Determination of the vitronectin binding site on plasminogen activator inhibitor 1 (PAI-1)
Autor: | Marja van Meijer, Raymond Klein Gebbink, Hans Pannekoek, Klaus T. Preissner |
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Přispěvatelé: | Other departments |
Rok vydání: | 1994 |
Předmět: |
medicine.drug_class
Biophysics PAI-1 Monoclonal antibody Biochemistry Tissue plasminogen activator Epitope chemistry.chemical_compound Epitopes Structural Biology Plasminogen Activator Inhibitor 1 Genetics medicine Humans Point Mutation Amino Acid Sequence Vitronectin Binding site Molecular Biology Glycoproteins chemistry.chemical_classification Extracellular Matrix Proteins Binding Sites biology Ligand binding assay Fibrinolysis Thrombin Antibodies Monoclonal Cell Biology Molecular biology Recombinant Proteins Amino acid body regions Kinetics chemistry Plasminogen activator inhibitor-1 Tissue Plasminogen Activator biology.protein Mutagenesis Site-Directed biological phenomena cell phenomena and immunity medicine.drug |
Zdroj: | FEBS letters, 352(3), 342-346. Wiley-Blackwell |
ISSN: | 0014-5793 |
Popis: | Vitronectin is the carrier protein of plasminogen activator inhibitor 1 (PAI-1). We used a well-characterized panel of anti-human PAI-1 monoclonal antibodies (MoAbs) to localize the vitronectin-binding site on PAI-1. By employing a direct vitronectin/PAI-1 binding assay and two vitronectin-dependent inhibition assays, we demonstrate that the anti-PAI-1 MoAbs CLB-5, CLB-10, CLB-2C8 and I1, directed against different epitopes in the region between amino acids 110 and 145, prevent the interaction of PAI-1 with vitronectin. We conclude that the region between amino acids 110 and 145 of PAI-1 harbours an important determinant for the interaction with vitronectin. |
Databáze: | OpenAIRE |
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