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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.

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Diminished expression of h2‐calponin in prostate cancer cells promotes cell proliferation, migration and the dependence of cell adhesion on substrate stiffness