Switch to
| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
7
|
| pubmed:dateCreated |
1988-4-6
|
| 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.
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| pubmed:grant | |
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Antibodies, Monoclonal,
http://linkedlifedata.com/resource/pubmed/chemical/Borohydrides,
http://linkedlifedata.com/resource/pubmed/chemical/Epitopes,
http://linkedlifedata.com/resource/pubmed/chemical/Fibronectins,
http://linkedlifedata.com/resource/pubmed/chemical/Glycopeptides,
http://linkedlifedata.com/resource/pubmed/chemical/Glycoside Hydrolases,
http://linkedlifedata.com/resource/pubmed/chemical/Hexosaminidases,
http://linkedlifedata.com/resource/pubmed/chemical/NAGA protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Oligopeptides,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Fragments,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Hydrolases,
http://linkedlifedata.com/resource/pubmed/chemical/Threonine,
http://linkedlifedata.com/resource/pubmed/chemical/alpha-N-Acetylgalactosaminidase,
http://linkedlifedata.com/resource/pubmed/chemical/sodium borohydride
|
| pubmed:status |
MEDLINE
|
| pubmed:month |
Mar
|
| pubmed:issn |
0021-9258
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
5
|
| pubmed:volume |
263
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
3314-22
|
| pubmed:dateRevised |
2007-11-14
|
| pubmed:meshHeading |
pubmed-meshheading:2449438-Amino Acid Sequence,
pubmed-meshheading:2449438-Antibodies, Monoclonal,
pubmed-meshheading:2449438-Borohydrides,
pubmed-meshheading:2449438-Carbohydrate Conformation,
pubmed-meshheading:2449438-Carcinoma, Hepatocellular,
pubmed-meshheading:2449438-Chromatography,
pubmed-meshheading:2449438-Epitopes,
pubmed-meshheading:2449438-Fetus,
pubmed-meshheading:2449438-Fibronectins,
pubmed-meshheading:2449438-Glycopeptides,
pubmed-meshheading:2449438-Glycoside Hydrolases,
pubmed-meshheading:2449438-Glycosylation,
pubmed-meshheading:2449438-Hexosaminidases,
pubmed-meshheading:2449438-Humans,
pubmed-meshheading:2449438-Liver Neoplasms,
pubmed-meshheading:2449438-Molecular Sequence Data,
pubmed-meshheading:2449438-Oligopeptides,
pubmed-meshheading:2449438-Peptide Fragments,
pubmed-meshheading:2449438-Peptide Hydrolases,
pubmed-meshheading:2449438-Protein Conformation,
pubmed-meshheading:2449438-Threonine,
pubmed-meshheading:2449438-Tumor Cells, Cultured,
pubmed-meshheading:2449438-alpha-N-Acetylgalactosaminidase
|
| pubmed:year |
1988
|
| 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.
|
| pubmed:affiliation |
Program of Biochemical Oncology, Fred Hutchinson Cancer Research Center, Seattle, Washington 98119.
|
| pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
|