Opposing effects of the angiopoietins on the thrombin-induced permeability of human pulmonary microvascular endothelial cells

PLoS One. 2011;6(8):e23448. doi: 10.1371/journal.pone.0023448. Epub 2011 Aug 15.

Abstract

Background: Angiopoietin-2 (Ang-2) is associated with lung injury in ALI/ARDS. As endothelial activation by thrombin plays a role in the permeability of acute lung injury and Ang-2 may modulate the kinetics of thrombin-induced permeability by impairing the organization of vascular endothelial (VE-)cadherin, and affecting small Rho GTPases in human pulmonary microvascular endothelial cells (HPMVECs), we hypothesized that Ang-2 acts as a sensitizer of thrombin-induced hyperpermeability of HPMVECs, opposed by Ang-1.

Methodology/principal findings: Permeability was assessed by measuring macromolecule passage and transendothelial electrical resistance (TEER). Angiopoietins did not affect basal permeability. Nevertheless, they had opposing effects on the thrombin-induced permeability, in particular in the initial phase. Ang-2 enhanced the initial permeability increase (passage, P = 0.010; TEER, P = 0.021) in parallel with impairment of VE-cadherin organization without affecting VE-cadherin Tyr685 phosphorylation or increasing RhoA activity. Ang-2 also increased intercellular gap formation. Ang-1 preincubation increased Rac1 activity, enforced the VE-cadherin organization, reduced the initial thrombin-induced permeability (TEER, P = 0.027), while Rac1 activity simultaneously normalized, and reduced RhoA activity at 15 min thrombin exposure (P = 0.039), but not at earlier time points. The simultaneous presence of Ang-2 largely prevented the effect of Ang-1 on TEER and macromolecule passage.

Conclusions/significance: Ang-1 attenuated thrombin-induced permeability, which involved initial Rac1 activation-enforced cell-cell junctions, and later RhoA inhibition. In addition to antagonizing Ang-1, Ang-2 had also a direct effect itself. Ang-2 sensitized the initial thrombin-induced permeability accompanied by destabilization of VE-cadherin junctions and increased gap formation, in the absence of increased RhoA activity.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Angiopoietin-1 / genetics
  • Angiopoietin-1 / metabolism
  • Angiopoietin-1 / pharmacology
  • Angiopoietin-2 / genetics
  • Angiopoietin-2 / metabolism
  • Angiopoietin-2 / pharmacology
  • Angiopoietins / genetics
  • Angiopoietins / metabolism
  • Angiopoietins / pharmacology*
  • Antigens, CD / metabolism
  • Cadherins / metabolism
  • Cell Membrane Permeability / drug effects*
  • Cells, Cultured
  • Coagulants / pharmacology
  • Electric Impedance
  • Endothelial Cells / drug effects*
  • Endothelial Cells / metabolism
  • Endothelial Cells / physiology
  • Humans
  • Immunoblotting
  • Lung / blood supply
  • Phosphorylation / drug effects
  • Receptor, TIE-2 / metabolism
  • Recombinant Proteins / pharmacology
  • Thrombin / pharmacology*
  • Time Factors
  • rac1 GTP-Binding Protein / metabolism
  • rhoA GTP-Binding Protein / metabolism

Substances

  • Angiopoietin-1
  • Angiopoietin-2
  • Angiopoietins
  • Antigens, CD
  • Cadherins
  • Coagulants
  • Recombinant Proteins
  • cadherin 5
  • Receptor, TIE-2
  • Thrombin
  • rac1 GTP-Binding Protein
  • rhoA GTP-Binding Protein