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comparative analysis of phd1, 2, and 3 expression in Xenopus laevis
we identified the beta2 adrenergic receptor (ADRB2) as a downstream target for PHD3 in skeletal muscle
PHD2 and PHD3 are essential for normal kidney development as the combined inactivation of stromal PHD2 and PHD3 resulted in renal failure that was associated with reduced kidney size, decreased numbers of glomeruli, and abnormal postnatal nephron formation.
PHD3 could protect against cardiac perivascular fibrosis and improve myocardial function in an obstructive sleep apnea mouse model by inhibiting endothelial-to-mesenchymal transition.
PHD3 expression induced by cytokines is NF-kappaB dependent in mesangial cells. Endogenously produced NO further augments PHD3 expression via HIF-1 alpha.
Opposing regulation and roles for PHD3 in lung dendritic cells and alveolar macrophages
PHD3 loss in cancer enables metabolic reliance on fatty acid oxidation via deactivation of ACC2.
Our observations disclose a novel role of PHD3 in the development of Tregs.
Epo transcription in brain pericytes was HIF-2 dependent and cocontrolled by PHD2 and PHD3, oxygen- and 2-oxoglutarate-dependent prolyl-4-hydroxylases that regulate HIF activity.
deleting Phd1-3 genes in osteoblasts increased osteoclast formation in vitro and in bone.
PHD3 is an active participant in atherogenesis
Cardiomyocyte-specific transgenic expression of PHD3 impairs the myocardial response to ischemia.
PHD3 protects intestinal epithelial barrier function and reveal a hydroxylase-independent function of PHD3 in stabilizing occludin
depletion of PHD3 leads to increased stabilization of HIF-1alpha and inhibition of DNA damage response, both of which may contribute to the cardioprotective effect seen with depletion of PHD3.
PHD3 loss sustains cell proliferation through the control of EGFR.
combined deletion of Phd2 and Phd3 dramatically decreased expression of phospholamban (PLN), resulted in sustained activation of calcium/calmodulin-activated kinase II (CaMKII), and sensitized mice to chronic beta-adrenergic stress-induced myocardial injury
PHD1 and PHD3 deletions promote angiogenesis in ischemia-injured tissue by increasing HIF1-alpha stability.
Using conditional PHD3-knockout mice, it was shown that PHD3 affects the production of Angptl2 and additionally influences the response toward this apoptosis-modulating factor.
ablation of the PHD3 gene resulted in increased angiogenesis and cardiac function after infarction thereby offering a potential target for management of ischemic myocardial disease
PHD3 depletion did not affect the expression of the PDH-E1alpha, E1beta, and E2 subunits, or the phosphorylation status of E1alpha, but destabilized the PDH complex (PDC), resulting in less functional PDC.
isoform-specific inhibition of Phd3 could be exploited to treat type 2 diabetes without the toxicity that could occur with chronic inhibition of multiple Phd isoforms.
PHD3 maintains high HIF2A mRNA levels in clear cell renal cell carcinoma
Acetylation-mediated Siah2 stabilization enhances PHD3 degradation in Helicobacter pylori-infected gastric epithelial cancer cells.
This study links the oxygen sensor PHD3 to metastasis and drug resistance in cancer, with implications for therapeutic improvement by targeting this system.
PHD3 overexpression may reduce the migratory and invasive capacity of gastric cancer cells, and inhibit the formation of tumor vasculature via negatively regulating HIF1A, which has been revealed to control VEGF transcription.
provides a rationale for targeting the PHD3-mediated regulation of the adaptive cellular hypoxic response in MM and suggests that targeting the O2-sensing pathway, alone or in combination with other anti-myeloma chemotherapeutics, may have clinical efficacy
These results indicate that the immunohistochemistry analysis of the protein expression of PDK1, PHD3, and HIF-1alpha defines the hypoxic status of Neuroblastoma tumors.
These findings indicate that downregulation of PHD3 and FIH in HCC is associated with more aggressive tumor behavior and a poor prognosis in hepatocellular carcinoma
Tuning the Transcriptional Response to Hypoxia by Inhibiting Hypoxia-inducible Factor (HIF) Prolyl and Asparaginyl Hydroxylases.
demonstrate that downregulation of PHD3 augments metastatic spread in human colorectal cancer and identify MCL-1 as a novel downstream effector of oxygen sensing
In pancreatic Beta cells, knock-down of PHD3 inhibited glucose-stimulated insulin secretion.
Loss of PHD3 expression is associated with breast cancer.
The selective efficacy of PZ was further demonstrated at the cellular level by observing inhibition of the PHD3-dependent DNA damage response pathway without stabilization of HIF-1alpha.
The enhanced expression of PHD3 might likely contribute to the poor neovascularization and affect the biological characterization in PDAC cancer cells
The data demonstrates that PHD3 can drive cell cycle entry at the G1/S transition through decreasing the half-life of p27 that occurs by attenuating p27S10 phosphorylation.
PHD3 controls EGFR activity by acting as a scaffolding protein that associates with the endocytic adaptor Eps15 and promotes the internalization of EGFR.
PHD3 SUMOylation occurs at a cluster of four lysines at the C-terminal end of the protein. Furthermore, PHD3 SUMOylation by SUMO2 or SUMO3 contributes to PHD3-mediated repression of HIF1-dependent transcriptional activity.
HIFPH3 expression in human non-small cell lung cancer lesions is significantly higher than that in para-cancerous and normal lung tissues and is positively associated with lymph node metastasis and microvessel density.
A novel role for PHD3 as a negative regulator of cell motility through posttranslational modification of nonmuscle actins.
Cellular oxygen sensor that catalyzes, under normoxic conditions, the post-translational formation of 4-hydroxyproline in hypoxia-inducible factor (HIF) alpha proteins. Hydroxylates a specific proline found in each of the oxygen-dependent degradation (ODD) domains (N-terminal, NODD, and C-terminal, CODD) of HIF1A. Also hydroxylates HIF2A. Has a preference for the CODD site for both HIF1A and HIF2A. Hydroxylation on the NODD site by EGLN3 appears to require prior hydroxylation on the CODD site. Hydroxylated HIFs are then targeted for proteasomal degradation via the von Hippel-Lindau ubiquitination complex. Under hypoxic conditions, the hydroxylation reaction is attenuated allowing HIFs to escape degradation resulting in their translocation to the nucleus, heterodimerization with HIF1B, and increased expression of hypoxy-inducible genes. ELGN3 is the most important isozyme in limiting physiological activation of HIFs (particularly HIF2A) in hypoxia. Also hydroxylates PKM2 in hypoxia, limiting glycolysis. Under normoxia, hydroxylates and regulates the stability of ADRB2. Regulator of cardiomyocyte and neuronal apoptosis. In cardiomyocytes, inhibits the anti-apoptotic effect of BCL2 by disrupting the BAX-BCL2 complex. In neurones, has a NGF-induced proapoptotic effect, probably through regulating CASP3 activity. Also essential for hypoxic regulation of neutrophilic inflammation.
, egl nine homolog 3
, egl nine homolog 3 (C. elegans)
, HIF-prolyl hydroxylase 3
, egl nine homolog 3, mitochondrial
, factor-responsive smooth muscle protein
, hypoxia-inducible factor prolyl hydroxylase 3
, prolyl hydroxylase domain-containing protein 3
, HIF prolyl hydroxylase 3
, egl nine-like protein 3 isoform