Cyclic strain-mediated regulation of vascular endothelial occludin and ZO-1: influence on intercellular tight junction assembly and function

Arterioscler Thromb Vasc Biol. 2006 Jan;26(1):62-8. doi: 10.1161/01.ATV.0000194097.92824.b3. Epub 2005 Nov 3.

Abstract

Objective: The vascular endothelium constitutes a highly effective fluid/solute barrier through the regulated apposition of intercellular tight junction complexes. Because endothelium-mediated functions and pathology are driven by hemodynamic forces (cyclic strain and shear stress), we hypothesized a dynamic regulatory link between endothelial tight junction assembly/function and hemodynamic stimuli. We, therefore, examined the effects of cyclic strain on the expression, modification, and function of 2 pivotal endothelial tight junction components, occludin and ZO-1.

Methods and results: For these studies, bovine aortic endothelial cells were subjected to physiological levels of equibiaxial cyclic strain (5% strain, 60 cycles/min, 24 hours). In response to strain, both occludin and ZO-1 protein expression increased by 2.3+/-0.1-fold and 2.0+/-0.3-fold, respectively, concomitant with a strain-dependent increase in occludin (but not ZO-1) mRNA levels. These changes were accompanied by reduced occludin tyrosine phosphorylation (75.7+/-8%) and increased ZO-1 serine/threonine phosphorylation (51.7+/-9% and 82.7+/-25%, respectively), modifications that could be completely blocked with tyrosine phosphatase and protein kinase C inhibitors (dephostatin and rottlerin, respectively). In addition, there was a significant strain-dependent increase in endothelial occludin/ZO-1 association (2.0+/-0.1-fold) in parallel with increased localization of both occludin and ZO-1 to the cell-cell border. These events could be completely blocked by dephostatin and rottlerin, and they correlated with a strain-dependent reduction in transendothelial permeability to FITC-dextran.

Conclusions: Overall, these findings indicate that cyclic strain modulates both the expression and phosphorylation state of occludin and ZO-1 in vascular endothelial cells, with putative consequences for endothelial tight junction assembly and barrier integrity.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acetophenones / pharmacology
  • Animals
  • Aorta / cytology
  • Benzopyrans / pharmacology
  • Capillary Permeability / physiology
  • Cattle
  • Dextrans / pharmacokinetics
  • Endothelial Cells / cytology*
  • Endothelial Cells / physiology*
  • Enzyme Inhibitors / pharmacology
  • Fluorescein-5-isothiocyanate / analogs & derivatives
  • Fluorescein-5-isothiocyanate / pharmacokinetics
  • Gene Expression / physiology
  • Hydroquinones / pharmacology
  • In Vitro Techniques
  • Membrane Proteins / genetics
  • Membrane Proteins / metabolism*
  • Occludin
  • Phosphoproteins / genetics
  • Phosphoproteins / metabolism*
  • Phosphorylation
  • Protein Kinase C / antagonists & inhibitors
  • Protein Kinase C / metabolism
  • Protein Tyrosine Phosphatases / antagonists & inhibitors
  • Protein Tyrosine Phosphatases / metabolism
  • RNA, Messenger / metabolism
  • Stress, Mechanical
  • Tight Junctions / metabolism
  • Tight Junctions / physiology*
  • Zonula Occludens-1 Protein

Substances

  • Acetophenones
  • Benzopyrans
  • Dextrans
  • Enzyme Inhibitors
  • Hydroquinones
  • Membrane Proteins
  • Occludin
  • Phosphoproteins
  • RNA, Messenger
  • Zonula Occludens-1 Protein
  • fluorescein isothiocyanate dextran
  • dephostatin
  • rottlerin
  • Protein Kinase C
  • Protein Tyrosine Phosphatases
  • Fluorescein-5-isothiocyanate