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pubmed-article:1280266pubmed:abstractTextWe 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.lld:pubmed
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pubmed-article:1280266pubmed:dateRevised2006-11-15lld:pubmed
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pubmed-article:1280266pubmed:articleTitleThe inclusion of the type III repeat ED-B in the fibronectin molecule generates conformational modifications that unmask a cryptic sequence.lld:pubmed
pubmed-article:1280266pubmed:affiliationLaboratory of Cell Biology, Istituto Nazionale per la Ricerca sul Cancro, Genoa, Italy.lld:pubmed
pubmed-article:1280266pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:1280266pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed
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