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Proteinase-Activated Receptor-2 Modulates Ve-Cadherin Expression to Affect Human Vascular Endothelial Barrier Function.
Journal of Cellular Biochemistry 2017 December
Published data indicate that the protease-activated receptor (PAR) 2 is involved in the pathogenesis of some cardiovascular diseases; the underlying mechanism is to be further investigated. Ve-cadherin is a critical molecule in maintaining the endothelial barrier integrity. This study aims to investigate the role of PAR2 activation in compromising the cardiac endothelial barrier function. In this study, human umbilical vein endothelial cells (Huvec cells) were cultured into monolayers using as an in vitro model of barrier function. The transepithelial electric resistance (TER) and permeability to dextran were assessed as indicators of barrier function. The expression of Ve-cadherin in Huvec cells was assessed by real-time RT-PCR, Western blotting, and chromatin immunoprecipitation. The results showed that exposure to tryptase in the culture, the barrier function of the Huvec monolayers, was markedly compromised; the levels of Ve-cadherin, one of the tight junction proteins, were suppressed as well. This was mimicked by exposing Huvec monolayers to the active PAR2 peptides (PAR2AP). After exposing to PAR2AP, the levels of histone deacetylase (HDAC)11 were increased in the Huvec cells. HDAC11 formed a complex with the transcription factor of Ve-cadherin to attenuate the Erg gene transcription activities and suppressed the expression of Ve-cadherin. In conclusion, activation of PAR2 compromises the vascular endothelial barrier function by suppressing the expression of Ve-cadherin. J. Cell. Biochem. 118: 4587-4593, 2017. © 2017 Wiley Periodicals, Inc.
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