EXPRESSION AND LOCATION OF VASP IN HUMAN ENDOTHELIAL CELLS. EFFECT OF A LAMINAR SHEAR STRESS

Recent elucidation of the primary VASP (vasodilator-simulated phosphoprotein) and identity of VASP binding proteins suggests that VASP is an important component of focal contacts which links signal transduction pathways and elements controlling cell motility. The aim of our study was to evaluate shear-stress-induced changes of VASP expression and localization in ECs. We showed, by western blotting measurements, that the shear stress involve some modifications on the expression of phosphorilated (50 kD) and non phosphorilated (46kD) VASP. Moreover, a fluorescence double-labeling shows the location of VASP on the actin fibers. At rest, ECs showed an array of microfilament bundles of the actin fibers and VASP were along their entire length. After exposure to shear stress, the stress fibers appeared and were oriented along with the flow. There were a thicker expression of VASP than in control, targeted to the ends of stress fibres. This seems to be an adjustment of the cells towards the mechanical stresses. These results suggest that VASP is a potential important component which participates in the regulation of cell actin remodelling induced by shear flow. VASP were involved in the mechano-transduction pathways.