ECHS1 acts as a novel HBsAg-binding protein enhancing apoptosis through the mitochondrial pathway in HepG2 cells

Cancer Lett. 2013 Mar 1;330(1):67-73. doi: 10.1016/j.canlet.2012.11.030. Epub 2012 Nov 23.

Abstract

We aimed to confirm the role of ECHS1 as a binding protein of HBsAg (HBs) and investigate its function during the development of hepatocellular carcinoma (HCC). Our results show that both exogenous and endogenous ECHS1 proteins bind to HBs and co-localize in the cytoplasm in vitro. The coexistence of HBs and ECHS1 enhances HepG2 cell apoptosis, affects ECHS1 localization in the mitochondria and induces apoptosis by decreasing the mitochondrial membrane potential (MMP). These findings suggest that ECHS1 may be applied as a potential therapeutic target during the treatment of HBV-related hepatitis or HCC.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Apoptosis / physiology
  • Carcinoma, Hepatocellular / metabolism*
  • Enoyl-CoA Hydratase / genetics
  • Enoyl-CoA Hydratase / metabolism*
  • Gene Knockdown Techniques
  • Hep G2 Cells
  • Hepatitis B Surface Antigens / genetics
  • Hepatitis B Surface Antigens / metabolism*
  • Humans
  • Liver Neoplasms / metabolism*
  • Membrane Potential, Mitochondrial / physiology
  • Microscopy, Confocal
  • Mitochondria / enzymology
  • Mitochondria / metabolism*
  • Phosphorylation
  • Protein Binding
  • Transfection

Substances

  • Hepatitis B Surface Antigens
  • Enoyl-CoA Hydratase