Maspin is physically associated with β1 integrin regulating cell adhesion in mammary epithelial cells

Nathalie Cella*, Alejandro Contreras, Khatri Latha, Jeffrey M. Rosen, Ming Zhang

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

55 Scopus citations

Abstract

Maspin is a tumor-suppressor serpin (serine protease inhibitor), which inhibits cell invasion and migration. Here, we analyzed maspin function in cell adhesion in nontransformed mammary epithelial cells and investigated the underlying mechanism involved in this process. We report that maspin acts in the early steps in the cell adhesion process. Addition of recombinant maspin rapidly increased MCF-10A cell adhesion to the endogenously deposited matrix, and conversely both an antimaspin antibody (Ab) and maspin knockdown by RNA interference resulted in decreased cell adhesion. Mutation analyses revealed that a region of 86 amino acids located between aa 139 and aa 225 was responsible for maspin effect on adhesion. In addition, we show that maspin is associated with detergent-insoluble cortical cytoskeleton elements. Collectively, these results suggest that maspin is part of the supramolecular structure of the adhesion plaque and it modulates cell adhesion via a β1 integrin-dependent mechanism.

Original languageEnglish (US)
Pages (from-to)E721-E731
JournalFASEB Journal
Volume20
Issue number9
DOIs
StatePublished - Jul 2006

Keywords

  • Cell adhesion
  • ECM
  • Maspin
  • RSL
  • β1 integrin

ASJC Scopus subject areas

  • Biotechnology
  • Biochemistry
  • Molecular Biology
  • Genetics

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