Premium
PTEN signaling modulates lung epithelial cells migration and wound repair through changes in cellular mechanics
Author(s) -
Mihai Cosmin,
Zielinski Rachel,
Bao Shaoying,
Knoell Daren,
Ghadiali Samir
Publication year - 2011
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.25.1_supplement.659.10
Subject(s) - pten , protein kinase b , pi3k/akt/mtor pathway , cell migration , chemistry , microbiology and biotechnology , cell , cancer research , signal transduction , biology , biochemistry
The PI3K/Akt pathway is a vital component of survival in lung epithelia. Previous work by our group indicates that pharmacological inhibition of PTEN, a major suppressor of this pathway, results in enhanced wound repair and cell migration following lung injury. However, the precise biomechanical mechanisms responsible for enhanced wound repair are not known. In this study, we used atomic force microscopy (AFM) and traction force microscopy (TFM) to characterize the biomechanical effects of PTEN inhibition in a bronchial epithelial cell line (BEAS2B). PTEN inhibition was found to induce a significant decrease in both cell stiffness and the power‐law exponent which indicates that PTEN‐inhibited cells behave more like a soft‐elastic‐solid than a viscous‐fluid. TFM measurements revealed that PTEN inhibited cells exhibited decreased contractility, consistent with weaker adhesion and increased migration. Concurrent inhibition of both PTEN activity and Akt phosphorylation resulted in viscoelasticity profiles similar to those obtained in control samples. These results indicate that enhanced cell migration and wound repair during PTEN inhibition is due to changes in the cell's biomechanical properties. In addition, these changes in cell mechanics appear to be mediated by Akt signaling pathways. Thus, Akt pathways may represent a novel target for wound repair following lung injury. Supported by NSF 0852417.