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2000
Volume 11, Issue 1
  • ISSN: 1570-1646
  • E-ISSN: 1875-6247

Abstract

Background and Aims: Our previous yeast two-hybrid screening data showed the Fibrinogen alpha chain (FGA) as one of the candidate binding proteins of S regional of the HBsAg (HBs). In this study, we aimed to define that FGA is a binding protein of HBs and to determine its function in Hepatocellular carcinoma (HCC) tumorigenesis. Methods: The binding and co-localization between HBs and FGA were confirmed using co-immunoprecipitation and confocal microscopy was employed flow cytometry to analyze cell apoptosis. The involved mechanisms were investigated using protein array and western blot. Results: Our results indicated that FGA is a binding protein of HBs and is co-localized in the cytoplasm in vitro. Interaction between HBs and FGA significantly induced apoptosis in HepG2 cells. Moreover, knockdown of the FGA protein decreased the expression levels of the pro-survival factors Bcl-XL and Mcl-1, increased the expression of the proapoptotic proteins, and decreased the phosphorylation levels of Akt in this cell. Conclusion: FGA is a binding protein of HBs and their interaction induced the apoptotic capacity of HepG2 cells, suggesting the interactions between viral and host cell proteins are involved in the development of virus-related hepatitis or HCC.

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/content/journals/cp/10.2174/1570164611666140412003740
2014-04-01
2025-07-15
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/content/journals/cp/10.2174/1570164611666140412003740
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  • Article Type:
    Research Article
Keyword(s): Binding protein; FGA; HBs; HepG2 cell apoptosis
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