Characterization of murine peritoneal macrophage receptors for fibrin(ogen) degradation products.
The binding of human fibrinogen degradation fragments D1, E, X, and Y, as well as fibrin fragment D1 dimer, to mouse peritoneal macrophages was examined. A Scatchard plot of fragment D1 binding was biphasic, suggesting two classes of receptors. Fragments D1, D1 dimer, X, and Y in low concentrations bound to macrophages with high affinity (Kd = 23 to 73 X 10(-11) mol/L). Fragment E bound specifically but at a much lower level than the other fragments. Fragment D1 was able to compete for the binding of radiolabeled fragments X and Y but not radiolabeled fragment E. These studies indicate that fragments D and E are recognized by separate receptor systems but that all of the fibrinogen degradation products that contain the D domain are recognized by the same receptor system.
D000818:Animals; D001202:Ascitic Fluid; D001667:Binding, Competitive; D002851:Chromatography, High Pressure Liquid; D005338:Fibrin Fibrinogen Degradation Products / Q000378:metabolism*; D007700:Kinetics; D046911:Macromolecular Substances; D008264:Macrophages / Q000378:metabolism*; D051379:Mice; D011956:Receptors, Cell Surface / Q000378:metabolism*; D018000:Receptors, Peptide
D005338:Fibrin Fibrinogen Degradation Products; D046911:Macromolecular Substances; D011956:Receptors, Cell Surface; D018000:Receptors, Peptide; C048650:fibrin-fibrinogen degradation products receptor; C015214:fibrinogen D fragment; C018543:fibrinogen fragment E; C030568:fibrinogen fragment X; C036129:fibrinogen fragment Y