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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
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.
Stabilized HIF-1alpha (show HIF1A Proteins) induced by PHD2 conditional knockout resulted in the transition of muscle fibers toward a slow fiber type via a calcineurin (show PPP3CA Proteins)/NFATc1 (show NFATC1 Proteins) signaling pathway.
HIF-P4H-2 inhibition may be a novel strategy for protecting against the development of atherosclerosis.
findings show hypoxia and loss of PHD2 revert cancer-associated fibroblast (CAF (show LAMA2 Proteins)) activation; this reversion is associated with loss of matrix stiffening and consequently reduction in spontaneous metastases to lungs and liver
Data (including data from studies in transgenic/knockout mice) suggest that expression of Phd2/Egln1 in chondrocytes plays key role in chondrogenesis, osteogenesis, and developmental gene expression regulation.
a genetic link between EGLN1 and VWF (show VWF Proteins) in a constitution specific manner which could modulate thrombosis/bleeding susceptibility and outcomes of hypoxia, is reported.
PHD2 in the liver has a role in survival in lactic acidosis by activating the Cori cycle
Regulatory link was discovered between mitochondrial Txnrd and the JNK (show MAPK8 Proteins)-PHD2-Hif-1alpha (show HIF1A Proteins) axis, which highlights how the loss of Txnrd2 (show TXNRD2 Proteins) and the resulting altered mitochondrial redox balance impairs tumor growth as well as tumor-related angiogenesis.
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.
findings show hypoxia and loss of PHD2 revert cancer-associated fibroblast (CAF (show KAT2B Proteins)) activation
In this article, UTMD/PEI mediated gene transfection was investigated and the US parameters were optimized. Furthermore, the biological effects of PHD2 shRNA were investigated in H9C2 cells.
Data show that dimethyl-2-ketoglutarate (DKG) inhibits hypoxia-inducible factor 1alpha (HIF-1alpha (show HIF1A Proteins)) proline hydroxylation and degradation mediated by prolyl-4-hydroxylase PHD2.
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