A new PKCα/β/TBX3/E-cadherin pathway is involved in PLCε-regulated invasion and migration in human bladder cancer cells

Cell Signal. 2014 Mar;26(3):580-93. doi: 10.1016/j.cellsig.2013.11.015. Epub 2013 Dec 6.

Abstract

Although PLCε has been verified to enhance bladder cancer cell invasion, the signaling pathways responsible for this remain elusive. Protein kinase C (PKCα/β), which is involved in cancer development and progression, has been demonstrated to be activated by PLCε. However, the roles of PKCα/β in PLCε-mediated bladder carcinoma cell invasion and migration have not been clearly identified. In this study, to determine what role PKCα/β plays in PLCε-mediated bladder cancer cell invasion and migration, we silenced PLCε gene by adenovirus-shPLCε in T24 and BIU-87 cells and then revealed that it significantly inhibited cell migration and invasion. Further research indicated that cell bio-function of PLCε-regulated was related with PKCα/β activity. These in vitro findings were supported by data from bladder carcinoma patient samples. In 35 case bladder cancer tumor samples, PLCε-overexpressing tumors showed significantly higher positive rates of PKCα/β membrane immunohistochemistry staining than PLCε-low-expressing tumors. Mechanistically, study further showed that PLCε knockdown gene induced E-cadherin expression and decreased TBX3 expression, both of which were dependent on PKCα/β activity. In addition, we demonstrated that treatment cells with TBX3-specific shorting hairpin RNA (shRNA) up-regulated E-cadherin expression and inhibited cell invasion/migration. Moreover, in in vivo experiment, immunohistochemistry analysis of Ad-shPLCε-infected tumor tissue showed low expression levels of phospho-PKCα/β and TBX3 and high expression levels of E-cadherin compared with those of the control group. In summary, our findings uncover that PKCα/β is critical for PLCε-mediated cancer cell invasion and migration and provide valuable insights for current and future Ad-shPLCε and PKCα/β clinical trials.

Keywords: Bladder cancer; E-cadherin; Invasion; Migration; PKCα; PKCα/β; PKCβ; PLCε; Phospholipase Cε; TBX3; protein kinase Cα; protein kinase Cβ.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Cadherins / biosynthesis
  • Carbazoles / pharmacology
  • Cell Line, Tumor
  • Cell Movement / genetics
  • Cell Proliferation
  • Humans
  • Mice
  • Mice, Nude
  • Neoplasm Invasiveness / genetics
  • Neoplasm Transplantation
  • Phosphoinositide Phospholipase C / genetics*
  • Protein Kinase C beta / antagonists & inhibitors
  • Protein Kinase C beta / biosynthesis
  • Protein Kinase C beta / metabolism*
  • Protein Kinase C-alpha / antagonists & inhibitors
  • Protein Kinase C-alpha / biosynthesis
  • Protein Kinase C-alpha / metabolism*
  • RNA Interference
  • RNA, Small Interfering
  • T-Box Domain Proteins / biosynthesis*
  • T-Box Domain Proteins / genetics
  • Transplantation, Heterologous

Substances

  • Cadherins
  • Carbazoles
  • RNA, Small Interfering
  • T-Box Domain Proteins
  • TBX3 protein, human
  • Go 6976
  • Protein Kinase C beta
  • Protein Kinase C-alpha
  • Phosphoinositide Phospholipase C
  • phospholipase C epsilon