Binding of bovine, ovine, porcine, canine, and rat plasminogen to rat hepatocytes and rat C6 glioma cells in vitro.
Plasminogens were purified by affinity chromatography from bovine, ovine, porcine, canine, and rat plasma. The binding of each plasminogen to rat hepatocytes in primary culture and to rat C6 glioma cells was studied by radiodisplacement experiments. All of the plasminogens inhibited human 125I-[Glu1]plasminogen type 2 binding to specific cell surface receptors. The IC50 values were similar. These studies suggest conservation of the receptor recognition site in plasminogens across species lines.
Hall
S W
SW
Departments of Pathology, University of Virginia Health Sciences Center, Charlottesville 22908.
Braud
L L
LL
Gonias
S L
SL
D000818:Animals; D001667:Binding, Competitive; D002417:Cattle; D002460:Cell Line; D002478:Cells, Cultured; D002846:Chromatography, Affinity; D004285:Dogs; D005260:Female; D005910:Glioma / Q000378:metabolism*; D007700:Kinetics; D008099:Liver / Q000378:metabolism*; D010958:Plasminogen / Q000302:isolation & purification / Q000378:metabolism*; D051381:Rats; D011919:Rats, Inbred Strains; D011956:Receptors, Cell Surface / Q000378:metabolism*; D055293:Receptors, Urokinase Plasminogen Activator; D012756:Sheep; D013045:Species Specificity; D013552:Swine
C524898:PLAUR protein, human; C524900:Plaur protein, rat; D011956:Receptors, Cell Surface; D055293:Receptors, Urokinase Plasminogen Activator; D010958:Plasminogen