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The Capital Region of Denmark - a part of Copenhagen University Hospital
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Cell-induced potentiation of the plasminogen activation system is abolished by a monoclonal antibody that recognizes the NH2-terminal domain of the urokinase receptor

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  4. Disorder in a two-domain neuronal Ca2+-binding protein regulates domain stability and dynamics using ligand mimicry

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  5. ANGPTL4 inactivates lipoprotein lipase by catalyzing the irreversible unfolding of LPL's hydrolase domain

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We have raised four monoclonal antibodies recognizing different epitopes within the human cell-surface receptor for urokinase-type plasminogen activator (u-PA). One of these antibodies completely abolishes the potentiation of plasmin generation observed upon incubation of the zymogens pro-u-PA and plasminogen with U937 cells. This antibody, which is also the only one to completely inhibit the binding of DFP-inactivated [125I]-u-PA to U937 cells, is directed against the u-PA binding NH2-terminal domain of u-PAR, a well-defined fragment formed by limited chymotrypsin digestion of purified u-PAR, demonstrating the functional independence of the u-PA binding domain as well as the critical role of u-PAR in the assembly of the cell-surface plasminogen activation system.

Original languageEnglish
JournalF E B S Letters
Volume288
Issue number1-2
Pages (from-to)233-6
Number of pages4
ISSN0014-5793
Publication statusPublished - 19 Aug 1991

    Research areas

  • Antibodies, Monoclonal, Cell Line, Chymotrypsin, Epitopes, Fibrinolysin, Humans, Kinetics, Plasminogen, Plasminogen Activators, Precipitin Tests, Receptors, Cell Surface, Receptors, Urokinase Plasminogen Activator, Structure-Activity Relationship

ID: 46434738