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Thioredoxin-Interacting Protein Mediates Sustained VEGFR2 Signaling in Endothelial Cells Required for Angiogenesis
Author(s) -
ShinYoung Park,
Xi Shi,
Jinjiang Pang,
Chen Yan,
Bradford C. Berk
Publication year - 2013
Publication title -
arteriosclerosis thrombosis and vascular biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.007
H-Index - 270
eISSN - 1524-4636
pISSN - 1079-5642
DOI - 10.1161/atvbaha.112.300386
Subject(s) - thioredoxin interacting protein , txnip , angiogenesis , phosphorylation , microbiology and biotechnology , endothelial stem cell , biology , signal transduction , protein kinase b , human umbilical vein endothelial cell , vascular endothelial growth factor a , cancer research , vascular endothelial growth factor , chemistry , biochemistry , thioredoxin , oxidative stress , vegf receptors , in vitro
Thioredoxin-interacting protein (TXNIP) is an α-arrestin protein whose function is important for the regulation of vascular endothelial growth factor receptor 2 (VEGFR2) signaling and endothelial cell survival. Because VEGFR2 is critical for angiogenesis, we explored the role of TXNIP in VEGF-induced angiogenesis.

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