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Inhibition of Hypoxia-inducible Factor (HIF) Hydroxylases by Citric Acid Cycle Intermediates
Open accessAbstract
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 K(i) values of 50-80 microM and succinate 350-460 microM, whereas neither inhibited FIH. Oxaloacetate was an additional inhibitor of all three HIF-P4Hs with K(i) values of 400-1000 microM and citrate of HIF-P4H-3, citrate being the most effective inhibitor of FIH with a K(i) of 110 microM. Culturing of cells with fumarate diethyl or dimethyl ester, or a high concentration of monoethyl ester, stabilized HIF-1alpha and increased production of vascular endothelial growth factor and erythropoietin. Similar, although much smaller, changes were found in cultured fibroblasts from a patient with fumarate hydratase (FH) deficiency and upon silencing FH using small interfering RNA. No such effects were seen upon culturing of cells with succinate diethyl or dimethyl ester. As FIH was not inhibited by fumarate, our data indicate that the transcriptional activity of HIF is quite high even when binding of the coactivator p300 is prevented. Our data also support recent suggestions that the increased fumarate and succinate levels present in the FH and succinate dehydrogenase-deficient tumors, respectively, can inhibit the HIF-P4Hs with consequent stabilization of HIF-alphas and effects on tumor pathology.
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“Loss-of-function mutations in SDH and FH cause a build-up of succinate and fumarate, respectively87. Accordingly, increased levels of succinate and fumarate caused by mutations in these genes can compete with αKG and inhibit activity of HIF hydroxylases and thus induce normoxic HIF1α activity in vitro88,89.”
From Targeting cancer vulnerabilities with high-dose vitamin C (2019) · cites this paper as [89]
Citations
Cites
Targeting HIF-1 for cancer therapy
Semenza, G. L. (2003) · Nature Reviews Cancer · doi:10.1038/nrc1187 · Cited by 6,717
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
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
A 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
Succinate links TCA cycle dysfunction to oncogenesis by inhibiting HIF-α prolyl hydroxylase
Selak, M. A., Armour, S. M., MacKenzie, E. D., Boulahbel, H., Watson, D. G., Mansfield, K. D., Pan, Y., Simon, M. C., Thompson, C. B., & Gottlieb, E. (2005) · Cancer Cell · doi:10.1016/j.ccr.2004.11.022 · Cited by 2,108
Oxygen sensing by HIF hydroxylases
Schofield, C. J., & Ratcliffe, P. J. (2004) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1366 · Cited by 2,068
The Multiple Leiomyoma Consortium (2002) · Nature Genetics · doi:10.1038/ng849 · Cited by 1,635
Asparagine Hydroxylation of the HIF Transactivation Domain: A Hypoxic Switch
Lando, D., Peet, D. J., Whelan, D. A., Gorman, J. J., & Whitelaw, M. L. (2002) · Science · doi:10.1126/science.1068592 · Cited by 1,558
Lando, D., Peet, D. J., Gorman, J. J., Whelan, D. A., Whitelaw, M. L., & Bruick, R. K. (2002) · Genes & Development · doi:10.1101/gad.991402 · Cited by 1,550
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Hu, S., Lin, Z., Zhao, Z., Liu, R., Ma, L., Luo, H., Zhou, F., & Bai, X. (2015) · Journal of Parenteral and Enteral Nutrition · doi:10.1177/0148607115577817 · Cited by 26
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Rapizzi, E., Fucci, R., Giannoni, E., Canu, L., Richter, S., Cirri, P., & Mannelli, M. (2015) · Endocrine Related Cancer · doi:10.1530/erc-14-0479 · Cited by 26
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van Patot, M. C. T., Serkova, N. J., Haschke, M., Kominsky, D. J., Roach, R. C., Christians, U., Henthorn, T. K., & Honigman, B. (2009) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2009.03.009 · Cited by 26
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Czibik, G. (2010) · Journal of Molecular Medicine · doi:10.1007/s00109-010-0646-x · Cited by 27
Alnahhas, N., Pouliot, É., & Saucier, L. (2023) · Frontiers in Physiology · doi:10.3389/fphys.2023.1260987 · Cited by 26
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Xiao, W., Shrimali, N. M., Vigder, N., Oldham, W. M., Clish, C. B., He, H., Wong, S. J., Wertheim, B. M., Arons, E., Haigis, M. C., et al. (2024) · Nature Metabolism · doi:10.1038/s42255-024-01150-4 · Cited by 27
Brewitz, L., Nakashima, Y., & Schofield, C. J. (2020) · Chemical Science · doi:10.1039/d0sc04301j · Cited by 25
Proline dehydrogenase in cancer: apoptosis, autophagy, nutrient dependency and cancer therapy
Liu, Y., Mao, C., Liu, S., Xiao, D., Shi, Y., & Tao, Y. (2021) · Amino Acids · doi:10.1007/s00726-021-03032-5 · Cited by 25
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Ma, C., Zhu, C., Zhang, Y., Yu, M., Song, Y., Chong, Y., Yang, Y., Zhu, C., Jiang, Y., Wang, C., et al. (2023) · Phytomedicine · doi:10.1016/j.phymed.2023.155266 · Cited by 23
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Lückmann, M., Trauelsen, M., Frimurer, T. M., & Schwartz, T. W. (2020) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2019.12.005 · Cited by 23
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Hypoxia‐inducible factors – regulation, role and comparative aspects in tumourigenesis
Hansen, A. E., Kristensen, A. T., Law, I. G., Jørgensen, J. T., & Engelholm, S. A. (2010) · Veterinary and Comparative Oncology · doi:10.1111/j.1476-5829.2010.00233.x · Cited by 23
Paddenberg, R., Tiefenbach, M., Faulhammer, P., Goldenberg, A., Gries, B., Pfeil, U., Lips, K. S., Piruat, J. I., López‐Barneo, J., SCHERMULY, R. T., et al. (2012) · Cardiovascular Research · doi:10.1093/cvr/cvr359 · Cited by 22
van der Wel, H., Johnson, J. M., Xu, Y., Karunaratne, C. V., Wilson, K. D., Vohra, Y., Boons, G., Taylor, C. M., Bendiak, B. K., & West, C. M. (2011) · Biochemistry · doi:10.1021/bi101977w · Cited by 21
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Noguchi, S., Ishikawa, H., Wakita, K., Matsuda, F., & Shimizu, H. (2020) · Scientific Reports · doi:10.1038/s41598-020-70000-6 · Cited by 12
Mreisat, A., Kanaani, H., Saada, A., & Horowitz, M. (2020) · Journal of Thermal Biology · doi:10.1016/j.jtherbio.2020.102691 · Cited by 12
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Kaelin, W. G. (2010) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.2010.05781.x · Cited by 12
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Gregorio, E. D., Miolo, G., Saorin, A., Steffan, A., & Corona, G. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22115574 · Cited by 11
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Metadata
- Authors
- Koivunen, P., Hirsilä, M., Remes, A. M., Hassinen, I. E., Kivirikko, K. I., & Myllyharju, J.
- Affiliations
- University of Oulu (FI)
- Corresponding author
- Myllyharju, Johanna
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2007-02
- Volume
- 282
- Issue
- 7
- Pages
- 4524-4532
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2004183689
- Semantic Scholar
- c3ddd6b07c5b433f324955c53930fb199e6ecc2a
- Cited by
- 521
- References
- 43
- Citations by year
- 2026: 15 · 2025: 17 · 2024: 23 · 2023: 23 · 2022: 23 · 2021: 39 · 2020: 25 · 2019: 38 · 2018: 25 · 2017: 28 · 2016: 29 · 2015: 33 · 2014: 29 · 2013: 36 · 2012: 32
- FWCI
- 7.09
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Cancer, Hypoxia, and Metabolism
- Health Sciences › Medicine › Hematology › Erythropoietin and Anemia Treatment
- Physical Sciences › Chemistry › Inorganic Chemistry › Metal-Catalyzed Oxygenation Mechanisms
- Keywords
- hypoxia-inducible factor, FIH, citric acid cycle intermediates, fumarate, succinic acid, oxaloacetate, citrate, fumarate hydratase deficiency, succinate dehydrogenase deficiency, HIF-1α stabilization, vascular endothelial growth factor, erythropoietin, p300 coactivator, cancer metabolism
- MeSH terms
- Cell Line, Citric Acid Cycle, Dose-Response Relationship, Drug, Enzyme Inhibitors, Erythropoietin, Fibroblasts, Fumarate Hydratase, Mixed Function Oxygenases, Neoplasms, Procollagen-Proline Dioxygenase, Succinate Dehydrogenase, Transcription, Genetic, Gene Expression Regulation, Enzymologic, Vascular Endothelial Growth Factor A, p300-CBP Transcription Factors, Hypoxia-Inducible Factor 1, alpha Subunit
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