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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
47
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pubmed:dateCreated |
1996-1-17
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pubmed:abstractText |
beta-D-mannoside beta-1,4-N-acetylglucosaminyltransferase III (GnT-III) catalyzes the addition of N-acetylglucosamine in beta 1-4 linkage to the beta-linked mannose of the trimannosyl core of N-linked oligosaccharides and forms a bisecting GlcNAc structure. Although the biological meaning of the bisecting GlcNAc structure remains unclear, it is known that the attachment of a bisecting GlcNAc inhibits further processing of oligosaccharides by other glycosyltransferases. To investigate whether or not structural changes of oligosaccharides affect secretion and gene expression of hepatitis B virus (HBV), we introduced the GnT-III gene into a human hepatoma cell line, HB611, which secreted HBV-related proteins into the medium. Positive transfectants were cloned by hygromycin resistant selection. Three clones have high activities of GnT-III and secreted lower levels of HBV-related proteins into the medium in comparison with other clones. These clones showed marked suppression of HBV-related mRNAs and an increased binding with E-PHA as judged by lectin blot. Expression of beta actin, alpha fetoprotein, albumin, and prealubmin was not correlated with GnT-III activity in all the seven clones. Treatment of these cells with tunicamycin or swainsonine resulted in enhanced expression of HBV-related mRNA. These results indicate that some glycoproteins whose oligosaccharide structures are changed by over-expression of GnT-III suppress HBV gene expression.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Glycosyltransferases,
http://linkedlifedata.com/resource/pubmed/chemical/Lectins,
http://linkedlifedata.com/resource/pubmed/chemical/N-Acetylglucosaminyltransferases,
http://linkedlifedata.com/resource/pubmed/chemical/Oligosaccharides,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Viral,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Viral Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/beta-1,4-mannosyl-glycoprotein...
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pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
0021-9258
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
24
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pubmed:volume |
270
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
28311-5
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:7499330-Blotting, Northern,
pubmed-meshheading:7499330-Carcinoma, Hepatocellular,
pubmed-meshheading:7499330-Cell Line,
pubmed-meshheading:7499330-Flow Cytometry,
pubmed-meshheading:7499330-Glycosyltransferases,
pubmed-meshheading:7499330-Hepatitis B virus,
pubmed-meshheading:7499330-Humans,
pubmed-meshheading:7499330-Lectins,
pubmed-meshheading:7499330-Liver Neoplasms,
pubmed-meshheading:7499330-N-Acetylglucosaminyltransferases,
pubmed-meshheading:7499330-Oligosaccharides,
pubmed-meshheading:7499330-RNA, Messenger,
pubmed-meshheading:7499330-RNA, Viral,
pubmed-meshheading:7499330-Recombinant Proteins,
pubmed-meshheading:7499330-Transfection,
pubmed-meshheading:7499330-Tumor Cells, Cultured,
pubmed-meshheading:7499330-Viral Proteins
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pubmed:year |
1995
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pubmed:articleTitle |
Transfection of N-acetylglucosaminyltransferase III gene suppresses expression of hepatitis B virus in a human hepatoma cell line, HB611.
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pubmed:affiliation |
Department of Biochemistry, Osaka University Medical School, Japan.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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