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http://purl.uniprot.org/citations/24758376http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/24758376http://www.w3.org/2000/01/rdf-schema#comment"

Background

The risk of hepatocellular carcinoma (HCC) increases in chronic hepatitis B surface antigen (HBsAg) carriers who often have concomitant increase in the levels of benzo[alpha]pyrene-7,8-diol-9,10-epoxide(±) (BPDE)-DNA adduct in liver tissues, suggesting a possible co-carcinogenesis of Hepatitis B virus (HBV) and benzo[alpha]pyrene in HCC; however the exact mechanisms involved are unclear.

Methods

The interaction between hepatitis B spliced protein (HBSP) and microsomal epoxide hydrolase (mEH) was confirmed using GST pull-down, co-immunoprecipitation and mammalian two-hybrid assay; the effects of HBSP on mEH-mediated B[alpha]P metabolism was examined by high performance liquid chromatography (HPLC); and the influences of HBSP on B[alpha]P carcinogenicity were evaluated by bromodeoxyuridine cell proliferation, anchorage-independent growth and tumor xenograft.

Results

HBSP could interact with mEH in vitro and in vivo, and this interaction was mediated by the N terminal 47 amino acid residues of HBSP. HBSP could greatly enhance the hydrolysis activity of mEH in cell-free mouse liver microsomes, thus accelerating the metabolism of benzo[alpha]pyrene to produce more ultimate carcinnogen, BPDE, and this effect of HBSP requires the intact HBSP molecule. Expression of HBSP significantly increased the formation of BPDE-DNA adduct in benzo[alpha]pyrene-treated Huh-7 hepatoma cells, and this enhancement was blocked by knockdown of mEH. HBSP could enhance the cell proliferation, accelerate the G1/S transition, and promote cell transformation and tumorigenesis of B[alpha]P-treated Huh-7 hepatoma cells.

Conclusions

Our results demonstrated that HBSP could promote carcinogenic effects of B[alpha]P by interacting with mEH and enhancing its hydrolysis activity."xsd:string
http://purl.uniprot.org/citations/24758376http://purl.org/dc/terms/identifier"doi:10.1186/1471-2407-14-282"xsd:string
http://purl.uniprot.org/citations/24758376http://purl.uniprot.org/core/author"Chen J.Y."xsd:string
http://purl.uniprot.org/citations/24758376http://purl.uniprot.org/core/author"Lin X."xsd:string
http://purl.uniprot.org/citations/24758376http://purl.uniprot.org/core/author"Lin W.S."xsd:string
http://purl.uniprot.org/citations/24758376http://purl.uniprot.org/core/author"Wu Y.L."xsd:string
http://purl.uniprot.org/citations/24758376http://purl.uniprot.org/core/author"Liu L.L."xsd:string
http://purl.uniprot.org/citations/24758376http://purl.uniprot.org/core/author"Chen W.N."xsd:string
http://purl.uniprot.org/citations/24758376http://purl.uniprot.org/core/author"Jiao B.Y."xsd:string
http://purl.uniprot.org/citations/24758376http://purl.uniprot.org/core/date"2014"xsd:gYear
http://purl.uniprot.org/citations/24758376http://purl.uniprot.org/core/name"BMC Cancer"xsd:string
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http://purl.uniprot.org/citations/24758376http://purl.uniprot.org/core/title"Hepatitis B spliced protein (HBSP) promotes the carcinogenic effects of benzo [alpha] pyrene by interacting with microsomal epoxide hydrolase and enhancing its hydrolysis activity."xsd:string
http://purl.uniprot.org/citations/24758376http://purl.uniprot.org/core/volume"14"xsd:string
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