Fibrinogen Alpha Chain Acts as a HBsAg Binding Protein and their Interaction Promotes HepG2 Cell Apoptosis

ISSN: 1875-6247 (Online)
ISSN: 1570-1646 (Print)


Volume 11, 4 Issues, 2014


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Current Proteomics

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Fibrinogen Alpha Chain Acts as a HBsAg Binding Protein and their Interaction Promotes HepG2 Cell Apoptosis

Author(s): Ping Li, Li Xiao, Ying-Ying Li, Xu Chen, Chuan-Xing Xiao, Jing-Jing Liu, Xiao-Ning Yang, Amarsanaa Jazag, Jian-Lin Ren and Bayasi Guleng

Affiliation: Department of Gastroenterology, Zhongshan Hospital affiliated with Xiamen University, 201 Hubin South Road, Xiamen, Fujian Province, China 361004.

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.


Keywords: Binding protein, FGA, HBs, HepG2 cell apoptosis.

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Article Details

Volume: 11
Issue Number: 1
First Page: 48
Last Page: 54
Page Count: 7
DOI: 10.2174/1570164611666140412003740
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