title: Extracellular HSP70/HSP70-PCs promote epithelial-mesenchymal transition of hepatocarcinoma cells.
abstract: BACKGROUND
  Extracellular heat shock protein 70 and peptide complexes (eHSP70/HSP70-PCs) regulate a variety of biological behaviors in tumor cells. Whether eHSP70/HSP70-PCs are involved in the epithelial-mesenchymal transition (EMT) of tumor cells remains unclear.
  
  
  OBJECTIVE
  To determine the effects of eHSP70/HSP70-PCs on EMT of hepatocarcinoma cells.
  
  
  METHODS
  The expressions of E-cadherin, HSP70, α-smooth muscle actin protein (α-SMA) and p-p38 were detected immunohistochemically in liver cancer samples. Immunofluorescence, western blotting and real-time RT-PCR methods were used to analyze the effects of eHSP70/HSP70-PCs on the expressions of E-cadherin, α-SMA and p38/MAPK in vivo.
  
  
  RESULTS
  HSP70, E-cadherin, α-SMA and p-p38 were elevated in hepatocellular carcinoma tissues. The expression of HSP70 was positively correlated with malignant differentiated liver carcinoma. The expressions of HSP70, α-SMA and p-p38 correlated with recurrence-free survival after resection. eHSP70/HSP70-PCs significantly promoted the expressions of α-SMA and p-p38 and reduced the expressions of E-cadherin in vivo. The effect was inhibited by SB203580.
  
  
  CONCLUSIONS
  The expressions of HSP70, E-cadherin, α-SMA and p-p38 may represent indicators of malignant potential and could discriminate the malignant degree of liver cancer. eHSP70/HSP70-PCs play an important role in the EMT of hepatocellular carcinoma via the p38/MAPK pathway.
authors.affiliation: Department of General Surgery, Shengjing Hospital Affiliated to China Medical University, Shenyang, China.
authors.forename: Hangyu
authors.initials: H
authors.lastname: Li
authors.affiliation: Department of General Surgery, Shengjing Hospital Affiliated to China Medical University, Shenyang, China.
authors.forename: Yan
authors.initials: Y
authors.lastname: Li
authors.affiliation: Department of General Surgery, Shengjing Hospital Affiliated to China Medical University, Shenyang, China.
authors.forename: Dan
authors.initials: D
authors.lastname: Liu
authors.affiliation: Department of General Surgery, First Hospital Affiliated to Liaoning Medical College, Jinzhou, China.
authors.forename: Hongzhi
authors.initials: H
authors.lastname: Sun
authors.affiliation: Center of Metabolic Disease Research, Nanjing Medical University, Nanjing, China.
authors.forename: Dongming
authors.initials: D
authors.lastname: Su
authors.affiliation: Department of General Surgery, Shengjing Hospital Affiliated to China Medical University, Shenyang, China.
authors.forename: Fuquan
authors.initials: F
authors.lastname: Yang
authors.affiliation: Department of General Surgery, Shengjing Hospital Affiliated to China Medical University, Shenyang, China.
authors.forename: Jingang
authors.initials: J
authors.lastname: Liu
mesh_terms: D000328:Adult; D006528:Carcinoma, Hepatocellular / Q000378:metabolism* / Q000473:pathology; D045744:Cell Line, Tumor; D058750:Epithelial-Mesenchymal Transition; D005260:Female; D015972:Gene Expression Regulation, Neoplastic; D018840:HSP70 Heat-Shock Proteins / Q000096:biosynthesis*; D006801:Humans; D008113:Liver Neoplasms / Q000378:metabolism* / Q000473:pathology; D008297:Male; D008875:Middle Aged; D009363:Neoplasm Proteins / Q000096:biosynthesis*
chemical_list: D018840:HSP70 Heat-Shock Proteins; D009363:Neoplasm Proteins