有哪些信誉好的足球投注网站a heat-shock protein axis regulates vegfr2 proteolysis, blood vessel development and repair热休克蛋白的轴调节vegfr2蛋白水解作用,血管发展和修复.pdfVIP
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a heat-shock protein axis regulates vegfr2 proteolysis, blood vessel development and repair热休克蛋白的轴调节vegfr2蛋白水解作用,血管发展和修复
A Heat-Shock Protein Axis Regulates VEGFR2 Proteolysis, Blood Vessel Development and Repair 1 2 1 1 3 Alexander F. Bruns , Nadira Yuldasheva , Antony M. Latham , Leyuan Bao , Caroline Pellet-Many , 3 1 1 2 2 Paul Frankel , Sam L. Stephen , Gareth J. Howell , Stephen B. Wheatcroft , Mark T. Kearney , 3 1 Ian C. Zachary , Sreenivasan Ponnambalam * 1 Endothelial Cell Biology Unit, School for Molecular and Cellular Biology, University of Leeds, Leeds, United Kingdom, 2 Division of Cardiovascular and Diabetes Research, Faculty of Medicine and Health, University of Leeds, Leeds, United Kingdom, 3 Centre for Cardiovascular Biology and Medicine, University College London, London, United Kingdom Abstract Vascular endothelial growth factor A (VEGF-A) binds to the VEGFR2 receptor tyrosine kinase, regulating endothelial function, vascular physiology and angiogenesis. However, the mechanism underlying VEGFR2 turnover and degradation in this response is unclear. Here, we tested a role for heat-shock proteins in regulating the presentation of VEGFR2 to a degradative pathway. Pharmacological inhibition of HSP90 stimulated VEGFR2 degradation in primary endothelial cells and blocked VEGF-A-stimulated intracellular signaling via VEGFR2. HSP90 inhibition stimulated the formation of a VEGFR2-HSP70 complex. Clathrin-mediated VEGFR2 endocytosis is required for this HSP-linked degradative pathway for targeting VEGFR2 to the endosome-lysosome system. HSP90 perturbation selectively inhibited VEGF-A-stimulated human e
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