[Crucial roles of PECAM-1 in shear stress sensing of vascular endothelial cells].
Fluid shear stress (FSS) induces many forms of responses, including phosphorylation of ERK in endothelial cells (ECs). We have earlier reported that FSS and hyper-osmotic shock rapidly induce tyrosine phosphorylation of PECAM-1 (CD31). The phosphorylated PECAM-1 acts as a plasma membrane anchoring site for SHP2, a protein tyrosine phosphatase involved in the signal transmission from receptor tyrosine kinases to ERK. Osmotic shock also induces transient ERK activation in ECs. The osmotic-shock-induced ERK activation but not p38 MAP kinase activation was dependent on the PECAM-1 engagement and was blocked by its downregulation. When magnetic beads coated with antibodies against the extracellular domain of PECAM-1 were attached to ECs and tugged by magnetic force, PECAM-1 associated with the beads was tyrosine phosphorylated. ERK was also phosphorylated in these cells. Binding of the beads by itself or pulling on the cell surface using poly-L-lysine coated beads did not induce phosphorylation of PECAM-1 and ERK. These results suggest that PECAM-1 is a mechanotransduction molecule.
Masuda
Michitaka
M
Department of Structural Analysis, National Cardiovascular Center Research Institute.
Kogata
Naoko
N
Mochizuki
Naoki
N
D000818:Animals; D042783:Endothelial Cells / Q000502:physiology*; D008465:Mechanoreceptors / Q000502:physiology*; D040542:Mechanotransduction, Cellular / Q000502:physiology; D008962:Models, Theoretical; D010766:Phosphorylation; D019408:Platelet Endothelial Cell Adhesion Molecule-1 / Q000502:physiology*; D015398:Signal Transduction / Q000502:physiology; D013718:Tensile Strength; D014443:Tyrosine / Q000378:metabolism
D019408:Platelet Endothelial Cell Adhesion Molecule-1; D014443:Tyrosine