S-nitrosylation regulates VE-cadherin phosphorylation and internalization in microvascular permeability.
Am J Physiol Heart Circ Physiol
; 310(8): H1039-44, 2016 Apr 15.
Article
en En
| MEDLINE
| ID: mdl-26921435
ABSTRACT
The adherens junction complex, composed mainly of vascular endothelial (VE)-cadherin, ß-catenin, p120, and γ-catenin, is the main element of the endothelial barrier in postcapillary venules.S-nitrosylation of ß-catenin and p120 is an important step in proinflammatory agents-induced hyperpermeability. We investigated in vitro and in vivo whether or not VE-cadherin isS-nitrosylated using platelet-activating factor (PAF) as agonist. We report that PAF-stimulates S-nitrosylation of VE-cadherin, which disrupts its association with ß-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.
Palabras clave
Texto completo:
1
Colección:
01-internacional
Banco de datos:
MEDLINE
Asunto principal:
Vénulas
/
Permeabilidad Capilar
/
Antígenos CD
/
Cadherinas
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Procesamiento Proteico-Postraduccional
/
Vasos Coronarios
/
Uniones Adherentes
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Células Endoteliales de la Vena Umbilical Humana
Límite:
Animals
/
Humans
Idioma:
En
Revista:
Am J Physiol Heart Circ Physiol
Asunto de la revista:
CARDIOLOGIA
/
FISIOLOGIA
Año:
2016
Tipo del documento:
Article