Enhanced invasive and metastatic potential induced by transforming growth factor-beta1 might be correlated with glutathione-S-transferase-pi, cofilin and heat shock protein 27 in SGC-7901 gastric cancer cells.
In our previous study, we found that the transforming growth factor (TGF)-beta1 enhanced the metastatic and invasive potential of gastric cancer cells. Proteomics was employed in this study to further illustrate the underlying molecular mechanisms. After two-dimensional electrophoresis, image analysis, spot identification, protein identification and database analysis, three proteins, namely, glutathione-S-transferase-pi (GST-pi), cofilin and heat shock protein 27 (HSP27), were found to be up-regulated in TGF-beta1 treated SGC-7901 cells. The findings were further confirmed by Western blot analysis. These results suggested that GST-pi, cofilin and HSP27 might participate in enhanced invasive potential induced by TGF-beta1.
Wang
Kuansong
K
Department of Pathology, Basic School of Medicine, Central South University, Changsha 410013, China.
Li
Jinghe
J
Zhen
Changli
C
Zhou
Jianhua
J
Xiao
Desheng
D
Liu
Jie
J
Liu
Ying
Y
Jiang
Haiying
H
Chen
Chen
C
Wen
Jifang
J
D051339:Actin Depolymerizing Factors / Q000502:physiology*; D000595:Amino Acid Sequence; D045744:Cell Line, Tumor; D051549:Glutathione S-Transferase pi / Q000502:physiology*; D006360:Heat-Shock Proteins / Q000502:physiology*; D006801:Humans; D008969:Molecular Sequence Data; D009361:Neoplasm Invasiveness; D009362:Neoplasm Metastasis; D013274:Stomach Neoplasms / Q000201:enzymology / Q000473:pathology*; D053773:Transforming Growth Factor beta1 / Q000502:physiology*
D051339:Actin Depolymerizing Factors; D006360:Heat-Shock Proteins; D053773:Transforming Growth Factor beta1; D051549:Glutathione S-Transferase pi