AI Article Synopsis
- Cancer spread begins when cells enter blood vessels, often triggered by a process called epithelial to mesenchymal transition (EMT).
- Proteases, particularly plasmin, play a crucial role in remodeling the extracellular matrix, which is essential for cell movement and invasion.
- The study links EMT and the plasminogen activation system, showing that TGFβ1 signaling and FOXC2 influence plasminogen activation and related proteins, impacting cell invasion dynamics.
Article Abstract
Cancer dissemination is initiated by the movement of cells into the vasculature which has been reported to be triggered by EMT (epithelial to mesenchymal transition). Cellular dissemination also requires proteases that remodel the extracellular matrix. The protease, plasmin is a prominent player in matrix remodeling and invasion. Despite the contribution of both EMT and the plasminogen activation (PA) system to cell dissemination, these processes have never been functionally linked. We reveal that canonical Smad-dependent TGFβ1 signaling and FOXC2-mediated PI3K signaling in cells undergoing EMT reciprocally modulate plasminogen activation partly by regulating the plasminogen receptor, S100A10 and the plasminogen activation inhibitor, PAI-1. Plasminogen activation and plasminogen-dependent invasion were more prominent in epithelial-like cells and were partly dictated by the expression of S100A10 and PAI-1.
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| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC6148250 | PMC |
| http://dx.doi.org/10.1038/s41598-018-32433-y | DOI Listing |
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