Role of lateral cell-cell border location and extracellular/transmembrane domains in PECAM/CD31 mechanosensation

Biochemical and Biophysical Research Communications
David A KaufmanPeter F Davies

Abstract

Phosphorylation of tyrosine residues on platelet-endothelial cell adhesion molecule-1 (PECAM-1), followed by signal transduction events, has been described in endothelial cells following exposure to hyperosmotic and fluid shear stress. However, it is unclear whether PECAM-1 functions as a primary mechanosensor in this process. Utilizing a PECAM-1-null EC-like cell line, we examined the importance of cellular localization and the extracellular and transmembrane domains in PECAM-1 phosphorylation responses to mechanical stress. Tyrosine phosphorylation of PECAM-1 was stimulated in response to mechanical stress in null cells transfected either with full length PECAM-1 or with PECAM-1 mutants that do not localize to the lateral cell-cell adhesion site and that do not support homophilic binding between PECAM-1 molecules. Furthermore, null cells transfected with a construct that contains the intact cytoplasmic domain of PECAM-1 fused to the extracellular and transmembrane domains of the interleukin-2 receptor also underwent mechanical stress-induced PECAM-1 tyrosine phosphorylation. These findings suggest that mechanosensitive PECAM-1 may lie downstream of a primary mechanosensor that activates a tyrosine kinase.

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Citations

Nov 5, 2008·Cell Biochemistry and Biophysics·Shampa ChatterjeeAron B Fisher
Aug 2, 2008·Arteriosclerosis, Thrombosis, and Vascular Biology·Reema GoelDebra K Newman
Dec 16, 2006·Endothelium : Journal of Endothelial Cell Research·Gwenaele Garin, Bradford C Berk
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Jun 6, 2013·International Journal of Pediatrics·Austin L OderSteven M Barlow

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