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10.1152/ajpheart.00063.2016 http://scihub22266oqcxt.onion/10.1152/ajpheart.00063.2016 C4867340!4867340 !26921435     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=26921435 &cmd=llinks): Failed to open stream: HTTP request failed! 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S-nitrosylation regulates VE-cadherin phosphorylation and internalization in microvascular permeability |pdf=|usr=}}{{26921435 }} gab.com Text S-nitrosylation regulates VE-cadherin phosphorylation and internalization in microvascular permeability JO: Am J Physiol Heart Circ Physiol http://www.kidney.de/pget.php?&tw=1&pmid=26921435 #FOAvip The adherens junction complex, composed mainly of vascular endothelial (VE)-cadherin, ?-catenin, p120, and ?-catenin, is the main element of the endothelial barrier in postcapillary venules.S-nitrosylation of ?-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 ?-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. Twit Text FOAVip S-nitrosylation regulates VE-cadherin phosphorylation and internalization in microvascular permeability ????Am J Physiol Heart Circ Physiol http://www.kidney.de/pget.php?&tw=1&pmid=26921435 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=26921435 #FOAvip English Wikipedia <ref>{{Cite pmid|26921435 }}</ref> S-nitrosylation regulates VE-cadherin phosphorylation and internalization in microvascular permeability #MMPMID26921435 Guequén A ; Carrasco R ; Zamorano P ; Rebolledo L ; Burboa P ; Sarmiento J ; Boric MP ; Korayem A ; Durán WN ; Sánchez FA Am J Physiol Heart Circ Physiol 2016[Apr]; 310 (8 ): H1039-44 PMID26921435 show ga The adherens junction complex, composed mainly of vascular endothelial (VE)-cadherin, ?-catenin, p120, and ?-catenin, is the main element of the endothelial barrier in postcapillary venules.S-nitrosylation of ?-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 ?-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. |*Capillary Permeability/drug effects [MESH] |*Protein Processing, Post-Translational/drug effects [MESH] |Adherens Junctions/drug effects/*metabolism [MESH] |Animals [MESH] |Antigens, CD/*metabolism [MESH] |Biological Transport [MESH] |Cadherins/*metabolism [MESH] |Catenins/metabolism [MESH] |Cattle [MESH] |Cell Line [MESH] |Coronary Vessels/drug effects/*metabolism [MESH] |Cricetinae [MESH] |Delta Catenin [MESH] |Human Umbilical Vein Endothelial Cells/drug effects/*metabolism [MESH] |Humans [MESH] |Mice [MESH] |Nitric Oxide/metabolism [MESH] |Nitrosation [MESH] |Phosphorylation [MESH] |Platelet Activating Factor/pharmacology [MESH] |Signal Transduction [MESH] |Time Factors [MESH] |Tyrosine [MESH] |Venules/*metabolism [MESH]S-nitrosylation regulates VE-cadherin phosphorylation and internalizat(epmc).pdf DeepDyve Pubget Overpricing