Abstract
Leukocyte transendothelial migration (TEM) is a complex process involving cytoskeletal remodeling controlled by several signaling pathways including RhoGTPases. Previous studies have shown that VE‐Cadherin (VE‐Cad) forms a complex with α‐,β‐,γ‐, and p120‐catenins, and that during TEM, this VE‐cad complex disassociates to form a transient gap. p120‐catenin (p120) over expression stabilized VE‐cad surface expression and prevented leukocyte TEM. This process was dependent on changes in VE‐cad tyrosine phosphorylation. Based on reports that p120‐catenin overexpression in fibroblasts inhibits RhoA and activates Rac and Cdc42, we speculated that a similar process may occur in human endothelial cells (HEC) and was responsible for blocking TEM. HEC overexpressing p120GFP or Adv‐GFP were treated with α‐thrombin or medium, lysed, and assayed for RhoA, Rac and Cdc42 activity. Neither overexpression of p120 or GFP affected basal activity of these GTPases. Thrombin induced a significant increase in both GTP‐loaded Rho‐A and actin stress fibers in both GFP and p120GFP transduced HEC. Our data provide evidence that regulation of VE‐Cad gap formation and TEM by p120 does not involve inhibition of RhoA activity. Supported by NIH HL053993 & HL094706.
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