title: Fibrinogen alpha C domains contain cryptic plasminogen and tPA binding sites.
abstract: Surface plasmon resonance and ELISA experiments revealed that recombinant fibrinogen alpha C fragment (residues A alpha 221-610) corresponding to the alpha C domain binds tPA and plasminogen with high affinity. This binding was found to be Lys-dependent and occurred via independent binding sites. Study with truncated variants of the alpha C fragment located these sites in its COOH-terminal half. Binding of tPA and plasminogen to these sites stimulated activation of the latter whereas proteolytic degradation of the alpha C fragment reduced this effect substantially, suggesting the importance of the alpha C domains in regulation of fibrinolysis.
authors.affiliation: Biochemistry Department, Holland Laboratory, American Red Cross, 15601 Crabbs Branch Way, Rockville, MD 20855, USA. tsiouriog@usa.redcross.org
authors.forename: G
authors.initials: G
authors.lastname: Tsurupa
authors.forename: L
authors.initials: L
authors.lastname: Medved
mesh_terms: D001665:Binding Sites; D005340:Fibrinogen / Q000737:chemistry / Q000378:metabolism*; D010958:Plasminogen / Q000378:metabolism*; D010959:Tissue Plasminogen Activator / Q000378:metabolism*
chemical_list: D005340:Fibrinogen; D010958:Plasminogen; D010959:Tissue Plasminogen Activator