Association of α2-macroglobulin-thrombin and α2-macroglobulin-plasmin complexes with isolated hepatocytes |
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Authors: | Zoltán Spolarics Jozsef Mandl Raymund Machovich Patrick Lambin Tamás Garzó Ferenc Antoni István Horváth |
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Affiliation: | 1. First and Second Institute of Biochemistry, Semmelweis University Medical School, Budapest H-1444, POB 262 Hungary;2. Centre National de Transfusion Sanguine, Paris 75739 France |
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Abstract: | 125I-labelled complexed with thrombin or plasmin bound to hepatocytes in a concentration-and time-dependent manner. The apparent values calculated from displacement experiments were 7.9 · 10?8 M for and 8.5 · 10?8 M for . Association of these complexes was only partially reversible; after a 180 min incubation period, 50–60% of the bound radioactivity was internalized by the cells. itself bound also to hepatocytes, but the affinity of the complexes was higher than that of the inhibitor alone, and was not internalized, either. 125I-labelled thrombin or plasmin bound to hepatocytes as well. These bindings were also concentration-dependent and could be decreased with an excess of unlabelled ligands. Binding rates and amounts of the bound proteinases were higher than those of their complexes. The complex competed with the complex in binding to hepatocytes, whereas there was no competition between these complexes and the antithrombin III-thrombin complex. These results suggest that the binding sites of hepatocytes for and antithrombin III-proteinase complexes are different. |
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Keywords: | Thrombin: Plasmin: Protein-protein interaction (Hepatocyte) |
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