Unraveling the mechanisms involved in endothelial barrier protective effects of angiopoietin-1 variant MAT.Ang-1 英文参考文献.docVIP

Zhang et al. Critical Care 2012,16:466 /content/16/6/466 LET TER Unraveling the mechanisms involved in endothelial barrier protective e? ects of angiopoietin-1 variant MAT.Ang-1 Ru-Yuan Zhang, Dong Min, Jun Wu, Lei Li, Hong-Ping Qu and Yao-Qing Tang* See related research by Al? eri et al., /content/16/5/R182 With great interest we read the recent article by Al? eri impaired barrier function via regulating VE-cadherin and colleagues [1], demonstrating that angiopoietin member localization [2]. Recently, among the nine (Ang)-1 variant MAT.Ang-1 improved endotoxemia- tyrosines in the cytoplasmic tail of VE-cadherin, Potter induced microvascular dysfunction and microvascular and colleagues [3] revealed that tyrosine phosphorylation hyperpermeability e authors suggested that MAT. of VE-cadherin at two critical tyrosines, Tyr-658 and Ang-1-induced recovery of microcirculatory tissue Tyr-731, was su? cient to disrupt VE-cadherin-mediated perfusion during sepsis is due to preservation of endo- cell-cell junctions, leading to inhibition of cell barrier thelial barrier integrity. To further elucidate the mecha- nism, they investigated the possibility of involve ment of VE-cadherin, a major adherens junctions protein respon- function. Previous studies have shown that Ang-1 restores the endothelial barrier function via phosphorylation-depen- dent redistribution of VE-cadherin [4,5]. While in the sible for microvascular leakage in in? am mation. ey found, however, while there was no change in overall present study the total amount of VE-cadherin was not expression of VE-cadherin, MAT.Ang-1 increased VE- changed, intriguingly MAT.Ang-1 increases VE-cadherin cadherin phosphorylation in the treated mice, which phosphorylation (at Y658) in sepsis. is is unexpected appears unable