Prolyl hydroxylase domain enzymes and their role in cell signaling and cancer metabolism

被引：31
作者：
Tra Ly Nguyen [1 ,2 ,3 ]
Duran, Raul V. [1 ,2 ,3 ]
机构：
[1] Inst Europeen Chim & Biol, 2 Rue Robert Escarpit, F-33607 Pessac, France
[2] INSERM U1218 Unit, Inst Bergonie, 229 Cours Argonne, F-33076 Bordeaux, France
[3] Univ Bordeaux, Bordeaux, France
来源：
INTERNATIONAL JOURNAL OF BIOCHEMISTRY & CELL BIOLOGY | 2016年 / 80卷
关键词：
2-Oxoglutarate; Cancer; Metabolism; mTOR; PHD; HYPOXIA-INDUCIBLE FACTOR-1-ALPHA; MITOCHONDRIAL COMPLEX-III; ENDOTHELIAL GROWTH-FACTOR; FACTOR HIF; TRANSCRIPTIONAL ACTIVITY; PYRUVATE-KINASE; DIRECT BINDING; OXYGEN; INHIBITION; EXPRESSION;
D O I：
10.1016/j.biocel.2016.09.026
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
The prolyl hydroxylase domain (PHD) enzymes regulate the stability of the hypoxia-inducible factor (HIF) in response to oxygen availability. During oxygen limitation, the inhibition of PHD permits the stabilization of HIF, allowing the cellular adaptation to hypoxia. This adaptation is especially important for solid tumors, which are often exposed to a hypoxic environment. However, and despite their original role as the oxygen sensors of the cell, PHD are currently known to display HIF-independent and hydroxylase-independent functions in the control of different cellular pathways, including mTOR pathway, NF-kappa B pathway, apoptosis and cellular metabolism. In this review, we summarize the recent advances in the regulation and functions of PHD in cancer signaling and cell metabolism. (C) 2016 Elsevier Ltd. All rights reserved.
引用
收藏
页码：71 / 80
页数：10
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