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Maspin, the Molecular Bridge between the Plasminogen Activator System and β1 Integrin That Facilitates Cell Adhesion
- Source :
- Journal of Biological Chemistry. 286:24599-24607
- Publication Year :
- 2011
- Publisher :
- Elsevier BV, 2011.
-
Abstract
- Maspin is a non-inhibitory serine protease inhibitor (serpin) that influences many cellular functions including adhesion, migration, and invasion. The underlying molecular mechanisms that facilitate these actions are still being elucidated. In this study we determined the mechanism by which maspin mediates increased MCF10A cell adhesion. Utilizing competition peptides and mutation analyses, we discovered two unique regions (amino acid residues 190–202 and 260–275) involved in facilitating the increased adhesion function of maspin. In addition, we demonstrate that the urokinase-type plasminogen activator (uPA)/uPA receptor (uPAR) complex is required for the localization and adhesion function of maspin. Finally, we showed that maspin, uPAR, and β1 integrin co-immunoprecipitate, suggesting a novel maspin-uPA-uPAR-β1 integrin mega-complex that regulates mammary epithelial cell adhesion.
- Subjects :
- Integrin beta1
Integrin
Maspin
Epithelial Cells
Cell Biology
Adhesion
Serpin
Biology
Biochemistry
Molecular biology
Receptors, Urokinase Plasminogen Activator
Cell biology
Urokinase receptor
Multiprotein Complexes
Cell Adhesion
biology.protein
Humans
Signal transduction
Cell adhesion
Molecular Biology
Plasminogen activator
Serpins
Cell Line, Transformed
Signal Transduction
Subjects
Details
- ISSN :
- 00219258
- Volume :
- 286
- Database :
- OpenAIRE
- Journal :
- Journal of Biological Chemistry
- Accession number :
- edsair.doi.dedup.....cd576700e1da1da48f8cec1e28711154