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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Larsen, Jørgen K. Kjøller, Lars Madsen, Daniel H. Engelholm, Lars H. Ploug, Michael Behrendt, Niels Ingvarsen, Signe Danø, Keld Hillig, Thore Gårdsvoll, Henrik |
| Description | Author Affiliation: Hillig T ( The Finsen Laboratory, Department 37.35, Rigshospitalet, Ole Maaløes Vej 5, Copenhagen North, Denmark.) |
| Abstract | The urokinase receptor, urokinase receptor (uPAR), is a glycosylphosphatidylinositol-anchored membrane protein engaged in pericellular proteolysis and cellular adhesion, migration, and modulation of cell morphology. A direct matrix adhesion is mediated through the binding of uPAR to vitronectin, and this event is followed by downstream effects including changes in the cytoskeletal organization. However, it remains unclear whether the adhesion through uPAR-vitronectin is the only event capable of initiating these morphological rearrangements or whether lateral interactions between uPAR and integrins can induce the same response. In this report, we show that both of these triggering mechanisms can be operative and that uPAR-dependent modulation of cell morphology can indeed occur independently of a direct vitronectin binding. Expression of wild-type uPAR on HEK293 cells led to pronounced vitronectin adhesion and cytoskeletal rearrangements, whereas a mutant uPAR, uPAR(W32A) with defective vitronectin binding, failed to induce both phenomena. However, upon saturation of uPAR(W32A) with the protease ligand, pro-uPA, or its receptor-binding domain, the ability to induce cytoskeletal rearrangements was restored, although this did not rescue the uPAR-vitronectin binding and adhesion capability. On the other hand, using other uPAR variants, we could show that uPAR-vitronectin adhesion is indeed capable and sufficient to induce the same morphological rearrangements. This was shown with cells expressing a different single-site mutant, uPAR(Y57A), in the presence of a synthetic uPAR-binding peptide, as well as with wild-type uPAR, which underwent cytoskeletal rearrangements even when cultivated in uPA-deficient serum. Blocking of integrins with an Arg-Gly-Asp-containing peptide counteracted the matrix contacts necessary to initiate the uPAR-dependent cytoskeletal rearrangements, whereas inactivation of the Rac signaling pathway in all cases suppressed the occurrence of the same events. |
| ISSN | 00219258 |
| e-ISSN | 1083351X |
| Journal | Journal of Biological Chemistry |
| Issue Number | 22 |
| Volume Number | 283 |
| Language | English |
| Publisher | American Society for Biochemistry and Molecular Biology (United States) |
| Publisher Date | 2008-05-30 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | Cell Shape Physiology Cytoskeleton Metabolism Receptors, Cell Surface Urokinase-Type Plasminogen Activator Vitronectin Amino Acid Substitution Cell Adhesion Drug Effects Cell Line Cell Movement Genetics Integrins Peptides Pharmacology Protein Binding Protein Structure, Tertiary Receptors, Urokinase Plasminogen Activator Research Support, Non-U.S. Gov't Biochemistry Molecular Biology |
| Content Type | Text |
| Resource Type | Article |
| Subject | Cell Biology Biochemistry Molecular Biology |
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