The role of VASP in regulation of cAMP- and Rac 1-mediated endothelial barrier stabilization

Am J Physiol Cell Physiol. 2008 Jan;294(1):C178-88. doi: 10.1152/ajpcell.00273.2007. Epub 2007 Nov 7.

Abstract

Regulation of actin dynamics is critical for endothelial barrier functions. We provide evidence that the actin-binding protein vasodilator-stimulated phosphoprotein (VASP) is required for endothelial barrier maintenance. Baseline permeability was significantly increased in VASP-deficient (VASP(-/-)) microvascular myocardial endothelial cells (MyEnd) in the absence of discernible alterations of immunostaining for adherens and tight junctions. We tested whether VASP is involved in the endothelium-stabilizing effects of cAMP or Rac 1. Forskolin and rolipram (F/R) to increase cAMP and cytotoxic necrotizing factor 1 (CNF-1) to activate Rac 1 were equally efficient to stabilize barrier functions in VASP(-/-) and wild-type (wt) cells. In wt cells, VASP was phosphorylated in response to F/R but did not localize to intercellular junctions. In contrast, CNF-1 and expression of constitutively active Rac 1 induced translocation of VASP to cell borders in wt cells, where it colocalized with active Rac 1. In VASP(-/-) cells, Rac 1 activity was reduced to 0.4 of wt levels in controls and increased approximately 20-fold in response to CNF-1 compared with 7-fold activation in wt cells. Moreover, inactivation of Rac 1 by lethal toxin led to a greater increase of permeability compared with wt cells. All these data suggest that VASP is involved in the regulation of Rac 1 activity. Taking these findings together, our study indicates that VASP at least in part stabilizes endothelial barrier functions by control of Rho-family GTPases.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adenylyl Cyclases / metabolism
  • Animals
  • Antigens, CD / metabolism
  • Bacterial Toxins / pharmacology
  • Cadherins / metabolism
  • Capillary Permeability* / drug effects
  • Cell Adhesion
  • Cell Adhesion Molecules / deficiency
  • Cell Adhesion Molecules / genetics
  • Cell Adhesion Molecules / metabolism*
  • Cell Line
  • Colforsin / pharmacology
  • Coronary Vessels / drug effects
  • Coronary Vessels / enzymology
  • Coronary Vessels / metabolism*
  • Cortactin / metabolism
  • Cyclic AMP / metabolism*
  • Endothelial Cells / drug effects
  • Endothelial Cells / enzymology
  • Endothelial Cells / metabolism*
  • Enzyme Activators / pharmacology
  • Escherichia coli Proteins / pharmacology
  • Intercellular Junctions / metabolism
  • Mice
  • Mice, Transgenic
  • Microfilament Proteins / deficiency
  • Microfilament Proteins / genetics
  • Microfilament Proteins / metabolism*
  • Neuropeptides / genetics
  • Neuropeptides / metabolism*
  • Phosphodiesterase Inhibitors / pharmacology
  • Phosphoproteins / deficiency
  • Phosphoproteins / genetics
  • Phosphoproteins / metabolism*
  • Phosphorylation
  • Protein Transport
  • Rolipram / pharmacology
  • Signal Transduction* / drug effects
  • Transfection
  • rac GTP-Binding Proteins / genetics
  • rac GTP-Binding Proteins / metabolism*
  • rac1 GTP-Binding Protein

Substances

  • Antigens, CD
  • Bacterial Toxins
  • Cadherins
  • Cell Adhesion Molecules
  • Cortactin
  • Cttn protein, mouse
  • Enzyme Activators
  • Escherichia coli Proteins
  • Microfilament Proteins
  • Neuropeptides
  • Phosphodiesterase Inhibitors
  • Phosphoproteins
  • Rac1 protein, mouse
  • cadherin 5
  • vasodilator-stimulated phosphoprotein
  • cytotoxic necrotizing factor type 1
  • Colforsin
  • Cyclic AMP
  • rac GTP-Binding Proteins
  • rac1 GTP-Binding Protein
  • Adenylyl Cyclases
  • Rolipram