Abstract：
:We report that the 12,000 dalton domain of fibronectin that interacts with fibroblast cell surfaces also binds specifically to thrombin-inducible, saturable receptors on platelets. Furthermore, we have used chemical cross-linking and monoclonal antibodies to show that the 12,000 dalton domain of fibronectin interacts directly with glycoprotein IIIa at the platelet cell surface. Both binding and cross-linking of this domain to platelets are competed by a hexapeptide previously shown to block fibroblast adhesion to fibronectin. Finally, we show that a complex of the platelet glycoproteins IIIa and IIb binds to affinity columns of a cell-attachment fragment of fibronectin. These results localize a major fibronectin-platelet interaction to a specific domain of fibronectin and to a specific platelet glycoprotein.
journal_name
Celljournal_title
Cellauthors
Gardner JM,Hynes ROdoi
10.1016/0092-8674(85)90101-1subject
Has Abstractpub_date
1985-09-01 00:00:00pages
439-48issue
2eissn
0092-8674issn
1097-4172pii
0092-8674(85)90101-1journal_volume
42pub_type
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