Binding of tissue plasminogen activator to human umbilical vein endothelial cells |
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| Authors: | D P Beebe |
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| Affiliation: | 1. Stockholm University, Department of Physical Geography and Bolin Centre for Climate Research, SE-106 91 Stockholm, Sweden;2. CERNAS, Agrarian School of Coimbra, Polytechnic Institute of Coimbra, Coimbra, Portugal;3. Trivector, Sweden;4. Soil Erosion and Degradation Research Group, Department of Geography, University of Valencia, Valencia, Spain;1. Manufacturing and Industrial Management Department, University of Pitesti, Pitesti, Romania;2. IRDL-UMR CNRS 6027, Univ. Bretagne Occidentale, F-29600 Morlaix, France;3. IRDL-UMR CNRS 6027, ENSTA Bretagne, F-29200 Brest, France;4. Institut Pascal, UMR 6602, Université Clermont Auvergne, CNRS, SIGMA Clermont Institut Pascal, Clermont-Ferrand, France;5. UMR CNRS 5510, Laboratoire MATEIS, University Lyon, INSA Lyon, Villeurbanne, France |
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| Abstract: | Binding of purified recombinant human tissue plasminogen activator to cultures of human umbilical vein endothelial cells (HUVEC) was studied in vitro. 125I-tPA was shown to bind to HUVEC in a specific, saturable, and dissociable manner. Scatchard analysis revealed a low affinity binding site with Keq = 4.2 X 10(6) M-1 and 1.2 X 10(7) sites per cell. Binding of tPA was inhibited by L-lysine, e-aminocaproic acid, and D-phenylalanyl-L-prolyl-L-arginine chloromethyl ketone but not by carbohydrates including mannose, galactose, N-acetyl glucosamine and N-acetyl galactosamine. Neat human plasma abrogates but does not totally inhibit binding of tPA to HUVEC. These results may indicate a role for endothelial cells in the removal of tPA from the circulation in vivo. |
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