S-nitrosylation regulates VE-cadherin phosphorylation and internalization in microvascular permeability

Anita Guequén, Rodrigo Carrasco, Patricia Zamorano, Lorena Rebolledo, Pia Burboa, José Sarmiento, Mauricio P. Boric, Adam Korayem, Walter N. Durán, Fabiola A. Sánchez

Research output: Contribution to journalArticlepeer-review

28 Scopus citations

Abstract

The adherens junction complex, composed mainly of vascular endothelial (VE)-cadherin, β-catenin, p120, and γ-catenin, is the main element of the endothelial barrier in postcapillary venules. S-nitrosylation of β-catenin and p120 is an important step in proinflammatory agents-induced hyperpermeability. We investigated in vitro and in vivo whether or not VE-cadherin is S-nitrosylated using platelet-activating factor (PAF) as agonist. We report that PAF-stimulates S-nitrosylation of VE-cadherin, which disrupts its association with β-catenin. In addition, based on inhibition of nitric oxide production, our results strongly suggest that S-nitrosylation is required for VE-cadherin phosphorylation on tyrosine and for its internalization. Our results unveil an important mechanism to regulate phosphorylation of junctional proteins in association with S-nitrosylation.

Original languageEnglish (US)
Pages (from-to)H1039-H1044
JournalAmerican Journal of Physiology - Heart and Circulatory Physiology
Volume310
Issue number8
DOIs
StatePublished - Apr 2016

All Science Journal Classification (ASJC) codes

  • Physiology
  • Cardiology and Cardiovascular Medicine
  • Physiology (medical)

Keywords

  • Adherens junction
  • Endothelial permeability
  • Inflammation
  • S-nitrosylation
  • VE-cadherin

Fingerprint

Dive into the research topics of 'S-nitrosylation regulates VE-cadherin phosphorylation and internalization in microvascular permeability'. Together they form a unique fingerprint.

Cite this