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Maspin, the molecular bridge between the plasminogen activator system and beta1 integrin that facilitates cell adhesion. J Biol Chem 2011 Jul 15;286(28):24599-607

Date

05/25/2011

Pubmed ID

21606500

Pubmed Central ID

PMC3137035

DOI

10.1074/jbc.M111.235788

Scopus ID

2-s2.0-79960129686 (requires institutional sign-in at Scopus site)   28 Citations

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.

Author List

Endsley MP, Hu Y, Deng Y, He X, Warejcka DJ, Twining SS, Gonias SL, Zhang M

Author

Sally S. Twining PhD Assistant Dean, Professor in the Biochemistry department at Medical College of Wisconsin




MESH terms used to index this publication - Major topics in bold

Cell Adhesion
Cell Line, Transformed
Epithelial Cells
Humans
Integrin beta1
Multiprotein Complexes
Receptors, Urokinase Plasminogen Activator
Serpins