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Involvement of PKA and VASP in PDGF‐induced cell migration

A wide variety of extracelluar signaling molecules utilize the cyclic AMP‐dependent protein kinase (PKA) pathway to regulate cell migration. PKA is targeted to specific sites of actin cytoskeleton reorganization and select accurate substrate to modulate actin cytoskeletal dynamics, thereby lead to migration. An actin binding protein Vasodilator‐stimulated phosphoprotein (VASP) is a substrate for PKA, which promotes nucleation and assembly of actin filaments. Phosphorylation of VASP appears to be critical for its function during cell migration. This study is to investigate the regulation of PKA and VASP to cell migration induced by Platelet‐derived growth factor (PDGF). We observed that PDGF significantly promote cell migration of ECV304 through cell scratch wound assays. Meanwhile, PDGF stimulation led to enhanced PKA activity and high phosphorylation expression of VASP analyzed by western blot. However, cell migration upon the treatment of PDGF was obviously inhibit by PKA selectivity inhibitor H‐89. Reduced PKA activity and dephosphorylation expression of VASP were also detected by adding H‐89 into PDGF pretreated cells. In addition, we examined redistribution of actin cytoskeleton and VASP induced by PDGF through immunofluorescence microscopy. After PDGF stimulation, Cells exhibited thick actin fibers, which aligned mainly in numerous elongated pseudopods along the direction of migration. Sporadic dot distribution of VASP transferred to the two extremities of actin fibers and partly accumulated at leading edge of pseudopods. These results indicate that both PKA and VASP are involved in PDGF‐induced cell migration and VASP participate in cytoskeleton reorganization during migration.