Abstract
The main ligand-binding determinant of the human urokinase receptor (uPAR) is located in the amino terminal domain D1, but when isolated this domain presents a 1500 fold lower affinity than the intact three-domain uPAR (D1D2D3). uPAR mutants missing either domain 2 (D1HD3) or domain 3 (D1D2) were expressed in murine LB6 cells and showed to be properly GPI-anchored to the cell surface. Binding assays with [125I]ATF demonstrated that these mutants possessed a normal (D1D2) or slightly reduced (D1HD3) affinity, indicating that a high ligand-affinity may be achieved by a combination of D1 with domain D2 or D3.
Publication types
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Comparative Study
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Animals
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Base Sequence
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Binding Sites
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Clone Cells
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Fluorescent Antibody Technique
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Glycosylphosphatidylinositols / metabolism
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Humans
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Kinetics
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L Cells
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Ligands
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Mice
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Molecular Sequence Data
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Mutagenesis
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Mutagenesis, Insertional
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Phosphatidylinositol Diacylglycerol-Lyase
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Phosphoric Diester Hydrolases / biosynthesis
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Phosphoric Diester Hydrolases / metabolism
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Phosphoric Diester Hydrolases / pharmacology
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Receptors, Cell Surface / biosynthesis
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Receptors, Cell Surface / isolation & purification
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Receptors, Cell Surface / metabolism*
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Receptors, Urokinase Plasminogen Activator
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Recombinant Proteins / biosynthesis
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Recombinant Proteins / isolation & purification
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Recombinant Proteins / metabolism
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Transfection
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Urokinase-Type Plasminogen Activator / metabolism
Substances
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Glycosylphosphatidylinositols
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Ligands
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PLAUR protein, human
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Plaur protein, mouse
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Receptors, Cell Surface
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Receptors, Urokinase Plasminogen Activator
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Recombinant Proteins
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Phosphoric Diester Hydrolases
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Urokinase-Type Plasminogen Activator
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Phosphatidylinositol Diacylglycerol-Lyase