Source:http://linkedlifedata.com/resource/pubmed/id/10580127
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
2000-1-11
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pubmed:abstractText |
Glycosylation of glycoproteins and glycolipids is one of many molecular changes that accompany malignant transformation. GlcNAc-branched N-glycans and terminal Lewis antigen sequences have been observed to increase in some cancers, and to correlate with poor prognosis. Herein, we review evidence that beta1, 6GlcNAc-branching of N-glycans contributes directly to cancer progression, and we consider possible functions for the glycans. Mgat5 encodes N-acetylglucosaminyltransferase V (GlcNAc-TV), the Golgi enzyme required in the biosynthesis of beta1,6GlcNAc-branched N-glycans. Mgat5 expression is regulated by RAS-RAF-MAPK, a signaling pathway commonly activated in tumor cells. Ectopic expression of GlcNAc-TV in epithelial cells results in morphological transformation and tumor growth in mice, and over expression in carcinoma cells has been shown to induce metastatic spread. Ectopic expression of GlcNAc-TIII, an enzyme that competes with GlcNAc-TV for acceptor, suppresses metastasis in B16 melanoma cells. Furthermore, breast cancer progression and metastasis induced by a viral oncogene expressed in transgenic mice is markedly suppressed in a GlcNAc-TV-deficient background. Mgat5 gene expression and beta1, 6GlcNAc-branching of N-glycans are associated with cell motility, a required phenotype of malignant cells.
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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/Amino Sugars,
http://linkedlifedata.com/resource/pubmed/chemical/Glycolipids,
http://linkedlifedata.com/resource/pubmed/chemical/Glycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/N-Acetylglucosaminyltransferases,
http://linkedlifedata.com/resource/pubmed/chemical/Polysaccharides,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Antigen, T-Cell,
http://linkedlifedata.com/resource/pubmed/chemical/alpha-1,6-mannosylglycoprotein...,
http://linkedlifedata.com/resource/pubmed/chemical/beta-1,4-mannosyl-glycoprotein...,
http://linkedlifedata.com/resource/pubmed/chemical/polylactosamine
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
0006-3002
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
6
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pubmed:volume |
1473
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
21-34
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:10580127-Amino Sugars,
pubmed-meshheading:10580127-Animals,
pubmed-meshheading:10580127-Epithelial Cells,
pubmed-meshheading:10580127-Gene Expression Regulation, Neoplastic,
pubmed-meshheading:10580127-Glycolipids,
pubmed-meshheading:10580127-Glycoproteins,
pubmed-meshheading:10580127-Glycosylation,
pubmed-meshheading:10580127-Humans,
pubmed-meshheading:10580127-N-Acetylglucosaminyltransferases,
pubmed-meshheading:10580127-Neoplasm Metastasis,
pubmed-meshheading:10580127-Neoplasms,
pubmed-meshheading:10580127-Polysaccharides,
pubmed-meshheading:10580127-Receptors, Antigen, T-Cell,
pubmed-meshheading:10580127-Transfection,
pubmed-meshheading:10580127-Tumor Cells, Cultured
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pubmed:year |
1999
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pubmed:articleTitle |
Glycoprotein glycosylation and cancer progression.
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pubmed:affiliation |
Samuel Lunenfeld Research Institute, Mount Sinai Hospital, 600 University Ave., Rm. 876, M5G 1X5, Toronto, Ont., Canada. dennis@mshri.on.ca
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pubmed:publicationType |
Journal Article,
Review,
Research Support, Non-U.S. Gov't
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