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Journal articles on the topic 'HIF asparaginyl hydroxylase'

Author: Grafiati

Published: 4 June 2021

Last updated: 1 February 2022

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1

McNEILL, Luke A., Kirsty S. HEWITSON, Timothy D. CLARIDGE, Jürgen F. SEIBEL, Louise E. HORSFALL та Christopher J. SCHOFIELD. "Hypoxia-inducible factor asparaginyl hydroxylase (FIH-1) catalyses hydroxylation at the β-carbon of asparagine-803". Biochemical Journal 367, № 3 (2002): 571–75. http://dx.doi.org/10.1042/bj20021162.

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Asparagine-803 in the C-terminal transactivation domain of human hypoxia-inducible factor (HIF)-1 α-subunit is hydroxylated by factor inhibiting HIF-1 (FIH-1) under normoxic conditions causing abrogation of the HIF-1α/p300 interaction. NMR and other analyses of a hydroxylated HIF fragment produced in vitro demonstrate that hydroxylation occurs at the β-carbon of Asn-803 and imply production of the threo-isomer, in contrast with other known aspartic acid/asparagine hydroxylases that produce the erythro-isomer.

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2

Pappalardi, Melissa B., Dean E. McNulty, John D. Martin, et al. "Biochemical characterization of human HIF hydroxylases using HIF protein substrates that contain all three hydroxylation sites." Biochemical Journal 436, no. 2 (2011): 363–69. http://dx.doi.org/10.1042/bj20101201.

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The HIF (hypoxia-inducible factor) plays a central regulatory role in oxygen homoeostasis. HIF proteins are regulated by three Fe(II)- and α-KG (α-ketoglutarate)-dependent prolyl hydroxylase enzymes [PHD (prolyl hydroxylase domain) isoenzymes 1–3 or PHD1, PHD2 and PHD3] and one asparaginyl hydroxylase [FIH (factor inhibiting HIF)]. The prolyl hydroxylases control the abundance of HIF through oxygen-dependent hydroxylation of specific proline residues in HIF proteins, triggering subsequent ubiquitination and proteasomal degradation. FIH inhibits the HIF transcription activation through asparagi

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3

Flashman, Emily, Sarah L. Davies, Kar Kheng Yeoh, and Christopher J. Schofield. "Investigating the dependence of the hypoxia-inducible factor hydroxylases (factor inhibiting HIF and prolyl hydroxylase domain 2) on ascorbate and other reducing agents." Biochemical Journal 427, no. 1 (2010): 135–42. http://dx.doi.org/10.1042/bj20091609.

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The HIF (hypoxia-inducible factor) hydroxylases [PHDs or EGLNs (prolyl hydroxylases), which in humans are PHD isoforms 1–3, and FIH (factor inhibiting HIF)] regulate HIF levels and activity. These enzymes are Fe(II)/2-oxoglutarate-dependent oxygenases, many of which are stimulated by ascorbate. We have investigated the ascorbate dependence of PHD2-catalysed hydroxylation of two prolyl hydroxylation sites in human HIF-1α, and of FIH-catalysed hydroxylation of asparaginyl hydroxylation sites in HIF-1α and in a consensus ankyrin repeat domain peptide. The initial rate and extent of hydroxylation

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4

Strowitzki, Moritz, Eoin Cummins, and Cormac Taylor. "Protein Hydroxylation by Hypoxia-Inducible Factor (HIF) Hydroxylases: Unique or Ubiquitous?" Cells 8, no. 5 (2019): 384. http://dx.doi.org/10.3390/cells8050384.

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All metazoans that utilize molecular oxygen (O2) for metabolic purposes have the capacity to adapt to hypoxia, the condition that arises when O2 demand exceeds supply. This is mediated through activation of the hypoxia-inducible factor (HIF) pathway. At physiological oxygen levels (normoxia), HIF-prolyl hydroxylases (PHDs) hydroxylate proline residues on HIF-α subunits leading to their destabilization by promoting ubiquitination by the von-Hippel Lindau (VHL) ubiquitin ligase and subsequent proteasomal degradation. HIF-α transactivation is also repressed in an O2-dependent way due to asparagin

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5

DALGARD, Clifton Lee, Huasheng LU, Ahmed MOHYELDIN, and Ajay VERMA. "Endogenous 2-oxoacids differentially regulate expression of oxygen sensors." Biochemical Journal 380, no. 2 (2004): 419–24. http://dx.doi.org/10.1042/bj20031647.

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Adaptations to change in oxygen availability are crucial for survival of multi-cellular organisms and are also implicated in several disease states. Such adaptations rely upon gene expression regulated by the heterodimeric transcription factors HIFs (hypoxia-inducible factors). Enzymes that link changes in oxygen tensions with the stability and transcriptional activity of HIFs are considered as oxygen sensors. These enzymes are oxygen-, iron- and 2-oxoglutarate-dependent dioxygenases that hydroxylate key proline and asparagine residues in HIFα subunits. The constitutive inhibitory action of th

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6

Semenza, Gregg L. "Involvement of oxygen-sensing pathways in physiologic and pathologic erythropoiesis." Blood 114, no. 10 (2009): 2015–19. http://dx.doi.org/10.1182/blood-2009-05-189985.

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Abstract Red blood cells deliver O2 from the lungs to every cell in the human body. Reduced tissue oxygenation triggers increased production of erythropoietin by hypoxia-inducible factor 1 (HIF-1), which is a transcriptional activator composed of an O2-regulated α subunit and a constitutively expressed β subunit. Hydroxylation of HIF-1α or HIF-2α by the asparaginyl hydroxylase FIH-1 blocks coactivator binding and transactivation. Hydroxylation of HIF-1α or HIF-2α by the prolyl hydroxylase PHD2 is required for binding of the von Hippel-Lindau protein (VHL), leading to ubiquitination and proteas

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7

Kanelakis, Kimon C., Heather L. Palomino, Lina Li, et al. "Characterization of a Robust Enzymatic Assay for Inhibitors of 2-Oxoglutarate-Dependent Hydroxylases." Journal of Biomolecular Screening 14, no. 6 (2009): 627–35. http://dx.doi.org/10.1177/1087057109333976.

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The prolyl-4-hydroxylase proteins regulate the hypoxia-inducible transcription factors (HIFs) by hydroxylation of proline residues targeting HIF-1α for proteasomal degradation. Using the purified catalytic domain of prolyl hydroxylase 2 (PHD2181-417), an enzymatic assay has been developed to test inhibitors of the enzyme in vitro. Because PHD2 hydroxylates HIF-1α, with succinic acid produced as an end product, radiolabeled [5-14C]-2-oxoglutaric acid was used and formation of [14C]-succinic acid was measured to quantify PHD2181-417 enzymatic activity. Comparison of the separation of 2-oxoglutar

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8

Webb, James D., Andrea Murányi, Christopher W. Pugh, Peter J. Ratcliffe, and Mathew L. Coleman. "MYPT1, the targeting subunit of smooth-muscle myosin phosphatase, is a substrate for the asparaginyl hydroxylase factor inhibiting hypoxia-inducible factor (FIH)." Biochemical Journal 420, no. 2 (2009): 327–36. http://dx.doi.org/10.1042/bj20081905.

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The asparaginyl hydroxylase FIH [factor inhibiting HIF (hypoxia-inducible factor)] was first identified as a protein that inhibits transcriptional activation by HIF, through hydroxylation of an asparagine residue in the CAD (C-terminal activation domain). More recently, several ARD [AR (ankyrin repeat) domain]-containing proteins were identified as FIH substrates using FIH interaction assays. Although the function(s) of these ARD hydroxylations is unclear, expression of the ARD protein Notch1 was shown to compete efficiently with HIF CAD for asparagine hydroxylation and thus to enhance HIF act

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9

Lawton, Margot, Ming Tong, Fusun Gundogan, Jack R. Wands та Suzanne M. de la Monte. "Aspartyl-(asparaginyl) β-Hydroxylase, Hypoxia-Inducible Factor-1α and Notch Cross-Talk in Regulating Neuronal Motility". Oxidative Medicine and Cellular Longevity 3, № 5 (2010): 347–56. http://dx.doi.org/10.4161/oxim.3.5.13296.

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Aspartyl-(Asparaginyl)-β-Hydroxylase (AAH ) promotes cell motility by hydroxylating Notch. Insulin and insulin-like growth factor, type 1 (IGF-I) stimulate AAH through Erk MAP K and phosphoinositol-3-kinase-Akt (PI3K-Akt). However, hypoxia/oxidative stress may also regulate AAH . Hypoxia-inducible factor-1alpha (HIF-1α) regulates cell migration, signals through Notch, and is regulated by hypoxia/oxidative stress, insulin/IGF signaling and factor inhibiting HIF-1α (FIH) hydroxylation. To examine cross-talk between HIF-1α and AAH , we measured AAH , Notch-1, Jagged-1, FIH, HIF-1α, HIF-1β and the

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10

Koivunen, Peppi, Maija Hirsilä, Anne M. Remes, Ilmo E. Hassinen, Kari I. Kivirikko, and Johanna Myllyharju. "Inhibition of Hypoxia-inducible Factor (HIF) Hydroxylases by Citric Acid Cycle Intermediates." Journal of Biological Chemistry 282, no. 7 (2006): 4524–32. http://dx.doi.org/10.1074/jbc.m610415200.

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The stability and transcriptional activity of the hypoxia-inducible factors (HIFs) are regulated by two oxygen-dependent events that are catalyzed by three HIF prolyl 4-hydroxylases (HIF-P4Hs) and one HIF asparaginyl hydroxylase (FIH). We have studied possible links between metabolic pathways and HIF hydroxylases by analyzing the abilities of citric acid cycle intermediates to inhibit purified human HIF-P4Hs and FIH. Fumarate and succinate were identified as in vitro inhibitors of all three HIF-P4Hs, fumarate having Ki values of 50–80 μm and succinate 350–460 μm, whereas neither inhibited FIH.

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11

Zhang, Na, Zhenxing Fu, Sarah Linke та ін. "The Asparaginyl Hydroxylase Factor Inhibiting HIF-1α Is an Essential Regulator of Metabolism". Cell Metabolism 11, № 5 (2010): 364–78. http://dx.doi.org/10.1016/j.cmet.2010.03.001.

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12

Acker, Helmut. "The oxygen sensing signal cascade under the influence of reactive oxygen species." Philosophical Transactions of the Royal Society B: Biological Sciences 360, no. 1464 (2005): 2201–10. http://dx.doi.org/10.1098/rstb.2005.1760.

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Structural and functional integrity of organ function profoundly depends on a regular oxygen and glucose supply. Any disturbance of this supply becomes life threatening and may result in severe loss of organ function. Particular reductions in oxygen availability (hypoxia) caused by respiratory or blood circulation irregularities cannot be tolerated for longer periods due to an insufficient energy supply by anaerobic glycolysis. Complex cellular oxygen sensing systems have evolved to tightly regulate oxygen homeostasis. In response to variations in oxygen partial pressure (PO 2 ), these systems

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13

Núñez-O’Mara, Analía, and Edurne Berra. "Deciphering the emerging role of SUMO conjugation in the hypoxia-signaling cascade." Biological Chemistry 394, no. 4 (2013): 459–69. http://dx.doi.org/10.1515/hsz-2012-0319.

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Abstract By driving the primary transcriptional response, the hypoxia inducible factor (HIF) is a master player of the hypoxia-signaling cascade, activation of which is essential to maintain oxygen homeostasis. HIF is formed by the interaction of a constitutive HIF-1β subunit with a HIF-α subunit tightly regulated through the concerted action of the prolyl hydroxylase domain containing proteins (PHDs) and factor inhibiting HIF. In well-oxygenated cells, HIF-α prolyl-hydroxylation by PHDs is the recognition signal for the binding of the ubiquitin E3 ligase pVHL, allowing protein poly-ubiquitina

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14

Jin, Peng, Jengmin Kang, Myung Kyu Lee, and Jong-Wan Park. "Ferritin heavy chain controls the HIF-driven hypoxic response by activating the asparaginyl hydroxylase FIH." Biochemical and Biophysical Research Communications 499, no. 3 (2018): 475–81. http://dx.doi.org/10.1016/j.bbrc.2018.03.173.

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15

Sim, Jingwei, Andrew S. Cowburn, Asis Palazon, et al. "The Factor Inhibiting HIF Asparaginyl Hydroxylase Regulates Oxidative Metabolism and Accelerates Metabolic Adaptation to Hypoxia." Cell Metabolism 27, no. 4 (2018): 898–913. http://dx.doi.org/10.1016/j.cmet.2018.02.020.

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16

Cockman, M. E., D. E. Lancaster, I. P. Stolze, et al. "Posttranslational hydroxylation of ankyrin repeats in I B proteins by the hypoxia-inducible factor (HIF) asparaginyl hydroxylase, factor inhibiting HIF (FIH)." Proceedings of the National Academy of Sciences 103, no. 40 (2006): 14767–72. http://dx.doi.org/10.1073/pnas.0606877103.

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17

Stolze, Ineke P., Ya-Min Tian, Rebecca J. Appelhoff, et al. "Genetic Analysis of the Role of the Asparaginyl Hydroxylase Factor Inhibiting Hypoxia-inducible Factor (HIF) in Regulating HIF Transcriptional Target Genes." Journal of Biological Chemistry 279, no. 41 (2004): 42719–25. http://dx.doi.org/10.1074/jbc.m406713200.

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18

Saban, Evren, Shannon C. Flagg, and Michael J. Knapp. "Uncoupled O2-activation in the human HIF-asparaginyl hydroxylase, FIH, does not produce reactive oxygen species." Journal of Inorganic Biochemistry 105, no. 5 (2011): 630–36. http://dx.doi.org/10.1016/j.jinorgbio.2011.01.007.

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19

Ma, Mingyang, Shuyao Hua, Gang Li, et al. "Prolyl hydroxylase domain protein 3 and asparaginyl hydroxylase factor inhibiting HIF-1 levels are predictive of tumoral behavior and prognosis in hepatocellular carcinoma." Oncotarget 8, no. 8 (2017): 12983–3002. http://dx.doi.org/10.18632/oncotarget.14677.

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20

Pelletier, J., F. Dayan, J. Durivault, et al. "The asparaginyl hydroxylase factor-inhibiting HIF is essential for tumor growth through suppression of the p53–p21 axis." Oncogene 31, no. 24 (2011): 2989–3001. http://dx.doi.org/10.1038/onc.2011.471.

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21

Lee, Sang-Hyeup, Jeong Hee Moon, Eun Ah Cho, Seong-Eon Ryu, and Myung Kyu Lee. "Monoclonal Antibody-Based Screening Assay for Factor Inhibiting Hypoxia-Inducible Factor Inhibitors." Journal of Biomolecular Screening 13, no. 6 (2008): 494–503. http://dx.doi.org/10.1177/1087057108318800.

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The factor-inhibiting hypoxia-inducible factor (FIH) hydroxylates the asparagine 803 (Asn803) residue of the hypoxia-inducible factor 1α (HIF-1α), and the modification abrogates the transcriptional activity of HIF-1α. Because FIH is more active on HIF-1α than prolyl hydroxylase domain proteins under hypoxic conditions, its inhibitors have potential to be developed as anti-ischemic drugs targeting normal cells stressed by hypoxia. In this study, the authors developed the first monoclonal antibody, SHN-HIF1α, specifically to Asn803 hydroxylated HIF-1α and a sensitive assay system for FIH inhibit

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22

Stolze, Ineke P., Ya-Min Tian, Rebecca J. Appelhoff, et al. "Genetic analysis of the role of the asparaginyl hydroxylase factor inhibiting hypoxia-inducible factor (FIH) in regulating hypoxia-inducible factor (HIF) transcriptional target genes. Vol. 279 (2004) 42719-42725." Journal of Biological Chemistry 279, no. 52 (2004): 54974. http://dx.doi.org/10.1016/s0021-9258(19)63268-0.

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23

Loenarz, Christoph, Rasheduzzaman Chowdhury, Christopher J. Schofield, and Emily Flashman. "Oxygenases for oxygen sensing." Pure and Applied Chemistry 80, no. 8 (2008): 1837–47. http://dx.doi.org/10.1351/pac200880081837.

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In animals, cellular and physiological responses to oxygen level variations are regulated via the post-translational modification of the heterodimeric hypoxia-inducible transcription factor (HIF). Hydroxylation of the HIF-α subunit at either of two conserved prolyl residues enables binding to the von Hippel-Lindau protein (pVHL) elongin C/B complex (VCB) which targets HIF-α for degradation via the ubiquitin proteasome pathway. Hydroxylation of an asparaginyl residue in the C-terminal transcriptional activation domain of HIF-α reduces its interaction with the transcriptional coactivator p300. T

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24

Kimura, Motohide, Satoshi Takabuchi, Tomoharu Tanaka, et al. "n-Propyl gallate activates hypoxia-inducible factor 1 by modulating intracellular oxygen-sensing systems." Biochemical Journal 411, no. 1 (2008): 97–105. http://dx.doi.org/10.1042/bj20070824.

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HIF-1 (hypoxia-inducible factor 1) is a master regulator of cellular adaptive responses to hypoxia. The expression and transcriptional activity of the HIF-1α subunit is stringently controlled by intracellular oxygen tension through the action of prolyl and asparaginyl hydroxylases. In the present study we demonstrate that PG (n-propyl gallate) activates HIF-1 and expression of its downstream target genes under normoxic conditions in cultured cells and in mice. The stability and transcriptional activity of HIF-1α are increased by PG. PG treatment inhibits the interaction between HIF-1α and VHL

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25

Zagórska, Anna, and Józef Dulak. "HIF-1: the knowns and unknowns of hypoxia sensing." Acta Biochimica Polonica 51, no. 3 (2004): 563–85. http://dx.doi.org/10.18388/abp.2004_3545.

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Hypoxia-inducible factor-1 (HIF-1) is a transcriptional activator that functions as a master regulator of cellular and systemic oxygen homeostasis. It consists of two constitutively produced subunits: HIF-1alpha and HIF-1beta. Under normoxic conditions HIF-1alpha undergoes hydroxylation at specific prolyl residues which leads to an immediate ubiquitination and subsequent proteasomal degradation of the alpha subunit. Additionally, hydroxylation of an asparaginyl residue blocks the transcriptional activity of HIF-1 due to inhibition of its interaction with co-activators. In contrast, under hypox

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26

LANCASTER, David E., Luke A. McNEILL, Michael A. McDONOUGH, et al. "Disruption of dimerization and substrate phosphorylation inhibit factor inhibiting hypoxia-inducible factor (FIH) activity." Biochemical Journal 383, no. 3 (2004): 429–37. http://dx.doi.org/10.1042/bj20040735.

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HIF (hypoxia-inducible factor) is an αβ transcription factor that modulates the hypoxic response in many animals. The cellular abundance and activity of HIF-α are regulated by its post-translational hydroxylation. The hydroxylation of HIF is catalysed by PHD (prolyl hydroxylase domain) enzymes and FIH (factorinhibiting HIF), all of which are 2-oxoglutarate- and Fe(II)-dependent dioxygenases. FIH hydroxylates a conserved asparagine residue in HIF-α (Asn-803), which blocks the binding of HIF to the transcriptional co-activator p300, preventing transcription of hypoxia-regulated genes under normo

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27

Hirota, Kiichi. "HIF-α Prolyl Hydroxylase Inhibitors and Their Implications for Biomedicine: A Comprehensive Review". Biomedicines 9, № 5 (2021): 468. http://dx.doi.org/10.3390/biomedicines9050468.

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Oxygen is essential for the maintenance of the body. Living organisms have evolved systems to secure an oxygen environment to be proper. Hypoxia-inducible factor (HIF) plays an essential role in this process; it is a transcription factor that mediates erythropoietin (EPO) induction at the transcriptional level under hypoxic environment. After successful cDNA cloning in 1995, a line of studies were conducted for elucidating the molecular mechanism of HIF activation in response to hypoxia. In 2001, cDNA cloning of dioxygenases acting on prolines and asparagine residues, which play essential role

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28

Hewitson, K. S., L. A. McNeill, J. M. Elkins, and C. J. Schofield. "The role of iron and 2-oxoglutarate oxygenases in signalling." Biochemical Society Transactions 31, no. 3 (2003): 510–15. http://dx.doi.org/10.1042/bst0310510.

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Sensing of ambient dioxygen levels and appropriate feedback mechanisms are essential processes for all multicellular organisms. In animals, moderate hypoxia causes an increase in the transcription levels of specific genes, including those encoding vascular endothelial growth factor and erythropoietin. The hypoxic response is mediated by hypoxia-inducible factor (HIF), an αβ heterodimeric transcription factor in which both the HIF subunits are members of the basic helix–loop–helix PAS (PER-ARNT-SIM) domain family. Under hypoxic conditions, levels of HIFα rise, allowing dimerization with HIFβ an

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29

Masson, N. "HIF prolyl and asparaginyl hydroxylases in the biological response to intracellular O2 levels." Journal of Cell Science 116, no. 15 (2003): 3041–49. http://dx.doi.org/10.1242/jcs.00655.

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30

Chan, Mun Chiang, Nicholas E. Ilott, Johannes Schödel, et al. "Tuning the Transcriptional Response to Hypoxia by Inhibiting Hypoxia-inducible Factor (HIF) Prolyl and Asparaginyl Hydroxylases." Journal of Biological Chemistry 291, no. 39 (2016): 20661–73. http://dx.doi.org/10.1074/jbc.m116.749291.

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31

Hewitson, Kirsty S., Luke A. McNeill, Madeline V. Riordan, et al. "Hypoxia-inducible Factor (HIF) Asparagine Hydroxylase Is Identical to Factor Inhibiting HIF (FIH) and Is Related to the Cupin Structural Family." Journal of Biological Chemistry 277, no. 29 (2002): 26351–55. http://dx.doi.org/10.1074/jbc.c200273200.

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32

Giatromanolaki, Alexandra, Michael I. Koukourakis, Francesco Pezzella, et al. "Expression of prolyl-hydroxylases PHD-1, 2 and 3 and of the asparagine hydroxylase FIH in non-small cell lung cancer relates to an activated HIF pathway." Cancer Letters 262, no. 1 (2008): 87–93. http://dx.doi.org/10.1016/j.canlet.2007.11.041.

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33

Fanale, Daniele, Viviana Bazan, Stefano Caruso, et al. "Hypoxia and Human Genome Stability: Downregulation of BRCA2 Expression in Breast Cancer Cell Lines." BioMed Research International 2013 (2013): 1–8. http://dx.doi.org/10.1155/2013/746858.

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Previously, it has been reported that hypoxia causes increased mutagenesis and alteration in DNA repair mechanisms. In 2005, an interesting study showed that hypoxia-induced decreases in BRCA1 expression and the consequent suppression of homologous recombination may lead to genetic instability. However, nothing is yet known about the involvement of BRCA2 in hypoxic conditions in breast cancer. Initially, a cell proliferation assay allowed us to hypothesize that hypoxia could negatively regulate the breast cancer cell growth in short term in vitro studies. Subsequently, we analyzed gene express

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34

Yan, Qin, Steven Bartz, Mao Mao, Lianjie Li та William G. Kaelin. "The Hypoxia-Inducible Factor 2α N-Terminal and C-Terminal Transactivation Domains Cooperate To Promote Renal Tumorigenesis In Vivo". Molecular and Cellular Biology 27, № 6 (2007): 2092–102. http://dx.doi.org/10.1128/mcb.01514-06.

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ABSTRACT Hypoxia-inducible factor (HIF) is a heterodimeric transcription factor, consisting of an alpha subunit and a beta subunit, that controls cellular responses to hypoxia. HIFα contains two transcriptional activation domains called the N-terminal transactivation domain (NTAD) and the C-terminal transactivation domain (CTAD). HIFα is destabilized by prolyl hydroxylation catalyzed by EglN family members. In addition, CTAD function is inhibited by asparagine hydroxylation catalyzed by FIH1. Both hydroxylation reactions are linked to oxygen availability. The von Hippel-Lindau tumor suppressor

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35

Chen, Da-Yuan, Jacqueline-Alba Fabrizio, Sarah E. Wilkins, et al. "Ankyrin Repeat Proteins of Orf Virus Influence the Cellular Hypoxia Response Pathway." Journal of Virology 91, no. 1 (2016). http://dx.doi.org/10.1128/jvi.01430-16.

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ABSTRACT Hypoxia-inducible factor (HIF) is a transcriptional activator with a central role in regulating cellular responses to hypoxia. It is also emerging as a major target for viral manipulation of the cellular environment. Under normoxic conditions, HIF is tightly suppressed by the activity of oxygen-dependent prolyl and asparaginyl hydroxylases. The asparaginyl hydroxylase active against HIF, factor inhibiting HIF (FIH), has also been shown to hydroxylate some ankyrin repeat (ANK) proteins. Using bioinformatic analysis, we identified the five ANK proteins of the parapoxvirus orf virus (ORF

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36

Semenza, Gregg L. "Breakthrough Science: Hypoxia-Inducible Factors, Oxygen Sensing, and Disorders of Hematopoiesis." Blood, August 19, 2021. http://dx.doi.org/10.1182/blood.2021011043.

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Hypoxia-inducible factors (HIF) were discovered as activators of erythropoietin gene transcription in response to reduced O2 availability. O2-dependent hydroxylation of HIFs on proline and asparagine residues regulates protein stability and transcription activity, respectively. Mutations in genes encoding components of the oxygen sensing pathway cause familial erythrocytosis. Several small molecule inhibitors of HIF prolyl hydroxylases are currently in clinical trials as erythropoiesis stimulating agents. HIFs are overexpressed in bone marrow neoplasms, and the development of HIF inhibitors ma

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