Regulation of Integrin Function by the Urokinase Receptor
Copyright policy )Regulation of Integrin Function by the Urokinase Receptor
Integrin function is central to inflammation, immunity, and tumor progression. The urokinase-type plasminogen activator receptor (uPAR) and integrins formed stable complexes that both inhibited native integrin adhesive function and promoted adhesion to vitronectin via a ligand binding site on uPAR. Interaction of soluble uPAR with the active conformer of integrins mimicked the inhibitory effects of membrane uPAR. Both uPAR-mediated adhesion and altered integrin function were blocked by a peptide that bound to uPAR and disrupted complexes. These data provide a paradigm for regulation of integrins in which a nonintegrin membrane receptor interacts with and modifies the function of activated integrins.
- University of California, San Francisco United States
- Brigham and Women's Faulkner Hospital United States
- Chiron Corporation United States
- GENENTECH INC United States
Integrins, Glycosylphosphatidylinositols, Integrin beta1, Recombinant Fusion Proteins, Molecular Sequence Data, Receptors, Cell Surface, Receptors, Cytoadhesin, Ligands, Transfection, Urokinase-Type Plasminogen Activator, Cell Line, Fibronectins, Receptors, Urokinase Plasminogen Activator, CD18 Antigens, Cell Adhesion, Humans, Amino Acid Sequence, Vitronectin
Integrins, Glycosylphosphatidylinositols, Integrin beta1, Recombinant Fusion Proteins, Molecular Sequence Data, Receptors, Cell Surface, Receptors, Cytoadhesin, Ligands, Transfection, Urokinase-Type Plasminogen Activator, Cell Line, Fibronectins, Receptors, Urokinase Plasminogen Activator, CD18 Antigens, Cell Adhesion, Humans, Amino Acid Sequence, Vitronectin
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