| pubmed-article:10580127 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:10580127 | lifeskim:mentions | umls-concept:C0017968 | lld:lifeskim |
| pubmed-article:10580127 | lifeskim:mentions | umls-concept:C1947901 | lld:lifeskim |
| pubmed-article:10580127 | lifeskim:mentions | umls-concept:C0017982 | lld:lifeskim |
| pubmed-article:10580127 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:10580127 | pubmed:dateCreated | 2000-1-11 | lld:pubmed |
| pubmed-article:10580127 | 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. | lld:pubmed |
| pubmed-article:10580127 | pubmed:language | eng | lld:pubmed |
| pubmed-article:10580127 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10580127 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:10580127 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:10580127 | pubmed:month | Dec | lld:pubmed |
| pubmed-article:10580127 | pubmed:issn | 0006-3002 | lld:pubmed |
| pubmed-article:10580127 | pubmed:author | pubmed-author:WarrenC ECE | lld:pubmed |
| pubmed-article:10580127 | pubmed:author | pubmed-author:DennisJ WJW | lld:pubmed |
| pubmed-article:10580127 | pubmed:author | pubmed-author:GranovskyMM | lld:pubmed |
| pubmed-article:10580127 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:10580127 | pubmed:day | 6 | lld:pubmed |
| pubmed-article:10580127 | pubmed:volume | 1473 | lld:pubmed |
| pubmed-article:10580127 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:10580127 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:10580127 | pubmed:pagination | 21-34 | lld:pubmed |
| pubmed-article:10580127 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
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| pubmed-article:10580127 | pubmed:year | 1999 | lld:pubmed |
| pubmed-article:10580127 | pubmed:articleTitle | Glycoprotein glycosylation and cancer progression. | lld:pubmed |
| pubmed-article:10580127 | pubmed:affiliation | Samuel Lunenfeld Research Institute, Mount Sinai Hospital, 600 University Ave., Rm. 876, M5G 1X5, Toronto, Ont., Canada. dennis@mshri.on.ca | lld:pubmed |
| pubmed-article:10580127 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:10580127 | pubmed:publicationType | Review | lld:pubmed |
| pubmed-article:10580127 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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