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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
34
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pubmed:dateCreated |
1992-12-30
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pubmed:abstractText |
We have previously reported an anti-fibronectin monoclonal antibody (mAb) (BC-1) which reacts with an ED-B-containing beta-galactosidase-fibronectin fusion protein but not with an identical beta-galactosidase-fibronectin fusion protein in which the ED-B sequence is omitted. In further experiments aimed at localizing more precisely the epitope recognized by this mAb, we demonstrate that 1) the mAb BC-1 is indeed specific for ED-B-containing fibronectin (FN) molecules even though the epitope recognized by this mAb is localized on the type III homology repeat 7 (the one which precedes the ED-B sequence) and 2) in fibronectin molecules lacking the ED-B sequence, this epitope is masked. We further demonstrate that, to mask the epitope recognized by the mAb BC-1, the presence of at least half of the FN type III homology repeat 9 is necessary. We also report the production of the mAb IST-6 which recognizes only FN molecules in which the ED-B sequence is lacking. These data clearly demonstrate that the presence of the ED-B sequence within FN molecules generates conformational modification in the central part of the molecules that unmasks previously cryptic sequences and masks others.
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pubmed:commentsCorrections | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Antibodies, Monoclonal,
http://linkedlifedata.com/resource/pubmed/chemical/Epitopes,
http://linkedlifedata.com/resource/pubmed/chemical/Fibronectins,
http://linkedlifedata.com/resource/pubmed/chemical/Macromolecular Substances,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/beta-Galactosidase
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
0021-9258
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
5
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pubmed:volume |
267
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
24689-92
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:1280266-Amino Acid Sequence,
pubmed-meshheading:1280266-Antibodies, Monoclonal,
pubmed-meshheading:1280266-Cell Line,
pubmed-meshheading:1280266-Cell Line, Transformed,
pubmed-meshheading:1280266-Cloning, Molecular,
pubmed-meshheading:1280266-Epitopes,
pubmed-meshheading:1280266-Escherichia coli,
pubmed-meshheading:1280266-Fibronectins,
pubmed-meshheading:1280266-Humans,
pubmed-meshheading:1280266-Immunoenzyme Techniques,
pubmed-meshheading:1280266-Macromolecular Substances,
pubmed-meshheading:1280266-Protein Conformation,
pubmed-meshheading:1280266-Radioimmunoassay,
pubmed-meshheading:1280266-Recombinant Fusion Proteins,
pubmed-meshheading:1280266-Repetitive Sequences, Nucleic Acid,
pubmed-meshheading:1280266-Sequence Homology, Amino Acid,
pubmed-meshheading:1280266-beta-Galactosidase
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pubmed:year |
1992
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pubmed:articleTitle |
The inclusion of the type III repeat ED-B in the fibronectin molecule generates conformational modifications that unmask a cryptic sequence.
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pubmed:affiliation |
Laboratory of Cell Biology, Istituto Nazionale per la Ricerca sul Cancro, Genoa, Italy.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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