The DOI matches its Crossref record; 110 of the 113 references it cites were found in a registry or an index.
Oxygen-dependent regulation of mitochondrial respiration by hypoxia-inducible factor 1
Abstract
The survival of metazoan organisms is dependent upon the utilization of O2 as a substrate for COX (cytochrome c oxidase), which constitutes Complex IV of the mitochondrial respiratory chain. Premature transfer of electrons, either at Complex I or at Complex III, results in the increased generation of ROS (reactive oxygen species). Recent studies have identified two critical adaptations that may function to prevent excessive ROS production in hypoxic cells. First, expression of PDK1 [PDH (pyruvate dehydrogenase) kinase 1] is induced. PDK1 phosphorylates and inactivates PDH, the mitochondrial enzyme that converts pyruvate into acetyl-CoA. In combination with the hypoxia-induced expression of LDHA (lactate dehydrogenase A), which converts pyruvate into lactate, PDK1 reduces the delivery of acetyl-CoA to the tricarboxylic acid cycle, thus reducing the levels of NADH and FADH2 delivered to the electron-transport chain. Secondly, the subunit composition of COX is altered in hypoxic cells by increased expression of the COX4-2 subunit, which optimizes COX activity under hypoxic conditions, and increased degradation of the COX4-1 subunit, which optimizes COX activity under aerobic conditions. Hypoxia-inducible factor 1 controls the metabolic adaptation of mammalian cells to hypoxia by activating transcription of the genes encoding PDK1, LDHA, COX4-2 and LON, a mitochondrial protease that is required for the degradation of COX4-1. COX subunit switching occurs in yeast, but by a completely different regulatory mechanism, suggesting that selection for O2-dependent homoeostatic regulation of mitochondrial respiration is ancient and likely to be shared by all eukaryotic organisms.
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“For example, H2O2-induced oxidation of a cysteine residue located in its catalytic site precisely and rapidly inhibits tyrosine phosphatase (278, 315).”
From Mitochondrial reactive oxygen species production in excitable cells: Modulators of mitochondrial and cell function (2009) · cites this paper as [278]
In the citing paper
“Mitochondria are essential regulators of cellular bioenergetics that respond to changes in environmental stimuli, such as hormones, nutrients, and oxygen tension (47, 94, 99, 109, 290, 301, 385).”
From Redox regulation of mitochondrial function (2012) · cites this paper as [385]
In the citing paper
“HIF-1 coordinately upregulates many genes to regulate metabolism, energy production, and mitochondrial function (385).”
From Redox regulation of mitochondrial function (2012) · cites this paper as [385]
In the citing paper
“Nonetheless, experimental evidence suggests that enhanced ROS production is not a sustained event in hypoxia (69, 385).”
From Redox regulation of mitochondrial function (2012) · cites this paper as [385]
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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
Activation of vascular endothelial growth factor gene transcription by hypoxia-inducible factor 1
Forsythe, J. A., Jiang, B.-H., Iyer, N. V., Agani, F., Leung, S. W., Koos, R. D., & Semenza, G. L. (1996) · Molecular and Cellular Biology · doi:10.1128/mcb.16.9.4604 · Cited by 3,981
Self-citationKim, J.-W., Tchernyshyov, I., Semenza, G. L., & Dang, C. V. (2006) · Cell Metabolism · doi:10.1016/j.cmet.2006.02.002 · Cited by 3,905
Self-citationEpstein, 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
Semenza, G. L., & Wang, G. L. (1992) · Molecular and Cellular Biology · doi:10.1128/mcb.12.12.5447 · Cited by 2,617
Self-citationProgenitor cell trafficking is regulated by hypoxic gradients through HIF-1 induction of SDF-1
Ceradini, D. J., Kulkarni, A. R., Callaghan, M. J., Tepper, O. M., Bastidas, N., Kleinman, M. E., Capla, J. M., Galiano, R. D., Levine, J. P., & Gurtner, G. C. (2004) · Nature Medicine · doi:10.1038/nm1075 · Cited by 2,600
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
Role of HIF-1α in hypoxia-mediated apoptosis, cell proliferation and tumour angiogenesis
Carmeliet, P., Dor, Y., Herbert, J.-M., Fukumura, D., Brusselmans, K., Dewerchin, M., Neeman, M., Bono, F., Abramovitch, R., Maxwell, P., et al. (1998) · Nature · doi:10.1038/28867 · Cited by 2,502
Cellular and developmental control of O 2 homeostasis by hypoxia-inducible factor 1α
Iyer, N. V., Kotch, L. E., Agani, F., Leung, S. W., Laughner, E., Wenger, R. H., Gassmann, M., Gearhart, J. D., Lawler, A. M., Yu, A. Y., et al. (1998) · Genes & Development · doi:10.1101/gad.12.2.149 · Cited by 2,476
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Moon, S., Chang, M.-S., Koh, S.-H., & Choi, Y. K. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22168543 · Cited by 104
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Chowdhury, R., Hardy, A., & Schofield, C. J. (2008) · Chemical Society Reviews · doi:10.1039/b701676j · Cited by 115
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Pinti, M., Gibellini, L., Nasi, M., Biasi, S. D., Bortolotti, C. A., Iannone, A., & Cossarizza, A. (2016) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2016.03.025 · Cited by 110
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Gabryelska, A., Karuga, F. F., Szmyd, B. M., & Białasiewicz, P. (2020) · Frontiers in Physiology · doi:10.3389/fphys.2020.01035 · Cited by 106
Salminen, A., Haapasalo, A., Kauppinen, A., Kaarniranta, K., Soininen, H. S., & Hiltunen, M. O. (2015) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2015.05.001 · Cited by 107
Bensellam, M., Duvillié, B., Rybachuk, G., Laybutt, D. R., Magnan, C., Guiot, Y., Pouysségur, J., & Jonas, J. (2012) · PLoS ONE · doi:10.1371/journal.pone.0029807 · Cited by 109
Permenter, M. G., Lewis, J. A., & Jackson, D. A. (2011) · PLoS ONE · doi:10.1371/journal.pone.0027730 · Cited by 102
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Gasparre, G., Porcelli, A. M., Lenaz, G., & Romeo, G. C. (2013) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a011411 · Cited by 102
Barrientos, A., Gouget, K., Horn, D., Soto, I. C., & Fontanesi, F. (2009) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2008.05.003 · Cited by 99
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Ingavale, S. S., Chang, Y. C., Lee, H., McClelland, C. M., Leong, M. L., & Kwon-Chung, K. J. (2008) · PLoS Pathogens · doi:10.1371/journal.ppat.1000155 · Cited by 78
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Salvadego, D., Domenis, R., Lazzer, S., Porcelli, S., Rittweger, J., Rizzo, G., Mavelli, I., Šimunič, B., Pišot, R., & Grassi, B. (2013) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00883.2012 · Cited by 68
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Baek, J. H., Liu, Y. V., McDonald, K. R., Wesley, J. B., Hubbi, M. E., Byun, H., & Semenza, G. L. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m703504200 · Cited by 65
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He, L., Li, B., Lu, X., Yuan, L., Yang, Y., Yuan, Y., Du, J., & Guo, S. (2015) · Scientific Reports · doi:10.1038/srep11391 · Cited by 62
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Okamoto, A., Sumi, C., Tanaka, H., Kusunoki, M., Iwai, T., Nishi, K., Matsuo, Y., Harada, H., Takenaga, K., Bono, H. U., et al. (2017) · Scientific Reports · doi:10.1038/s41598-017-03980-7 · Cited by 60
Verma, S. K., Jha, E., Panda, P. K., Thirumurugan, A., Parashar, S. K. S., Patro, S., & Suar, M. (2018) · ACS Omega · doi:10.1021/acsomega.7b01522 · Cited by 59
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Contreras-López, R. A., Elizondo-Vega, R. J., Luque‐Campos, N., Torres, M. J., Pradenas, C., Téjédor, G., Paredes-Martínez, M. J., Vega-Letter, A. M., Campos‐Mora, M., Rigual-Gonzalez, Y., et al. (2020) · Theranostics · doi:10.7150/thno.51631 · Cited by 59
Kim, H. K. W., Bian, H., Aya-ay, J., Garces, A. H., Morgan, E. F., & Gilbert, S. R. (2009) · Bone · doi:10.1016/j.bone.2009.03.665 · Cited by 56
Marignac, V. L. M., Smith, S. E., Toban, N., Bazile, M., & Aloyz, R. S. (2013) · Oncotarget · doi:10.18632/oncotarget.1508 · Cited by 54
Magda, D. J., Lecane, P. S., Prescott, J. E., Thiemann, P. A., Ma, X., Dranchak, P. K., TOLENO, D. M., Ramaswamy, K. A., Siegmund, K. D., & Hacia, J. G. (2008) · BMC Genomics · doi:10.1186/1471-2164-9-521 · Cited by 53
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Xu, L., Cao, Y., Ya, X., Li, R., & Xu, X. (2023) · Macromolecular Bioscience · doi:10.1002/mabi.202300238 · Cited by 54
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Merelli, A., Czornyj, L. A., & Lazarowski, A. (2013) · Current Pharmaceutical Design · doi:10.2174/1381612811319380011 · Cited by 53
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Hale, A., Lee, C., Annis, S., Min, P., Pande, R. L., Creager, M. A., Julian, C. G., MOORE, L. G., Mitsialis, S. A., Hwang, S. J., et al. (2014) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2014.06.012 · Cited by 54
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Horowitz, M., & Assadi, H. (2010) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.2009.05101.x · Cited by 53
Pendleton, A. L., Wesolowski, S. R., Regnault, T., Lynch, R., & Limesand, S. (2021) · Frontiers in Endocrinology · doi:10.3389/fendo.2021.612888 · Cited by 43
Richards, J. G., Sardella, B. A., & Schulte, P. M. (2008) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.00192.2008 · Cited by 52
Jia, Y., Guo, Y., Qiu, J., Qu, H., Qi, D., Song, P., Zhang, X., Wang, X., Xu, W., Dong, Y., et al. (2020) · Journal of Experimental & Clinical Cancer Research · doi:10.1186/s13046-020-01547-5 · Cited by 52
Gamma rays induce a p53-independent mitochondrial biogenesis that is counter-regulated by HIF1α
Bartoletti‐Stella, A., Mariani, E., Kurelac, I., Maresca, A., Caratozzolo, M. F., Iommarini, L., Carelli, V., Eusebi, L. H., Guido, A., Cenacchi, G., et al. (2013) · Cell Death and Disease · doi:10.1038/cddis.2013.187 · Cited by 52
Hammoud, M., Vlaski‐Lafarge, M., Duchez, P., Chevaleyre, J., Lafarge, X., Boiron, J.-M., Praloran, V., de la Grange, P. B., & Ivanović, Z. (2011) · Journal of Cellular Physiology · doi:10.1002/jcp.23019 · Cited by 51
Yu, Q., & Chan, S. Y. (2017) · Advances in experimental medicine and biology · doi:10.1007/978-3-319-63245-2_24 · Cited by 51
Wei, X. S., Hou, Y., Long, M., Jiang, L., & Du, Y. (2022) · Frontiers in Endocrinology · doi:10.3389/fendo.2022.927329 · Cited by 58
Metadata
- Authors
- Semenza, G. L.
- Affiliations
- Johns Hopkins University (US)
- Corresponding author
- Semenza, Gregg L.
- ORCID
- Semenza, Gregg L.
- Venue
- Biochemical Journal
- Publisher
- Portland Press Ltd.
- Published
- 2007-06-13
- Volume
- 405
- Issue
- 1
- Pages
- 1-9
- ISSN
- 0264-6021 (ISSN-L)
- 1470-8728
- OpenAlex
- W1799768544
- Cited by
- 541
- References
- 113
- Citations by year
- 2026: 8 · 2025: 9 · 2024: 15 · 2023: 16 · 2022: 19 · 2021: 37 · 2020: 25 · 2019: 27 · 2018: 29 · 2017: 27 · 2016: 29 · 2015: 29 · 2014: 29 · 2013: 36 · 2012: 37
- FWCI
- 3.75
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Biochemical Journal (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health (n01hv28180-13-0-0)
- National Heart, Lung, and Blood Institute (N01 HV-28180, R01HL055338)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Cancer, Hypoxia, and Metabolism
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Keywords
- HIF-1, mitochondrial respiration, cytochrome c oxidase, PDK1, pyruvate dehydrogenase, LDHA, reactive oxygen species, electron transport chain, TCA cycle, Lon protease, oxygen homeostasis
- MeSH terms
- Pyruvate Dehydrogenase Acetyl-Transferring Kinase, Electron Transport Complex IV, Electron Transport, Gene Expression Regulation, Glucose, Glycolysis, Homeostasis, Mitochondria, Oxidative Phosphorylation, Oxygen, Protein Kinases, Protein Serine-Threonine Kinases, Cell Respiration, Hypoxia-Inducible Factor 1
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