| pubmed-article:2449438 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:2449438 | lifeskim:mentions | umls-concept:C0086418 | lld:lifeskim |
| pubmed-article:2449438 | lifeskim:mentions | umls-concept:C0016055 | lld:lifeskim |
| pubmed-article:2449438 | lifeskim:mentions | umls-concept:C0003250 | lld:lifeskim |
| pubmed-article:2449438 | lifeskim:mentions | umls-concept:C0003317 | lld:lifeskim |
| pubmed-article:2449438 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:2449438 | lifeskim:mentions | umls-concept:C1999230 | lld:lifeskim |
| pubmed-article:2449438 | lifeskim:mentions | umls-concept:C1710548 | lld:lifeskim |
| pubmed-article:2449438 | lifeskim:mentions | umls-concept:C1704788 | lld:lifeskim |
| pubmed-article:2449438 | lifeskim:mentions | umls-concept:C1514873 | lld:lifeskim |
| pubmed-article:2449438 | pubmed:issue | 7 | lld:pubmed |
| pubmed-article:2449438 | pubmed:dateCreated | 1988-4-6 | lld:pubmed |
| pubmed-article:2449438 | pubmed:abstractText | Previously, monoclonal antibody FDC-6 was established, which defines a structure specific for fibronectins isolated from fetal and malignant cells and tissues. The presence of the FDC-6-defined structure at type III connecting segment (III CS) is characteristic of oncofetal fibronectin (onf-FN), and its absence is characteristic of normal fibronectin (nor-FN) (Matsuura, H., and Hakomori, S. (1985) Proc. Natl. Acad. Sci. U. S. A. 82, 6517-6521). Hepatoma fibronectin was sequentially digested by various proteases, followed by subsequent chromatography on an FDC-6 affinity column and reverse-phase columns at each step of digestion. A single strongly active glycosylhexapeptide (glycopeptide 1) and an inactive glycosylpentapeptide (glycopeptide 3) were isolated from glycopeptide A containing 35 amino acid residues. The minimum essential structure required for the FDC-6 activity was found to be a hexapeptide sequence Val-Thr-His-Pro-Gly-Tyr having NeuAc alpha 2----3Gal beta 1----3GalNAc or its core (Gal beta 1----3GalNAc or GalNAc) linked at threonine. Various synthetic peptides including the Val-Thr-His-Pro-Gly-Tyr sequence and a glycopeptide having the Val-Thr-His-Pro-Gly pentapeptide with the same glycosylation at threonine were all inactive. Elimination of sialic acid slightly increased the activity, and subsequent elimination of galactose did not alter the activity; however, removal of the Gal beta 1----3GalNAc residue by endo-alpha-N-acetylgalactosaminidase from desialylated glycopeptide A resulted in total inactivation of the reactivity with FDC-6 antibody. Thus, a single glycosylation at a defined threonine residue of the III CS region may induce conformational changes in the peptide to form the specific oncofetal epitope recognized by FDC-6 antibody. This finding opens the possibility that a number of other oncofetal epitopes consist of a peptide and a common O-linked carbohydrate and that the combination produces a conformation specific to cancer or to a stage of development. | lld:pubmed |
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| pubmed-article:2449438 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:2449438 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:2449438 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:2449438 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:2449438 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:2449438 | pubmed:author | pubmed-author:HakomoriSS | lld:pubmed |
| pubmed-article:2449438 | pubmed:author | pubmed-author:MatsuuraHH | lld:pubmed |
| pubmed-article:2449438 | pubmed:author | pubmed-author:TitaniKK | lld:pubmed |
| pubmed-article:2449438 | pubmed:author | pubmed-author:GreeneTT | lld:pubmed |
| pubmed-article:2449438 | pubmed:author | pubmed-author:LeveryS BSB | lld:pubmed |
| pubmed-article:2449438 | pubmed:author | pubmed-author:TakioKK | lld:pubmed |
| pubmed-article:2449438 | pubmed:author | pubmed-author:SalyanM EME | lld:pubmed |
| pubmed-article:2449438 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:2449438 | pubmed:day | 5 | lld:pubmed |
| pubmed-article:2449438 | pubmed:volume | 263 | lld:pubmed |
| pubmed-article:2449438 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:2449438 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:2449438 | pubmed:pagination | 3314-22 | lld:pubmed |
| pubmed-article:2449438 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
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| pubmed-article:2449438 | pubmed:year | 1988 | lld:pubmed |
| pubmed-article:2449438 | pubmed:articleTitle | The oncofetal structure of human fibronectin defined by monoclonal antibody FDC-6. Unique structural requirement for the antigenic specificity provided by a glycosylhexapeptide. | lld:pubmed |
| pubmed-article:2449438 | pubmed:affiliation | Program of Biochemical Oncology, Fred Hutchinson Cancer Research Center, Seattle, Washington 98119. | lld:pubmed |
| pubmed-article:2449438 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:2449438 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:2449438 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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