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


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.


CONCLUSIONS
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.
Taba
Kumiko
K
Department of Biochemistry and Functional Proteomics, Yamaguchi University Graduate School of Medicine, 1-1-1 Minami-Kogushi, Ube, Yamaguchi 755-8505, Japan.
Kuramitsu
Yasuhiro
Y
Ryozawa
Shomei
S
Yoshida
Kanako
K
Tanaka
Toshiyuki
T
Maehara
Shin-Ichiro
S
Maehara
Yoshihiro
Y
Sakaida
Isao
I
Nakamura
Kazuyuki
K
D000964:Antimetabolites, Antineoplastic / Q000494:pharmacology*; D015153:Blotting, Western; D045744:Cell Line, Tumor; D003841:Deoxycytidine / Q000031:analogs & derivatives* / Q000494:pharmacology; D019008:Drug Resistance, Neoplasm; D015180:Electrophoresis, Gel, Two-Dimensional; D055551:HSP27 Heat-Shock Proteins / Q000378:metabolism*; D006801:Humans; D010190:Pancreatic Neoplasms / Q000188:drug therapy* / Q000378:metabolism*; D010766:Phosphorylation; D020033:Protein Isoforms; D015854:Up-Regulation; D000093542:Gemcitabine
D000964:Antimetabolites, Antineoplastic; D055551:HSP27 Heat-Shock Proteins; D020033:Protein Isoforms; D003841:Deoxycytidine; D000093542:Gemcitabine