The DOI matches its Crossref record; 10 of the 10 references it cites were found in a registry or an index.
Hypoxia-inducible factor 1: Regulator of mitochondrial metabolism and mediator of ischemic preconditioning
Open accessAbstract
Hypoxia-inducible factor 1 (HIF-1) mediates adaptive responses to reduced oxygen availability by regulating gene expression. A critical cell-autonomous adaptive response to chronic hypoxia controlled by HIF-1 is reduced mitochondrial mass and/or metabolism. Exposure of HIF-1-deficient fibroblasts to chronic hypoxia results in cell death due to excessive levels of reactive oxygen species (ROS). HIF-1 reduces ROS production under hypoxic conditions by multiple mechanisms including: a subunit switch in cytochrome c oxidase from the COX4-1 to COX4-2 regulatory subunit that increases the efficiency of complex IV; induction of pyruvate dehydrogenase kinase 1, which shunts pyruvate away from the mitochondria; induction of BNIP3, which triggers mitochondrial selective autophagy; and induction of microRNA-210, which blocks assembly of Fe/S clusters that are required for oxidative phosphorylation. HIF-1 is also required for ischemic preconditioning and this effect may be due in part to its induction of CD73, the enzyme that produces adenosine. HIF-1-dependent regulation of mitochondrial metabolism may also contribute to the protective effects of ischemic preconditioning.
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Cites
1 retracted
Mitochondrial Autophagy Is an HIF-1-dependent Adaptive Metabolic Response to Hypoxia
Zhang, H., Bosch-Marce, M., Shimoda, L. A., Tan, Y. S., Baek, J. H., Wesley, J. B., Gonzalez, F. J., & Semenza, G. L. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m800102200 · Cited by 1,601
Self-citationRetractedOxygen sensing by metazoans: the central role of the HIF hydroxylase pathway.
Kaelin, W. G., & Ratcliffe, P. J. (2008) · Molecular Cell · doi:10.1016/j.molcel.2008.04.009 · Cited by 3,251 · cited 1×
“In the presence of O2, HIF-1α and HIF-2α are subjected to hydroxylation by prolyl-4-hydroxylase domain proteins (PHDs) that use O2 and α-ketoglutarate as substrates and generate CO2 and succinate as by-products [19].”
BackgroundChandel, N. S., McClintock, D. S., Feliciano, C. E., Wood, T. M., Melendez, J. A., Rodriguez, A. M., & Schumacker, P. T. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m001914200 · Cited by 2,000
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 · cited 2×
“(C) HIF-1 activates the transcription of nes alters chromatin structure, which either decreases (as illustrated) or increases the ncodingmicroRNAs that bind to mRNAs and either block their translation or induce their encoding the mismatch DNA repair protein MSH2, thereby functioning as a co-repressor. vation of Notch…”
BackgroundBellot, G., Garcia-Medina, R., Gounon, P., Chiche, J., Roux, D., Pouysségur, J., & Mazure, N. M. (2009) · Molecular and Cellular Biology · doi:10.1128/mcb.00166-09 · Cited by 1,501
Mahon, P. C., Hirota, K., & Semenza, G. L. (2001) · Genes & Development · doi:10.1101/gad.924501 · Cited by 1,385
Self-citationTranscriptional regulation of vascular endothelial cell responses to hypoxia by HIF-1
Manalo, D. J., Rowan, A., Lavoie, T., Natarajan, L., Kelly, B. D., Ye, S. Q., Garcia, J. G. N., & Semenza, G. L. (2005) · Blood · doi:10.1182/blood-2004-07-2958 · Cited by 1,154
Self-citationHypoxia requires Notch signaling to maintain the undifferentiated cell state
Gustafsson, M. V., Zheng, X., Pereira, T., Gradin, K., Jin, S., Lundkvist, J., Ruas, J. L., Poellinger, L., Lendahl, U., & Bondesson, M. (2005) · Developmental Cell · doi:10.1016/j.devcel.2005.09.010 · Cited by 1,109
A MicroRNA Signature of Hypoxia
Kulshreshtha, R., Ferracin, M., Wojcik, S. E., Garzon, R., Alder, H., Agosto-Perez, F. J., Davuluri, R., Liu, C.-G., Croce, C. M., Negrini, M., et al. (2007) · Molecular and Cellular Biology · doi:10.1128/mcb.01395-06 · Cited by 1,055
Chan, S. Y., Zhang, Y.-Y., Hemann, C., Mahoney, C. E., Zweier, J. L., & Loscalzo, J. (2009) · Cell Metabolism · doi:10.1016/j.cmet.2009.08.015 · Cited by 702 · cited 1×
“HIF-1 activates the transcription of the microRNA miR-210 in many cell types [10,31] andmiR-210was shown to block expression of the iron– sulfur cluster assembly proteins ISCU1/2, which are required for the function of the TCA cycle enzyme aconitase and ETC complex I [32].”
Background
Cited by
Reactive Oxygen Species in Metabolic and Inflammatory Signaling
Forrester, S. J., Kikuchi, D. S., Hernandes, M. S., Xu, Q., & Griendling, K. K. (2018) · Circulation Research · doi:10.1161/circresaha.117.311401 · Cited by 2,081
ROS and Autophagy: Interactions and Molecular Regulatory Mechanisms
Li, L., Tan, J., Miao, Y., Lei, P., & Zhang, Q. (2015) · Cellular and Molecular Neurobiology · doi:10.1007/s10571-015-0166-x · Cited by 876
Wu, J., Jiao, Y., Dal Molin, M., Maitra, A., de Wilde, R. F., Wood, L. D., Eshleman, J. R., Goggins, M. G., Wolfgang, C. L., Canto, M. I., et al. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1118046108 · Cited by 640
Cancer metabolism and the Warburg effect: the role of HIF-1 and PI3K
Courtnay, R., Ngo, D. C., Malik, N., Ververis, K., Tortorella, S. M., & Karagiannis, T. C. (2015) · Molecular Biology Reports · doi:10.1007/s11033-015-3858-x · Cited by 567
Mitohormesis: Promoting Health and Lifespan by Increased Levels of Reactive Oxygen Species (ROS)
Ristow, M., & Schmeisser, K. (2014) · Dose-Response · doi:10.2203/dose-response.13-035.ristow · Cited by 534
Metadata
- Authors
- Semenza, G. L.
- Venue
- Biochimica et Biophysica Acta (BBA) - Molecular Cell Research
- Publisher
- Elsevier BV
- Published
- 2011-07
- Volume
- 1813
- Issue
- 7
- Pages
- 1263-1268
- ISSN
- 0167-4889 (ISSN-L)
- OpenAlex
- W2135881241
- Cited by
- 483
- References
- 10
- FWCI
- 16.54
- Type
- journal article
- Language
- en
- Open access
- bronze
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- Semenza, G. L. (2011). Hypoxia-inducible factor 1: Regulator of mitochondrial metabolism and mediator of ischemic preconditioning. Biochimica et Biophysica Acta (BBA) - Molecular Cell Research. https://doi.org/10.1016/j.bbamcr.2010.08.006
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
