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oxygen via Phd2 has a decisive influence on the formation of the vascular network during vertebrate embryogenesis.
comparative analysis of phd1 (show EGLN2 Proteins), 2, and 3 expression in Xenopus laevis
miR-21 contributes to the protection of delayed ischemic preconditioning against renal ischemia reperfusion injury in mice, which is at least in part mediated by targeting of PHD2 and subsequently up-regulating HIF-1alpha/VEGF pathway.
Phd2 is the dominant HIF-hydroxylase in neutrophils under normoxic conditions; intrinsic regulation of glycolysis and glycogen (show GYS1 Proteins) stores is linked to the resolution of neutrophil-mediated inflammatory responses
Epo (show EPO Proteins) transcription in brain pericytes was HIF-2 dependent and cocontrolled by PHD2 and PHD3 (show EGLN3 Proteins), oxygen- and 2-oxoglutarate-dependent prolyl-4-hydroxylases that regulate HIF activity.
Notch ligand (show JAG2 Proteins) genes Jag1 (show JAG1 Proteins), Jag2 (show JAG2 Proteins), and Dll1 (show DLL1 Proteins) and target Hes1 became downregulated upon aging HIF-2alpha (show EPAS1 Proteins) dependently.
Results identified a critical role of PHD2 for a reversible glycolytic reprogramming in macrophages with a direct impact on their function.
Results found that loss of endothelial PHD2 induced pulmonary arterial hypertension and vascular remodeling in a HIF-2-dependent fashion.
We conclude that the activation of the HIF pathway induced by PHD2 deficiency enhances the effect of running training
deleting Phd1 (show EGLN2 Proteins)-3 genes in osteoblasts increased osteoclast formation in vitro and in bone.
Key messages: HIF-P4H-2 deficiency protects skeletal muscle from ischemia-reperfusion injury. The mechanisms involved are mediated via normoxic HIF-1alpha (show HIF1A Proteins) and HIF-2alpha (show EPAS1 Proteins) stabilization. HIF-P4H-2 deficiency increases capillary size but not number. HIF-P4H-2 deficiency maintains energy metabolism during ischemia-reperfusion.
Diminished degradation of FLNA upon PHD2 inactivation in hypoxia rearranges the actin cytoskeleton to reduce the number of dendritic spines, synapses.
Genetic variants in HIF-1alpha (show HIF1A Proteins) and PHD2 genes exist in Caucasians but do not appear to alter 30-day mortality in sepsis
The role of PHD-2 in breast cancer [review]
Sulfur mustard negatively affects hypoxia-stimulated HIF-1alpha (show HIF1A Proteins) signaling in keratinocytes and fibroblasts and thus possibly contributes to delayed wound healing in SM-injured patients, which could be treated with PHD-2 inhibitors.
The HIFalpha subunit is usually prolyl-hydroxylated by EglN family members under normoxic conditions, causing its rapid degradation. Study confirmed that triple-negative breast cancer cells secrete glutamate (show GRIN1 Proteins), which is both necessary and sufficient for the paracrine induction of HIF1alpha (show HIF1A Proteins) in such cells under normoxic conditions.
Disulfide bond-mediated PHD2 dimerization and inactivation result in the activation of HIF-1alpha (show HIF1A Proteins) and aerobic glycolysis in response to oxidative stress.
The present study demonstrated that the antiapoptotic effect of TMP in CoCl2-induced HUVECs was, at least in part, via the regulation of the PHD2/HIF-1alpha (show HIF1A Proteins) signaling pathway.
the levels of both miR-182 and HIF1alpha were elevated, while the expression PHD2 and FIH1 was downregulated in a mouse model of prostate cancer.
The protein encoded by this gene catalyzes the post-translational formation of 4-hydroxyproline in hypoxia-inducible factor (HIF) alpha proteins. HIF is a transcriptional complex that plays a central role in mammalian oxygen homeostasis. This protein functions as a cellular oxygen sensor, and under normal oxygen concentration, modification by prolyl hydroxylation is a key regulatory event that targets HIF subunits for proteasomal destruction via the von Hippel-Lindau ubiquitylation complex. Mutations in this gene are associated with erythrocytosis familial type 3 (ECYT3).
egl nine homolog 1 (C. elegans)
, egl nine homolog 1
, egl nine homolog 1-like
, egl nine homolog 2
, HIF-prolyl hydroxylase 2
, hypoxia-inducible factor prolyl hydroxylase 2
, prolyl hydroxylase domain-containing protein 2
, HIF prolyl hydroxylase 2
, egl nine-like protein 1
, zinc finger MYND domain-containing protein 6