HIF prolyl‐hydroxylase 2 is the key oxygen sensor setting low steady‐state levels of HIF‐1α in normoxia

By E. Berra, E. Benizri, A. Ginouvès, Véronique Volmat, D. Roux, J. Pouysségur. EMBO Journal, 2003

1,412 citations recorded by the source corpus.

Subfields: Cancer Research, Genetics, Molecular Biology

View Paper: https://www.semanticscholar.org/paper/eb6b550c5fd3a1e72808d7c1422935721843de5a

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Citations in the corpus

Hypoxia signalling in cancer and approaches to enforce tumour regression (2006, background): “Of the three PHD isoforms in humans, PHD2 is the key limiting enzyme targeting HIF-1α for degradation under normoxic condition”
Hypoxia-Induced Autophagy Is Mediated through Hypoxia-Inducible Factor Induction of BNIP3 and BNIP3L via Their BH3 Domains (2009, methodology): “siRNA sequences targeting SIMA (also known as Drosophila HIF-) have been described previously ( 2 ).”
HIF overexpression correlates with biallelic loss of fumarate hydratase in renal cancer: novel role of fumarate in regulation of HIF stability. (2005, background): “, 2005), the primary enzyme responsible for regulating HIF levels under normoxia (Berra et al., 2003), in a similar VHL capture assay.”
Vascular endothelial growth factor (VEGF) signaling in tumor progression. (2007, neutral): “53 chief HIF-1á regulatory enzyme [220].”
Pyruvate Kinase M2 is a PHD3-stimulated Coactivator for Hypoxia-Inducible Factor 1 (2011, background): “…identified (Epstein et al., 2001), although PHD3 is less active in mediating HIF-1a hydroxylation than PHD2, which is the primary regulator of HIF-1a hydroxylation and proteasomal degradation in well- 742 Cell 145, 732–744, May 27, 2011 ª2011 Elsevier Inc. oxygenated cells (Berra et al., 2003).”
Transcriptional Regulation by Hypoxia Inducible Factors (2013, background): “In normoxia, a family of prolyl-4-hydroxylases (PHD1-4), most prominently PHD2 (also known as EGLN1), hydroxylate the oxygen-sensitive alpha subunits (Appelhoff, 2004; Berra et al., 2003; Koivunen et al., 2007; Landazuri et al., 2006).”
Differentiating the functional role of hypoxia‐inducible factor (HIF)‐1α and HIF‐2α (EPAS‐1) by the use of RNA interference: erythropoietin is a HIF‐2α target gene in Hep3B and Kelly cells (2004, background): “PHD2 was recently shown to be the HIF prolyl hydroxylase with the highest impact on HIF destabilization (34).”
Oxygen sensing by HIF hydroxylases (2004, background): “In a range of cell lines, these studies have shown that inactivation of PHD2 alone is sufficient to upregulate HIF1α protein levels and HIF-target-gene expression in oxygenated cells, and it has been proposed that PHD2 is the most important enzyme in regulating oxygenated levels of HIF1α under these”
Oxygen sensing by metazoans: the central role of the HIF hydroxylase pathway. (2008, background): “Of the three PHD family members, PHD2 (also called EglN1) appears to be the primary HIF prolyl hydroxylase, contributing the majority of HIF prolyl hydroxylase activity in normoxic cells and hence setting normoxic HIF1a levels (Berra et al., 2003; Minamishima et al., 2008; Takeda et al., 2008).”
Hypoxia and the hypoxia-inducible-factor pathway in glioma growth and angiogenesis. (2005, background): “…that specifi c silencing of only PHD2 and not PHD1 or PHD3 in a battery of immortalized human cell lines and pri- mary cell cultures led to increased HIF stability, which suggests that PHD2 may be the only physiologically relevant hydroxylase involved in HIF regulation (Berra et al., 2003).”