Prostate cancer cell migration induced by myopodin isoforms is associated with formation of morphologically and biochemically distinct actin networks

摘要: Myopodin is an actin-binding protein that promotes cancer cell migration in response to serum stimulation and associated with invasive tumor development. To determine whether enhanced reflects changes actin cytoskeleton remodeling, fluorescence confocal microscopy was used examine the composition morphology of filamentous structures mock-transduced cells vs. stably transduced PC3 expressing human myopodin isoforms, chemokinetic quantified using transwell assays. The same approaches were analyze effects external stimuli, polymerization inhibitors or deletion isoform-specific amino- and/or carboxy termini on bundle formation. Results indicate isoforms differentially alter formation morphologically distinct F-actin networks also differ their myosin staining patterns. Furthermore, reduced by >50% when impaired myopodin-truncation, low concentrations inhibitor, absence stimulus. Human are therefore potent regulators stress fiber formation, inducing biochemically body whose presence directly correlates increased migration.