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2016 ; 6
(ä): 23770
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BET Bromodomain Suppression Inhibits VEGF-induced Angiogenesis and Vascular
Permeability by Blocking VEGFR2-mediated Activation of PAK1 and eNOS
#MMPMID27044328
Huang M
; Qiu Q
; Xiao Y
; Zeng S
; Zhan M
; Shi M
; Zou Y
; Ye Y
; Liang L
; Yang X
; Xu H
Sci Rep
2016[Apr]; 6
(ä): 23770
PMID27044328
show ga
The tyrosine kinase receptor vascular endothelial growth factor receptor 2
(VEGFR2) is a critical modulator of angiogenesis. Increasing evidence indicate
the important role of bromodomain and extra-terminal domain (BET) of chromatin
adaptors in regulating tumor growth and inflammatory response. However, whether
BET proteins have a role in angiogenesis and endothelial permeability is unclear.
In this study, we observed that treatment with JQ1, a specific BET inhibitor,
suppressed in vitro tube formation of human umbilical vein endothelial cells
(HUVECs) and in vivo angiogenesis in a Matrigel plug and oxygen-induced
retinopathy neovascularization. JQ1 attenuated the VEGF-induced decrease in TEER
in HUVECs and prevented Evans blue dye leakage in the VEGF-induced Miles assay in
athymic Balb/c nude mice. BET inhibition with JQ1 or shRNA for Brd2 or Brd4
suppressed VEGF-induced migration, proliferation, and stress fiber formation of
HUVECs. Furthermore, BET inhibition suppressed phosphorylation of VEGFR2 and
PAK1, as well as eNOS activation in VEGF-stimulated HUVECs. Inhibition with
VEGFR2 and PAK1 also reduced migration and proliferation, and attenuated the
VEGF-induced decrease in TEER. Thus, our observations suggest the important role
of BET bromodomain in regulating VEGF-induced angiogenesis. Strategies that
target the BET bromodomain may provide a new therapeutic approach for
angiogenesis-related diseases.