| pubmed-article:9482919 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:9482919 | lifeskim:mentions | umls-concept:C0003069 | lld:lifeskim |
| pubmed-article:9482919 | lifeskim:mentions | umls-concept:C0227525 | lld:lifeskim |
| pubmed-article:9482919 | lifeskim:mentions | umls-concept:C0036536 | lld:lifeskim |
| pubmed-article:9482919 | lifeskim:mentions | umls-concept:C0036537 | lld:lifeskim |
| pubmed-article:9482919 | lifeskim:mentions | umls-concept:C1521816 | lld:lifeskim |
| pubmed-article:9482919 | lifeskim:mentions | umls-concept:C0003593 | lld:lifeskim |
| pubmed-article:9482919 | lifeskim:mentions | umls-concept:C0053374 | lld:lifeskim |
| pubmed-article:9482919 | lifeskim:mentions | umls-concept:C1159705 | lld:lifeskim |
| pubmed-article:9482919 | lifeskim:mentions | umls-concept:C1512167 | lld:lifeskim |
| pubmed-article:9482919 | lifeskim:mentions | umls-concept:C0205263 | lld:lifeskim |
| pubmed-article:9482919 | pubmed:issue | 5 | lld:pubmed |
| pubmed-article:9482919 | pubmed:dateCreated | 1998-4-9 | lld:pubmed |
| pubmed-article:9482919 | pubmed:abstractText | N-Acetylglucosaminyltransferase III (GnT-III) produces "bisecting-GlcNAc" and regulates the branching of N-glycans. GnT-III activity is elevated during hepatocarcinogenesis, which is in contrast to the undetectable level found in normal hepatocytes. To determine the biological significance of GnT-III in hepatocytes, transgenic mice that specifically express GnT-III in the liver were established and characterized. The transgenic hepatocytes had a swollen oval-like morphology, with many lipid droplets. Apolipoprotein B, which contained increased level of bisecting-GlcNAc accumulated in the transgenic hepatocytes. In the transgenic serum, triglycerides, the beta- and pre-beta-lipoprotein fractions, and apolipoprotein B100 were significantly decreased, compared with levels in nontransgenic serum. These abnormal phenotypes were more prominent in the mice with more copies of the transgene and a resulting high GnT-III activity. We demonstrate that aberrant glycosylation, as the direct result of the formation of bisecting-GlcNAc, disrupts the function of apolipoprotein B, leading to the generation of fatty liver. This observation suggests a novel mechanism for the pathogenesis of fatty liver. | lld:pubmed |
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| pubmed-article:9482919 | pubmed:language | eng | lld:pubmed |
| pubmed-article:9482919 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9482919 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:9482919 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:9482919 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:9482919 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:9482919 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:9482919 | pubmed:issn | 0027-8424 | lld:pubmed |
| pubmed-article:9482919 | pubmed:author | pubmed-author:TaniguchiNN | lld:pubmed |
| pubmed-article:9482919 | pubmed:author | pubmed-author:SuzukiMM | lld:pubmed |
| pubmed-article:9482919 | pubmed:author | pubmed-author:OhnishiAA | lld:pubmed |
| pubmed-article:9482919 | pubmed:author | pubmed-author:YoshimuraMM | lld:pubmed |
| pubmed-article:9482919 | pubmed:author | pubmed-author:YamamuraKK | lld:pubmed |
| pubmed-article:9482919 | pubmed:author | pubmed-author:IharaYY | lld:pubmed |
| pubmed-article:9482919 | pubmed:author | pubmed-author:IjuhinNN | lld:pubmed |
| pubmed-article:9482919 | pubmed:author | pubmed-author:NishikawaAA | lld:pubmed |
| pubmed-article:9482919 | pubmed:author | pubmed-author:MiyoshiEE | lld:pubmed |
| pubmed-article:9482919 | pubmed:author | pubmed-author:ToyosawaSS | lld:pubmed |
| pubmed-article:9482919 | pubmed:author | pubmed-author:SultanA SAS | lld:pubmed |
| pubmed-article:9482919 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:9482919 | pubmed:day | 3 | lld:pubmed |
| pubmed-article:9482919 | pubmed:volume | 95 | lld:pubmed |
| pubmed-article:9482919 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:9482919 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:9482919 | pubmed:pagination | 2526-30 | lld:pubmed |
| pubmed-article:9482919 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:9482919 | pubmed:meshHeading | pubmed-meshheading:9482919-... | lld:pubmed |
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| pubmed-article:9482919 | pubmed:meshHeading | pubmed-meshheading:9482919-... | lld:pubmed |
| pubmed-article:9482919 | pubmed:year | 1998 | lld:pubmed |
| pubmed-article:9482919 | pubmed:articleTitle | Ectopic expression of N-acetylglucosaminyltransferase III in transgenic hepatocytes disrupts apolipoprotein B secretion and induces aberrant cellular morphology with lipid storage. | lld:pubmed |
| pubmed-article:9482919 | pubmed:affiliation | Department of Biochemistry, Osaka University Medical School, 2-2 Yamadaoka, 1-8 Yamadaoka, Suita, Osaka 565, Japan. | lld:pubmed |
