolism*
  • Phosphorylation
  • Protein Isoforms
  • Up-Regulation

Substances

  • Antimetabolites, Antineoplastic
  • HSP27 Heat-Shock Proteins
  • Protein Isoforms
  • Deoxycytidine
  • Gemcitabine