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AMP-Activated Protein Kinase and Sirtuin 1 Coregulation of Cortactin Contributes to Endothelial Function
Author(s) -
TzuPin Shentu,
Ming He,
Xiaoli Sun,
Jianlin Zhang,
Fan Zhang,
Brendan Gongol,
Traci Marin,
Jiao Zhang,
Liang Wen,
Yinsheng Wang,
Gregory G. Geary,
Yi Zhu,
David A. Johnson,
John Y.J. Shyy
Publication year - 2016
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.116.307871
Subject(s) - cortactin , sirtuin , microbiology and biotechnology , function (biology) , protein kinase a , sirtuin 1 , chemistry , biology , kinase , biochemistry , enzyme , gene , downregulation and upregulation , cytoskeleton , cell , nad+ kinase
Cortactin translocates to the cell periphery in vascular endothelial cells (ECs) on cortical-actin assembly in response to pulsatile shear stress. Because cortactin has putative sites for AMP-activated protein kinase (AMPK) phosphorylation and sirtuin 1 (SIRT1) deacetylation, we examined the hypothesis that AMPK and SIRT1 coregulate cortactin dynamics in response to shear stress.

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