Abstract
Calponin is an actin filament-associated protein and its h2 isoform inhibits cell motility. Here we report significant expression of h2-calponin in prostate epithelial cells, which is diminished in cancerous cells. Comparison between a prostate cancer cell line PC3 and its metastatic derivative PC3-M showed lower levels of h2-calponin in PC3-M, corresponding to faster rates of cell proliferation and migration. Substrate adhesion of PC3 and PC3-M cells was positively correlated to the level of h2-calponin and the adhesion of PC3-M exhibited a higher dependence on substrate stiffness. Such effects of h2-calponin on cell proliferation, migration and substrate adhesion were also seen in normal versus cancerous primary prostate cells. Further supporting the role of h2-calponin in inhibiting cell motility, fibroblasts isolated from h2-calponin knockout mice proliferated and migrated faster than that of wild type fibroblasts. Transfective over-expression of h2-calponin in PC3-M cells effectively inhibited cell proliferation and migration. The results suggest that the diminished expression of h2-calponin in prostate cancer cells increases cell motility, decreases substrate adhesion, and promotes adhesion on high stiffness substrates.
Original language | English (US) |
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Pages (from-to) | 627-636 |
Number of pages | 10 |
Journal | FEBS Open Bio |
Volume | 4 |
DOIs | |
State | Published - 2014 |
Externally published | Yes |
Keywords
- Cell motility
- Cytoskeleton
- H2-calponin
- Mechanical regulation
- Substrate stiffness
ASJC Scopus subject areas
- General Biochemistry, Genetics and Molecular Biology