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| Content Provider | Journal of Biological Chemistry (JBC) |
|---|---|
| Author | Ghosh, Supurna Brown, Renee Jones, Jonathan C. R. Ellerbroek, Shawn M. Stack, M. Sharon |
| Abstract | Expression of urinary-type plasminogen activator (uPA) and its receptor (uPAR) is correlated with matrix proteolysis, cell adhesion, motility, and invasion. To evaluate the functional link between adhesion and proteolysis in gingival keratinocytes (pp126), cells were treated with immobilized integrin antibodies to induce integrin clustering. Clustering of α3 and β1 integrin subunits, but not α2, α5, α6, or β4, enhanced uPA secretion. Bead-immobilized laminin-5 and collagen I, two major α3β1 ligands, also induced uPA expression. Coordinate regulation of the serpin plasminogen activator inhibitor 1 was also apparent; however, a net increase in uPA activity was predominant. α3β1 integrin clustering induced extracellular signal-regulated kinase 1/2 phosphorylation, and both uPA induction and extracellular signal-regulated kinase activation were blocked by the mitogen-activated protein kinase/extracellular signal-regulated kinase kinase inhibitor PD98059. Integrin aggregation also promoted a dramatic redistribution of uPAR on the cell surface to sites of clustered α3β1 integrins. Co-immunoprecipitation of β1 integrin with uPAR provided further evidence that protein-protein interactions between uPAR and β1 integrin control uPAR distribution. As a functional consequence of uPA up-regulation and uPA-mediated plasminogen activation, the globular domain of the laminin-5 α3subunit, a major pp126 matrix protein, was proteolytically processed from a 190-kDa form to a 160-kDa species. Laminin-5 containing the 160-kDa α3 subunit efficiently nucleates hemidesmosome formation and reduces cell motility. Together, these data suggest that multivalent aggregation of the α3β1integrin regulates proteinase expression, matrix proteolysis, and subsequent cellular behavior. |
| Related Links | http://www.jbc.org/content/275/31/23869.abstract |
| Ending Page | 23876 |
| Starting Page | 23869 |
| Page Count | 8 |
| File Format | HTM / HTML PDF |
| ISSN | 00219258 |
| Journal | Journal of Biological Chemistry (JBC) |
| Issue Number | 31 |
| Volume Number | 275 |
| DOI | 10.1074/jbc.M000935200 |
| e-ISSN | 1083351X |
| Language | English |
| Publisher | American Society for Biochemistry and Molecular Biology |
| Publisher Date | 2000-08-04 |
| Access Restriction | Open |
| Subject Keyword | Urinary-type plasminogen activator (uPA) Bovine pituitary extract (BPE) Bovine serum albumin (BSA) Extracellular matrix (ECM) Epidermal growth factor (EGF) Enzyme-linked immunosorbent assay (ELISA) Extracellular signal-regulated kinase (ERK) Mitogen-activated protein kinase (MAPK) Mitogen-activated protein kinase/extracellular signal-regulated kinase kinase (MEK) Serpin plasminogen activator inhibitor (PAI) Phosphate-buffered saline (PBS) UPA receptor (uPAR) Receptor-bound uPA (uPA/R) ENZYME CATALYSIS AND REGULATION |
| Content Type | Text |
| Resource Type | Article |
| Subject | Cell Biology Biochemistry Molecular Biology |
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