Cited by 334Erythropoietin and Anemia TreatmentCancer, Hypoxia, and MetabolismHemoglobinopathies and Related Disorders

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A family with erythrocytosis establishes a role for prolyl hydroxylase domain protein 2 in oxygen homeostasis

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Percy, Melanie J., Zhao, Quan, Flores, Adrian, Harrison, Claire, Lappin, Terence R. J., Maxwell, Patrick H., McMullin, Mary Frances, Lee, Frank S.·2006·Proceedings of the National Academy of Sciences

DOI 10.1073/pnas.0508423103PMC PMC1334658

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Abstract

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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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: Zhao, Quan
Harrison, Claire
Lappin, Terence R. J.
Maxwell, Patrick H.
McMullin, Mary Frances
Lee, Frank S.
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
DOI: 10.1073/pnas.0508423103
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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A family with erythrocytosis establishes a role for prolyl hydroxylase domain protein 2 in oxygen homeostasis

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