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A family with erythrocytosis establishes a role for prolyl hydroxylase domain protein 2 in oxygen homeostasis
Open accessAbstract
The number of red blood cells is normally tightly regulated by a classic homeostatic mechanism based on oxygen sensing in the kidney. Decreased oxygen delivery resulting from anemia induces the production of erythropoietin, which increases red cell production and hence oxygen delivery. Investigations of erythropoietin regulation identified the transcription factor hypoxia-inducible factor (HIF). HIF is now recognized as being a key regulator of genes that function in a comprehensive range of processes besides erythropoiesis, including energy metabolism and angiogenesis. HIF itself is regulated through the α-subunit, which is hydroxylated in the presence of oxygen by a family of three prolyl hydroxylase domain proteins (PHDs)/HIF prolyl hydroxylases/egg-laying-defective nine enzymes. Hydroxylation allows capture by the von Hippel–Lindau tumor suppressor gene product, ubiquitination, and destruction by the proteasome. Here we describe an inherited mutation in a mammalian PHD enzyme. We show that this mutation in PHD2 results in a marked decrease in enzyme activity and is associated with familial erythrocytosis, identifying a previously unrecognized cause of this condition. Our findings indicate that PHD2 is critical for normal regulation of HIF in humans.
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“Conversely, several PHD2 missense mutations have been identified that resulted in diminished hydroxylase activity. 157, 158”
From Regulation of erythropoiesis by hypoxia-inducible factors (2013) · cites this paper as [157]
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“Patients, who were heterozygous for these mutations were characterized by increased rbc values in the presence of inappropriately normal serum EPO levels. 157–162”
From Regulation of erythropoiesis by hypoxia-inducible factors (2013) · cites this paper as [157]
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Cites
Targeting HIF-1 for cancer therapy
Semenza, G. L. (2003) · Nature Reviews Cancer · doi:10.1038/nrc1187 · Cited by 6,717
Smith, D. B., & Johnson, K. S. (1988) · Gene · doi:10.1016/0378-1119(88)90005-4 · Cited by 5,844
Jaakkola, P., Mole, D. R., Tian, Y.-M., Wilson, M. I., Gielbert, J., Gaskell, S. J., Kriegsheim, A. V., Hebestreit, H. F., Mukherji, M., Schofield, C. J., et al. (2001) · Science · doi:10.1126/science.1059796 · Cited by 5,535
Self-citationThe tumour suppressor protein VHL targets hypoxia-inducible factors for oxygen-dependent proteolysis
Maxwell, P. H., Wiesener, M. S., Chang, G.-W., Clifford, S. C., Vaux, E. C., Cockman, M. E., Wykoff, C. C., Pugh, C. W., Maher, E. R., & Ratcliffe, P. J. (1999) · Nature · doi:10.1038/20459 · Cited by 5,180
Self-citationTargeting Hypoxia-Inducible Factors for the Treatment of Anemia in Chronic Kidney Disease Patients
Locatelli, F., Fishbane, S. N., Block, G. A., & Macdougall, I. C. (2017) · American Journal of Nephrology · doi:10.1159/000455166 · Cited by 4,836
HIFα Targeted for VHL-Mediated Destruction by Proline Hydroxylation: Implications for O 2 Sensing
Ivan, M., Kondo, K., Yang, H., Kim, W., Valiando, J., Ohh, M., Salic, A., Asara, J. M., Lane, W. S., & Kaelin Jr., W. G. (2001) · Science · doi:10.1126/science.1059817 · Cited by 4,735
Epstein, A. C. R., Gleadle, J. M., McNeill, L. A., Hewitson, K. S., O'Rourke, J., Mole, D. R., Mukherji, M., Metzen, E., Wilson, M. I., Dhanda, A., et al. (2001) · Cell · doi:10.1016/s0092-8674(01)00507-4 · Cited by 3,333
Self-citationA conserved family of prolyl-4-hydroxylases that modify HIF
Bruick, R. K., & McKnight, S. L. (2001) · Science · doi:10.1126/science.1066373 · Cited by 2,549
Regulation of angiogenesis by hypoxia: role of the HIF system
Pugh, C. W., & Ratcliffe, P. J. (2003) · Nature Medicine · doi:10.1038/nm0603-677 · Cited by 2,520
Ohh, M., Park, C. W., Ivan, M., Hoffman, M. A., Kim, T.-Y., Huang, L. E., Pavletich, N., Chau, V., & Kaelin, W. G. (2000) · Nature Cell Biology · doi:10.1038/35017054 · Cited by 1,577
Research works printed but not linked: 4
- Gordeuk, V. R., Stockton, D. W. & Prchal, J. T. (2005) Haematologica 90, 109–116.15642677
- Cario, H., Schwarz, K., Jorch, N., Kyank, U., Petrides, P. E., Schneider, D. T., Uhle, R., Debatin, K. M. & Kohne, E. (2005) Haematologica 90, 19–24.15642664
- Kato, H., Inoue, T., Asanoma, K., Nishimura, C., Matsuda, T. & Wake, N. (2005) Int. J. Cancer 118, 1144–1153.
- Yu, F., White, S. B., Zhao, Q. & Lee, F. S. (2001) Cancer Res. 61, 4136–4142.11358837
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Self-citationMartini, M., Teofili, L., Cenci, T., Giona, F., Torti, L., Rea, M., Foa, R., Leone, G., & Larocca, L. M. (2008) · Haematologica · doi:10.3324/haematol.13210 · Cited by 73
Koeman, J. M., Russell, R. C., Tan, M., Petillo, D., Westphal, M., Koelzer, K., Metcalf, J. L., Zhang, Z., Matsuda, D., Dykema, K. J., et al. (2008) · PLoS Genetics · doi:10.1371/journal.pgen.1000176 · Cited by 74
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Ameln, A. K., Muschter, A., Mamlouk, S., Kalucka, J. M., Prade, I., Franke, K., Rezaei, M., Poitz, D. M., Breier, G., & Wielockx, B. (2011) · Cancer Research · doi:10.1158/0008-5472.can-10-3838 · Cited by 71
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Váchal, P., Miao, S., Pierce, J. M., Guiadeen, D., Colandrea, V. J., Wyvratt, M. J., Salowe, S. P., Sonatore, L. M., Milligan, J. A., Hajdu, R., et al. (2012) · Journal of Medicinal Chemistry · doi:10.1021/jm201542d · Cited by 67
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Shao, Z., Zhang, Y., & Powell‐Coffman, J. A. (2009) · Genetics · doi:10.1534/genetics.109.107284 · Cited by 59
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Yoon, D., Ponka, P., & Prchal, J. T. (2011) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00044.2011 · Cited by 63
Erythrocytosis associated with a novel missense mutation in the BPGM gene
Petousi, N., Copley, R. R., Lappin, T. R. J., Haggan, S. E., Bento, C., Cario, H., Percy, M. J., Ratcliffe, P. J., Robbins, P. A., McMullin, M. F., et al. (2014) · Haematologica · doi:10.3324/haematol.2014.109306 · Cited by 59
Self-citationLaitala, A., Aro, E., Walkinshaw, G., Mäki, J. M., Rossi, M., Heikkilä, M., Savolainen, E.-R., Arend, M., Kivirikko, K. I., Koivunen, P., et al. (2012) · Blood · doi:10.1182/blood-2012-07-441824 · Cited by 58
Furlow, P. W., Percy, M. J., Sutherland, S., Bierl, C., McMullin, M. F., Master, S. R., Lappin, T. R. J., & Lee, F. S. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m808737200 · Cited by 58
Self-citationSong, D., Li, L.-S., Heaton-Johnson, K. J., Arsenault, P. R., Master, S. R., & Lee, F. S. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.440552 · Cited by 59
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Taïeb, D., Yang, C., Delenne, B., Zhuang, Z., Barlier, A., Sebag, F. A., & Pacák, K. (2013) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jc.2013-1217 · Cited by 59
Idiopathic erythrocytosis: a disappearing entity
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Self-citationLadroue, C., Hoogewijs, D., Gad, S., Carcenac, R., Storti, F., Barrois, M., Gimenez-Roqueplo, A.-P., Leporrier, M., Casadevall, N., Hermine, O., et al. (2012) · Haematologica · doi:10.3324/haematol.2011.044644 · Cited by 55
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Astuti, D., Ricketts, C. J., Chowdhury, R., McDonough, M. A., Gentle, D., Kirby, G. A., Schlisio, S., Kenchappa, R. S., Carter, B. D., Kaelin, W. G., et al. (2010) · Endocrine Related Cancer · doi:10.1677/erc-10-0113 · Cited by 56
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Arsenault, P. R., Pei, F., Lee, R., Kerestes, H., Percy, M. J., Keith, B., Simon, M. C., Lappin, T. R. J., Khurana, T. S., & Lee, F. S. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.482364 · Cited by 54
Self-citationSeeley, T. W., Sternlicht, M. D., Klaus, S. J., Neff, T. B., & Liu, D. Y. (2017) · Hypoxia · doi:10.2147/hp.s130526 · Cited by 54
Recent advances and clinical application of erythropoietin and erythropoiesis-stimulating agents
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Hara, K., Takahashi, N., Wakamatsu, A., & Caltabiano, S. (2015) · Drug Metabolism and Pharmacokinetics · doi:10.1016/j.dmpk.2015.08.004 · Cited by 51
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Al-Sheikh, M., Moradkhani, K., Lopez, M., Wajcman, H., & Préhu, C. (2008) · Blood Cells Molecules and Diseases · doi:10.1016/j.bcmd.2007.07.017 · Cited by 50
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Wang, Z., Zhu, Q., Xia, M., Li, P., Hinton, S. J., & Li, N. (2010) · Hypertension · doi:10.1161/hypertensionaha.109.145896 · Cited by 49
The clinical and laboratory evaluation of the patient with erythrocytosis
Lee, G., & Arcasoy, M. O. (2015) · European Journal of Internal Medicine · doi:10.1016/j.ejim.2015.03.007 · Cited by 48
Searching for molecular hypoxia sensors among oxygen-dependent enzymes
Li, L., Shen, S. Q., Bickler, P. E., Jacobson, M. P., Wu, L. F., & Altschuler, S. J. (2023) · eLife · doi:10.7554/elife.87705 · Cited by 43
Tegley, C. M., Viswanadhan, V. N., Biswas, K., Frohn, M. J., Peterkin, T. A. N., Chang, C. W. T., Bürli, R. W., Dao, J. H., Veith, H., Rogers, N. E., et al. (2008) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2008.06.031 · Cited by 45
Bond, J., Gale, D. P., Connor, T. M. F., Adams, S. P., de Boer, J., Gascoyne, D. M., Williams, O., Maxwell, P. H., & Ancliff, P. (2011) · Blood · doi:10.1182/blood-2010-12-327569 · Cited by 46
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Wu, D.-C., & Paulson, R. F. (2010) · PLoS ONE · doi:10.1371/journal.pone.0011303 · Cited by 43
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A mechanistic link between renal ischemia and fibrosis
Tanaka, T. (2016) · Medical Molecular Morphology · doi:10.1007/s00795-016-0146-3 · Cited by 42
Roles of HIF and 2-Oxoglutarate-Dependent Dioxygenases in Controlling Gene Expression in Hypoxia
Frost, J., Frost, M. G., Batie, M., Jiang, H., & Rocha, S. (2021) · Cancers · doi:10.3390/cancers13020350 · Cited by 47
Genetic causes of erythrocytosis and the oxygen-sensing pathway
Lee, F. S. (2008) · Blood Reviews · doi:10.1016/j.blre.2008.04.003 · Cited by 43
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Li, J., Haase, V. H., & Hao, C. (2022) · Kidney Diseases · doi:10.1159/000527835 · Cited by 42
Prolyl hydroxylase 3 interacts with Bcl-2 to regulate doxorubicin-induced apoptosis in H9c2 cells.
Liu, Y., Huo, Z., Yan, B., Lin, X.-B., Zhou, Z.-N., Liang, X.-Q., Zhu, W., Liang, D.-D., Li, L., Liu, Y., et al. (2010) · Biochemical and Biophysical Research Communications - BBRC · doi:10.1016/j.bbrc.2010.09.037 · Cited by 43
High oxygen affinity hemoglobins
Mangin, O. (2016) · La Revue de Médecine Interne · doi:10.1016/j.revmed.2016.06.003 · Cited by 41
Advances in understanding the pathogenesis of familial myeloproliferative neoplasms
Rumi, E., & Cazzola, M. (2017) · British Journal of Haematology · doi:10.1111/bjh.14713 · Cited by 41
Variations within oxygen-regulated gene expression in humans
Brooks, J., Elvidge, G. P., Glenny, L., Gleadle, J., Liu, C., Ragoussis, J., Smith, T. G., Talbot, N. P., Winchester, L. M., Maxwell, P. H., et al. (2008) · Journal of Applied Physiology · doi:10.1152/japplphysiol.90578.2008 · Cited by 43
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Erythrocytosis associated with a novel missense mutation in the HIF2A gene
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Self-citationTanaka, T., & Nangaku, M. (2009) · Journal of Pharmacological Sciences · doi:10.1254/jphs.08r09fm · Cited by 38
Two new mutations in the HIF2A gene associated with erythrocytosis
Percy, M. J., Chung, Y. J., Harrison, C., Mercieca, J., Hoffbrand, A. V., Dinardo, C. L., Santos, P. C. J. L., Fonseca, G. H. H., Gualandro, S. F. M., Pereira, A. C., et al. (2012) · American Journal of Hematology · doi:10.1002/ajh.23123 · Cited by 37
Self-citationAl-Sheikh, M., Mazurier, E., Gardie, B., Casadevall, N., Galactéros, F., Goossens, M., Wajcman, H., Préhu, C., & Ugo, V. (2008) · Haematologica · doi:10.3324/haematol.12260 · Cited by 37
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Bellanné‐Chantelot, C., Moraes, G. R., Schmaltz-Panneau, B., Marty, C., Vainchenker, W., & Plo, I. (2020) · Blood Reviews · doi:10.1016/j.blre.2020.100710 · Cited by 36
Cario, H., McMullin, M. F., Bento, C., Pospı́šilová, D., Percy, M. J., Hussein, K., Schwarz, J., Åström, M., & Hermouet, S. (2013) · Pediatric Blood & Cancer · doi:10.1002/pbc.24625 · Cited by 35
Self-citationBreakthrough science: hypoxia-inducible factors, oxygen sensing, and disorders of hematopoiesis
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Familial chronic myeloproliferative disorders: the state of the art
Rumi, E. (2008) · Hematological Oncology · doi:10.1002/hon.863 · Cited by 34
Schlisio, S. (2009) · Journal of Cellular and Molecular Medicine · doi:10.1111/j.1582-4934.2009.00881.x · Cited by 33
Structural and mechanistic studies on the peroxisomal oxygenase phytanoyl-CoA 2-hydroxylase (PhyH)
Schofield, C. J., & McDonough, M. A. (2007) · Biochemical Society Transactions · doi:10.1042/bst0350870 · Cited by 32
Tefferi, A., & Pardanani, A. D. (2007) · Mayo Clinic Proceedings · doi:10.4065/82.5.599 · Cited by 33
Genetically heterogeneous origins of idiopathic erythrocytosis
Percy, M. J. (2007) · Hematology · doi:10.1080/10245330601111979 · Cited by 33
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Fiorini, G., & Schofield, C. J. (2024) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2024.102428 · Cited by 33
Su, Y. Y., Loos, M., Giese, N., Metzen, E., Büchler, M. W., Frieß, H., Kornberg, A., & Büchler, P. (2011) · Cancer · doi:10.1002/cncr.26344 · Cited by 31
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MacInnis, M. J., Wang, P., Koehle, M. S., & Rupert, J. L. (2011) · Journal of Occupational and Environmental Medicine · doi:10.1097/jom.0b013e318206b112 · Cited by 34
Grow₂: the HIF system, energy homeostasis and the cell cycle.
Moniz, S., Biddlestone, J., & Rocha, S. (2014) · PubMed · doi:10.14670/hh-29.10.589 · Cited by 30
Schultz, K., Murthy, V., Tatro, J. B., & Beasley, D. (2009) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.90393.2008 · Cited by 32
Albiero, E., Ruggeri, M., Fortuna, S., Finotto, S., Bernardi, M., Madeo, D., & Rodeghiero, F. (2012) · Haematologica · doi:10.3324/haematol.2010.039545 · Cited by 28
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Percy, M. J., & Rumi, E. (2008) · American Journal of Hematology · doi:10.1002/ajh.21313 · Cited by 30
Self-citationPerrotta, S., Stiehl, D. P., Punzo, F., Scianguetta, S., Borriello, A., Bencivenga, D., Casale, M., Nobili, B., Fasoli, S., Balduzzi, A., et al. (2013) · Haematologica · doi:10.3324/haematol.2013.088369 · Cited by 29
Singh, M., Devi, U., Roy, S., Gupta, P. S., Saraf, S. A., & Kaithwas, G. (2016) · Breast Cancer · doi:10.1007/s12282-016-0683-6 · Cited by 28
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McMullin, M. F. (2012) · Therapeutic Advances in Hematology · doi:10.1177/2040620712458947 · Cited by 29
Self-citationRahikkala, E., Myllykoski, M., Hinttala, R., Vieira, P., Nayebzadeh, N., Weiss, S., Plomp, A. S., Bittner, R. E., Kurki, M., Kuismin, O., et al. (2019) · Genetics in Medicine · doi:10.1038/s41436-019-0503-4 · Cited by 27
Jiang, W., Zhang, M., Gao, C., Yan, C., Gao, R., He, Z., Wei, X. L., Xiong, J., Ruan, Z.-L., Yang, Q., et al. (2023) · The EMBO Journal · doi:10.15252/embj.2023113743 · Cited by 30
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Moslehi, J., & Rathmell, W. K. (2019) · Journal of Clinical Investigation · doi:10.1172/jci134813 · Cited by 25
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Self-citationFrohn, M., Viswanadhan, V. N., Pickrell, A. J., Golden, J. E., Muller, K. M., Bürli, R. W., Biddlecome, G. H., Yoder, S. C., Rogers, N. E., Dao, J. H., et al. (2008) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2008.08.012 · Cited by 25
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Metadata
- Authors
- Percy, M. J., Zhao, Q., Flores, A., Harrison, C., Lappin, T. R. J., Maxwell, P. H., McMullin, M. F., & Lee, F. S.
- Affiliations
- Queen's University Belfast (GB)
- ORCID
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 2006-01-09
- Volume
- 103
- Issue
- 3
- Pages
- 654-659
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC1334658
- OpenAlex
- W2059951197
- Cited by
- 330
- References
- 49
- Citations by year
- 2026: 6 · 2025: 7 · 2024: 8 · 2023: 7 · 2022: 5 · 2021: 14 · 2020: 11 · 2019: 9 · 2018: 12 · 2017: 12 · 2016: 20 · 2015: 13 · 2014: 16 · 2013: 22 · 2012: 21
- FWCI
- 19.94
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- UCL Discovery (University College London) (submittedVersion)
- Research Portal (Queen's University Belfast) (submittedVersion)
- Funders
- National Cancer Institute (R01CA090261)
- Topics
- Health Sciences › Medicine › Hematology › Erythropoietin and Anemia Treatment
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Cancer, Hypoxia, and Metabolism
- Health Sciences › Medicine › Genetics (clinical) › Hemoglobinopathies and Related Disorders
- Keywords
- PHD2, familial erythrocytosis, hypoxia-inducible factor, oxygen homeostasis, erythropoietin regulation, von Hippel-Lindau tumor suppressor, erythropoiesis
- MeSH terms
- Adult, Cell Line, Female, Homeostasis, Humans, Isoenzymes, Male, Middle Aged, Oxygen, Polycythemia, Procollagen-Proline Dioxygenase, Protein Binding, Point Mutation, Protein Structure, Tertiary, Immediate-Early Proteins, Amino Acid Substitution, Hypoxia-Inducible Factor 1, alpha Subunit, Hypoxia-Inducible Factor-Proline Dioxygenases
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