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Desferrioxamine induces erythropoietin gene expression and hypoxia- inducible factor 1 DNA-binding activity: implications for models of hypoxia signal transduction
Open accessAbstract
Erythropoietin (EPO) gene transcription is activated in kidney cells in vivo and in Hep3B cells exposed to hypoxia or cobalt chloride. Hypoxia- inducible factor 1 (HIF-1) is a nuclear factor that binds to the hypoxia-inducible enhancer of the EPO gene at a site that is required for transcriptional activation. HIF-1 DNA-binding activity is induced by hypoxia or cobalt chloride treatment of Hep3B cells. We report that treatment of Hep3B cells with desferrioxamine (DFX) induced HIF-1 activity and EPO RNA expression with kinetics similar to the induction of HIF-1 by hypoxia or cobalt chloride. Induction by each of these stimuli was inhibited by cycloheximide, indicating a requirement for de novo protein synthesis. DFX appears to induce HIF-1 by chelating iron as induction was inhibited by coadministration of ferrous ammonium sulfate. DFX administration to mice transiently increased EPO RNA levels in the kidney. As previously shown for hypoxia and cobalt treatment, DFX also induced HIF-1 activity in non-EPO-producing cells, suggesting the existence of a common hypoxia signal-transduction pathway leading to HIF-1 induction in different cell types.
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“HIF stabilization can be induced by iron chelators including desferrioxamine and bacterial siderophores [62, 63].”
From Hypoxia and hypoxia-inducible factors as regulators of T cell development, differentiation, and function (2013) · cites this paper as [62]
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Cites
Single-Step Method of RNA Isolation by Acid Guanidinium Thiocyanate–Phenol–Chloroform Extraction
Chomczynski, P., & Sacchi, N. (1987) · Analytical Biochemistry · doi:10.1006/abio.1987.9999 · Cited by 65,515
Semenza, G. L., & Wang, G. L. (1992) · Molecular and Cellular Biology · doi:10.1128/mcb.12.12.5447 · Cited by 2,617
Self-citationGeneral involvement of hypoxia-inducible factor 1 in transcriptional response to hypoxia.
Wang, G. L., & Semenza, G. L. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.9.4304 · Cited by 1,468
Self-citationErythropoietin: structure, control of production, and function
JELKMANN, W. E. B. (1992) · Physiological Reviews · doi:10.1152/physrev.1992.72.2.449 · Cited by 1,167
Regulation of the Erythropoietin Gene: Evidence That the Oxygen Sensor Is a Heme Protein
Goldberg, M. A., Dunning, S. P., & Bunn, H. F. (1988) · Science · doi:10.1126/science.2849206 · Cited by 1,032
Semenza, G. L., Nejfelt, M. K., Chi, S. M., & Antonarakis, S. E. (1991) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.88.13.5680 · Cited by 990
Self-citationCharacterization of hypoxia-inducible factor 1 and regulation of DNA binding activity by hypoxia.
Wang, G. L., & Semenza, G. L. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(20)80571-7 · Cited by 863
Self-citationA haemoprotein with kinase activity encoded by the oxygen sensor of Rhizobium meliloti
Gilles‐Gonzalez, M., Ditta, G. S., & Helinski, D. R. (1991) · Nature · doi:10.1038/350170a0 · Cited by 477
Localization of erythropoietin synthesizing cells in murine kidneys by in situ hybridization
Koury, S., Bondurant, M. C., & Koury, M. (1988) · Blood · doi:10.1182/blood.v71.2.524.524 · Cited by 469
Peritubular cells are the site of erythropoietin synthesis in the murine hypoxic kidney.
Lacombe, C., Silva, J. L. D., Bruneval, P., Fournier, J. G., Wendling, F., Casadevall, N., Camilleri, J.-P., Bariety, J., Varet, B. R., & Tambourin, P. E. (1988) · Journal of Clinical Investigation · doi:10.1172/jci113363 · Cited by 437
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Oxygen-mediated Regulation of Tumor Cell Invasiveness
Postovit, L.-M. M., ADAMS, M. A., Lash, G. E., Heaton, J. P. W., & Graham, C. H. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m204529200 · Cited by 96
Ji, Z., Yang, G., Shahzidi, S., Tkacz-Stachowska, K., Suo, Z., Nesland, J. M., & Peng, Q. (2006) · Cancer Letters · doi:10.1016/j.canlet.2005.12.010 · Cited by 96
Maxwell, P., Pugh, C. W., & Ratcliffe, P. J. (2001) · Advances in experimental medicine and biology · doi:10.1007/978-1-4757-3401-0_24 · Cited by 98
Transferrin Receptor‐Mediated Iron Uptake Promotes Colon Tumorigenesis
Kim, H., Villareal, L., Liu, Z., Haneef, M., Falcon, D. M., Martin, D. R., Lee, H., Dame, M. K., Attili, D., Chen, Y., et al. (2023) · Advanced Science · doi:10.1002/advs.202207693 · Cited by 97
Iron Homeostasis in the Lungs—A Balance between Health and Disease
Neves, J., Haider, T., Gassmann, M., & Muckenthaler, M. U. (2019) · Pharmaceuticals · doi:10.3390/ph12010005 · Cited by 94
The role of calcium in hypoxia-induced signal transduction and gene expression
Seta, K. A., Yuan, Y., Spicer, Z., Lü, G., Bedard, J. E. J., Ferguson, T., Pathrose, P., Cole-Strauss, A., Kaufhold, A., & Millhorn, D. E. (2004) · Cell Calcium · doi:10.1016/j.ceca.2004.02.006 · Cited by 94
Feng, D., Xiang, X., Guan, Y., Guillot, A., Lu, H., Chang, C., He, Y., Wang, H., Pan, H., Ju, C., et al. (2023) · Journal of Clinical Investigation · doi:10.1172/jci166954 · Cited by 93
Li, Q., Chen, H., Huang, X., & Costa, M. (2006) · Toxicology and Applied Pharmacology · doi:10.1016/j.taap.2005.11.006 · Cited by 94
Agani, F. H., & Semenza, G. L. (1998) · Molecular Pharmacology · doi:10.1124/mol.54.5.749 · Cited by 93
Self-citationBeuck, S., Schänzer, W., & Thevis, M. (2012) · Drug Testing and Analysis · doi:10.1002/dta.390 · Cited by 94
Miles, A. L., Burr, S. P., Grice, G. L., & Nathan, J. A. (2017) · eLife · doi:10.7554/elife.22693 · Cited by 95
Complex Role of Heme Oxygenase-1 in Angiogenesis
Dulak, J., Łoboda, A., Zagórska, A., & Józkowicz, A. (2004) · Antioxidants and Redox Signaling · doi:10.1089/ars.2004.6.858 · Cited by 93
Mueller, S., Millonig, G., & Waite, G. N. (2009) · Advances in Medical Sciences · doi:10.2478/v10039-009-0042-3 · Cited by 90
Hoffmann, A., GLOE, T. R., & Pohl, U. (2001) · Journal of Cellular Physiology · doi:10.1002/jcp.1092 · Cited by 95
Zhou, Y., Kim, Y.-P., Li, X., Baerson, S. R., Agarwal, A. K., Hodges, T. W., Ferreira, D., & Nagle, D. G. (2004) · Journal of Natural Products · doi:10.1021/np040140c · Cited by 88
Mohammed, K. A., Hossain, C. F., Zhang, L., Bruick, R. K., Zhou, Y.-D., & Nagle, D. G. (2004) · Journal of Natural Products · doi:10.1021/np049753f · Cited by 88
Epolones induce erythropoietin expression via hypoxia-inducible factor-1α activation
Wanner, R. M., Spielmann, P., Stroka, D., Camenisch, G., Camenisch, I., Scheid, A., Houck, D. R., Bauer, C., Gassmann, M., & Wenger, R. H. (2000) · Blood · doi:10.1182/blood.v96.4.1558.h8001558_1558_1565 · Cited by 88
Flavonoids induce HIF-1α but impair its nuclear accumulation and activity
Triantafyllou, A., Mylonis, I., Simos, G., Bonanou, S., & Tsakalof, A. K. (2007) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2007.10.050 · Cited by 87
Regulation of the iron regulatory proteins by reactive nitrogen and oxygen species.
Hanson, E. S., & Leibold, E. A. (1999) · Europe PMC (PubMed Central) · Cited by 87
Diphenylene Iodonium Inhibits the Induction of Erythropoietin and Other Mammalian Genes by Hypoxia
Gleadle, J., Ebert, B. L., & Ratcliffe, P. J. (1995) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1995.092_c.x · Cited by 87
Yan, L. Y., Colandrea, V. J., & Hale, J. J. (2010) · Expert Opinion on Therapeutic Patents · doi:10.1517/13543776.2010.510836 · Cited by 87
Daijo, H., Hoshino, Y., Kai, S., Suzuki, K., Nishi, K., Matsuo, Y., Harada, H., & Hirota, K. (2016) · Scientific Reports · doi:10.1038/srep34424 · Cited by 88
Hypoxia and inflammatory bowel disease
Cummins, E. P., & Crean, D. (2016) · Microbes and Infection · doi:10.1016/j.micinf.2016.09.004 · Cited by 88
Cerrada, I., Ruiz‐Saurí, A., Carrero, R., Trigueros, C., Dorronsoro, A., Sánchez-Puelles, J.-M., Díez‐Juan, A., Montero, J., & Sepúlveda, P. (2012) · Stem Cells and Development · doi:10.1089/scd.2012.0340 · Cited by 85
Hypoxia induces B-type natriuretic peptide release in cell lines derived from human cardiomyocytes
Casals, G., Ros, J., Sionís, A., Davidson, M. M., Morales‐Ruiz, M., & Jiménez, W. (2009) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00250.2009 · Cited by 83
Responding to Hypoxia: Lessons From a Model Cell Line
Seta, K. A., Spicer, Z., Yuan, Y., Lü, G., & Millhorn, D. E. (2002) · Science Signaling · doi:10.1126/stke.2002.146.re11 · Cited by 85
Kupershmidt, L., Weinreb, O., Amit, T., Mandel, S. A., Bar‐Am, O., & Youdim, M. B. H. (2011) · Neuroscience · doi:10.1016/j.neuroscience.2011.03.040 · Cited by 80
Iron Homeostasis and Its Interaction with Prolyl Hydroxylases
Mole, D. R. (2009) · Antioxidants and Redox Signaling · doi:10.1089/ars.2009.2790 · Cited by 80
Beck, H., Jeske, M., Thede, K., Stoll, F., Flamme, I., Akbaba, M., Ergüden, J., Karig, G., Keldenich, J., Oehme, F., et al. (2018) · ChemMedChem · doi:10.1002/cmdc.201700783 · Cited by 82
Erythropoietin: the story of hypoxia and a finely regulated hematopoietic hormone
Koury, M. J. (2005) · Experimental Hematology · doi:10.1016/j.exphem.2005.06.031 · Cited by 80
Impaired Oxygen-dependent Reduction of HIF-1α and -2α Proteins in Pre-eclamptic Placentae
Rajakumar, A., Doty, K. D., Daftary, A., Harger, G. F., & Conrad, K. P. (2003) · Placenta · doi:10.1016/s0143-4004(03)00081-x · Cited by 78
Sugimoto, R., Kumagai, Y., Nakai, Y., & Ishii, T. (2004) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2004.11.003 · Cited by 78
Hypoxia‐mediated regulation of gene expression in mammalian cells
Shih, S., & Claffey, K. P. (1998) · International Journal of Experimental Pathology · doi:10.1046/j.1365-2613.1998.00088.x · Cited by 79
NRF2 and Hypoxia-Inducible Factors: Key Players in the Redox Control of Systemic Iron Homeostasis
Duarte, T. L., Talbot, N. P., & Drakesmith, H. (2020) · Antioxidants and Redox Signaling · doi:10.1089/ars.2020.8148 · Cited by 77
Therapeutic Manipulation of the HIF Hydroxylases
Nagel, S., Talbot, N. P., Mecinović, J., Smith, T. G., Buchan, A. M., & Schofield, C. J. (2009) · Antioxidants and Redox Signaling · doi:10.1089/ars.2009.2711 · Cited by 77
MiR-483-5p controls angiogenesis in vitro and targets serum response factor
Qiao, Y., Ma, N., Wang, X., Hui, Y., Li, F., Xiang, Y., Zhou, J., Zou, C., Jin, J., Lv, G., et al. (2011) · FEBS Letters · doi:10.1016/j.febslet.2011.08.039 · Cited by 77
Oxygen-sensing under the influence of nitric oxide
Berchner‐Pfannschmidt, U., Tug, S., Kirsch, M., & Fandrey, J. (2009) · Cellular Signalling · doi:10.1016/j.cellsig.2009.10.004 · Cited by 78
Dopamine promotes cellular iron accumulation and oxidative stress responses in macrophages
Dichtl, S., Haschka, D., Nairz, M., Seifert, M., Volani, C., Lutz, O., & Weiss, G. (2018) · Biochemical Pharmacology · doi:10.1016/j.bcp.2017.12.001 · Cited by 76
Ponti, C. D., Carini, R., Alchera, E., Nitti, M. P., Locati, M., Albano, E., Cairo, G., & Tacchini, L. (2007) · Journal of Leukocyte Biology · doi:10.1189/jlb.0107060 · Cited by 78
HIF prolyl hydroxylase inhibitors for anemia
Muchnik, E., & Kaplan, J. (2011) · Expert Opinion on Investigational Drugs · doi:10.1517/13543784.2011.566861 · Cited by 76
Mitochondrial complex III: An essential component of universal oxygen sensing machinery?
Chandel, N. S. (2010) · Respiratory Physiology & Neurobiology · doi:10.1016/j.resp.2010.08.004 · Cited by 81
Jeong, H., Hong, S., Park, R., Shin, T., An, N., & Kim, H. (2005) · Hearing Research · doi:10.1016/j.heares.2005.04.003 · Cited by 77
Taheem, D. K., Foyt, D. A., Loaiza, S., Ferreira, S. A., Ilić, D., Auner, H. W., Grigoriadis, A. E., Jell, G., & Gentleman, E. (2018) · Stem Cells · doi:10.1002/stem.2844 · Cited by 75
Iron and the anemia of chronic disease.
Spivak, J. L. (2002) · PubMed · Cited by 75
Jones, D. T., Trowbridge, I. S., & Harris, A. L. (2006) · Cancer Research · doi:10.1158/0008-5472.can-05-3857 · Cited by 75
Hydrogen sulfide inhibits the translational expression of hypoxia‐inducible factor‐1α
Wu, B., Teng, H., Yang, G., Wu, L., & Wang, R. (2012) · British Journal of Pharmacology · doi:10.1111/j.1476-5381.2012.02113.x · Cited by 74
Cobalt stimulates HIF-1-dependent but inhibits HIF-2-dependent gene expression in liver cancer cells
Befani, C. D., Mylonis, I., Gkotinakou, I., Georgoulias, P., Hu, C., Simos, G., & Liakos, P. (2013) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2013.07.025 · Cited by 75
Role of copper in regression of cardiac hypertrophy
Zheng, L., Han, P., Liu, J., Li, R., Yin, W., Wang, T., Zhang, W., & Kang, Y. J. (2014) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2014.11.014 · Cited by 74
Statin Treatment and 3′ Polyadenylation of eNOS mRNA
Kosmidou, I., Moore, J. P., Weber, M., & Searles, C. D. (2007) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/atvbaha.107.154492 · Cited by 74
Endothelin-2 is a hypoxia-induced autocrine survival factor for breast tumor cells.
Grimshaw, M. J., Naylor, S., & Balkwill, F. R. (2002) · PubMed · Cited by 74
Seta, K. A., Kim, R., Kim, H., Millhorn, D. E., & Beitner‐Johnson, D. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m103346200 · Cited by 74
Role of HIF Signaling on Tumorigenesis in Response to Chronic Low-Dose Arsenic Administration
Kamat, C. D., Green, D. E., Curilla, S., Warnke, L. A., Hamilton, J. W., Stürup, S., Clark, C., & Ihnat, M. A. (2005) · Toxicological Sciences · doi:10.1093/toxsci/kfi190 · Cited by 72
Oxygen-regulated Expression of TGF-β3, a Growth Factor Involved in Trophoblast Differentiation
Schäffer, L., Scheid, A., Spielmann, P., Breymann, C., Zimmermann, R., Meuli, M., Gassmann, M., Marti, H. H., & Wenger, R. H. (2003) · Placenta · doi:10.1016/s0143-4004(03)00166-8 · Cited by 74
Ferriero, D. M. (2005) · Epilepsia · doi:10.1111/j.1528-1167.2005.00302.x · Cited by 72
Sadek, C. M., Jalaguier, S., Feeney, E. P., Aitola, M., Damdimopoulos, A. E., Pelto‐Huikko, M., & Gustafsson, J.-Å. (2000) · Mechanisms of Development · doi:10.1016/s0925-4773(00)00415-9 · Cited by 72
Zhou, Y., Kim, Y.-P., Mohammed, K. A., Jones, D. K., Muhammad, I., Dunbar, D. C., & Nagle, D. G. (2005) · Journal of Natural Products · doi:10.1021/np050029m · Cited by 72
Saururus cernuus lignans—Potent small molecule inhibitors of hypoxia-inducible factor-1
Hossain, C. F., Kim, Y.-P., Baerson, S. R., Zhang, L., Bruick, R. K., Mohammed, K. A., Agarwal, A. K., Nagle, D. G., & Zhou, Y.-D. (2005) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2005.05.191 · Cited by 74
Deng, A., Arndt, M. A., Satriano, J. A., Singh, P., Rieg, T., Thomson, S. C., Tang, T., & Blantz, R. C. (2010) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.00153.2010 · Cited by 71
Nickel, D., Busch, M., Mayer, D., Hagemann, B., Knoll, V., & Stenger, S. (2012) · The Journal of Immunology · doi:10.4049/jimmunol.1100976 · Cited by 74
Ascorbate Depletion: A Critical Step in Nickel Carcinogenesis?
Salnikow, K., & Kasprzak, K. S. (2005) · Environmental Health Perspectives · doi:10.1289/ehp.7605 · Cited by 72
Huang, E. L., Ho, V. T., Arany, Z. P., Krainc, D., Galson, D. L., Tendler, D. S., Livingston, D. M., & Bunn, H. F. (1997) · Kidney International · doi:10.1038/ki.1997.76 · Cited by 71
Zhang, T., Xu, D., Liu, J., Wang, M., Duan, L., Liu, M., Meng, H., Zhuang, Y., Wang, H., Wang, Y., et al. (2023) · Nature Cell Biology · doi:10.1038/s41556-023-01170-4 · Cited by 73
Control of Erythropoietin Gene Expression and its Use in Medicine
JELKMANN, W. E. B. (2007) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(07)35010-6 · Cited by 72
Regulatory role of vHL/HIF-1α in hypoxia-induced VEGF production in hepatic stellate cells
Wang, Y. Q., Luk, J. M., Ikeda, K., Man, K., Chu, A. C. Y., Kaneda, K., & Fan, S. T. (2004) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2004.03.050 · Cited by 71
Veschini, L., Belloni, D., Foglieni, C., Cangi, M. G., Ferrarini, M., Caligaris‐Cappio, F., & Ferrero, E. (2006) · Blood · doi:10.1182/blood-2006-06-032664 · Cited by 71
Hypoxia‐induced pathways in breast cancer
Goonewardene, T. I., Sowter, H., & Harris, A. L. (2002) · Microscopy Research and Technique · doi:10.1002/jemt.10175 · Cited by 71
Targeting hypoxia-inducible factor 1 to stimulate tissue vascularization
Semenza, G. L. (2015) · Journal of Investigative Medicine · doi:10.1097/jim.0000000000000206 · Cited by 70
Self-citationErythropoietin and derivatives: Potential beneficial effects on the brain
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Transcriptional regulation of heme oxygenases by HIF-1α in renal medullary interstitial cells
Yang, Z.-Z., & Zou, A.-P. (2001) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.2001.281.5.f900 · Cited by 69
Organ Protection by Hypoxia and Hypoxia‐Inducible Factors
Bernhardt, W. M., Warnecke, C., Willam, C., Tanaka, T., Wiesener, M. S., & Eckardt, K. (2007) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(07)35012-x · Cited by 70
Deferoxamine induces prolonged cardiac preconditioning via accumulation of oxygen radicals
Dendorfer, A., Heidbreder, M., Hellwig-Bürgel, T., Jöhren, O., Qadri, F., & Dominiak, P. (2005) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2004.10.015 · Cited by 68
Natural Product-Derived Small Molecule Activators of Hypoxia-Inducible Factor-1 (HIF-1)
Nagle, D. G., & Zhou, Y. (2006) · Current Pharmaceutical Design · doi:10.2174/138161206777698783 · Cited by 68
Characterization of Physiologically Regulated Vectors for the Treatment of Ischemic Disease
Boast, K., Binley, K., Iqball, S., Price, T., Spearman, H., Kingsman, S. M., Kingsman, A. J., & Naylor, S. (1999) · Human Gene Therapy · doi:10.1089/10430349950017185 · Cited by 67
Desferrioxamine elevates pulmonary vascular resistance in humans: potential for involvement of HIF-1
Balanos, G. M., Dorrington, K. L., & Robbins, P. A. (2002) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00965.2001 · Cited by 69
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Jeong, H., Oh, H., Nam, S., Han, N., Kim, Y., Kim, J., Lee, S., Kim, M., Moon, P., Kim, H., et al. (2012) · International Journal of Cancer · doi:10.1002/ijc.27937 · Cited by 66
Effects of desferrioxamine on serum erythropoietin and ventilatory sensitivity to hypoxia in humans
Ren, X., Dorrington, K. L., Maxwell, P. H., & Robbins, P. A. (2000) · Journal of Applied Physiology · doi:10.1152/jappl.2000.89.2.680 · Cited by 66
Hypoxic up-regulation of erythroid 5-aminolevulinate synthase
Höfer, T., Wenger, R. H., Kramer, M. F., Ferreira, G. C., & Gassmann, M. (2002) · Blood · doi:10.1182/blood-2002-03-0773 · Cited by 66
Hypoxia and cobalt stimulate lactate dehydrogenase (LDH) activity in vascular smooth muscle cells
Marti, H. H., Jung, H. H., Pfeilschifter, J. M., & Bauer, C. (1994) · Pflügers Archiv - European Journal of Physiology · doi:10.1007/bf00374315 · Cited by 64
Li, Z., You, Q., & Zhang, X. (2019) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.8b01596 · Cited by 64
Zeng, L., Yang, K., Yu, G., Hao, W., Zhu, X., Ge, A., Chen, J., & Sun, L. (2024) · Cell Death and Disease · doi:10.1038/s41419-024-06807-2 · Cited by 66
Roudkenar, M. H., Halabian, R., Roushandeh, A. M., Nourani, M. R., Masroori, N., Ebrahimi, M., Nikogoftar, M., Rouhbakhsh, M., Bahmani, P., Jahanian‐Najafabadi, A., et al. (2009) · Experimental Cell Research · doi:10.1016/j.yexcr.2009.08.019 · Cited by 62
Catrina, S., Botusan, I. R., Rantanen, A., Catrina, A. I., Pyakurel, P., Savu, O., Axelson, M., Biberfeld, P., Poellinger, L., & Brismar, K. (2006) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-05-2473 · Cited by 63
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HIF1α-dependent mitophagy facilitates cardiomyoblast differentiation
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Khurana, A., Liu, P., Mellone, P., Lorenzon, L., Vincenzi, B., Datta, K., Yang, B., Linhardt, R. J., Lingle, W. L., CHIEN, J. R., et al. (2011) · Cancer Research · doi:10.1158/0008-5472.can-10-3059 · Cited by 65
Callapina, M., Zhou, J., Schnitzer, S. E., Metzen, E., Lohr, C., Deitmer, J. W., & Brüne, B. (2005) · Experimental Cell Research · doi:10.1016/j.yexcr.2005.02.018 · Cited by 61
Dai, J., Fishback, J. A., Zhou, Y., & Nagle, D. G. (2006) · Journal of Natural Products · doi:10.1021/np060278q · Cited by 60
Wilson, J. L., Burchell, J., & Grimshaw, M. J. (2006) · Cancer Research · doi:10.1158/0008-5472.can-06-1222 · Cited by 60
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Jiang, B., Ren, C., Li, Y., Lu, Y., Li, W., Wu, Y., Gao, Y., Ratcliffe, P. J., Liu, H., & Zhang, C. (2010) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s00775-010-0723-1 · Cited by 61
Piccoli, C., D’Aprile, A., Ripoli, M. C., Scrima, R., Boffoli, D., Tabilio, A., & Capitanio, N. (2007) · FEBS Letters · doi:10.1016/j.febslet.2007.05.077 · Cited by 59
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Self-citationNagao, M., Ebert, B. L., Ratcliffe, P. J., & Pugh, C. W. (1996) · FEBS Letters · doi:10.1016/0014-5793(96)00484-x · Cited by 58
Ioannou, M., Papamichali, R., Kouvaras, E., Mylonis, I., Vageli, D., Kerenidou, T., Barbanis, S., Daponte, A., Simos, G., Gourgoulianis, K., et al. (2009) · Lung · doi:10.1007/s00408-009-9169-z · Cited by 57
Hara, A., Niwa, M., Aoki, H., Kumada, M., Kunisada, T., Oyama, T., Yamamoto, T., Kozawa, O., & Mori, H. (2006) · Brain Research · doi:10.1016/j.brainres.2006.06.037 · Cited by 57
Coma, S., Shimizu, A., & Klagsbrun, M. (2011) · Cell Adhesion & Migration · doi:10.4161/cam.5.3.16294 · Cited by 57
Metadata
- Authors
- Wang, G., & Semenza, G.
- Affiliations
- Johns Hopkins University (US)
- Venue
- Blood
- Publisher
- American Society of Hematology
- Published
- 1993-12-15
- Volume
- 82
- Issue
- 12
- Pages
- 3610-3615
- ISSN
- 0006-4971 (ISSN-L)
- 1528-0020
- OpenAlex
- W1545825939
- Cited by
- 766
- References
- 33
- Citations by year
- 2026: 4 · 2025: 9 · 2024: 12 · 2023: 24 · 2022: 18 · 2021: 26 · 2020: 24 · 2019: 18 · 2018: 19 · 2017: 17 · 2016: 34 · 2015: 24 · 2014: 26 · 2013: 26 · 2012: 32
- FWCI
- 5.23
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Blood (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health (5r01dk039869-16)
- National Institute of Diabetes and Digestive and Kidney Diseases (DK 39869)
- Topics
- Health Sciences › Medicine › Hematology › Erythropoietin and Anemia Treatment
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Cancer, Hypoxia, and Metabolism
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Hemoglobin structure and function
- Keywords
- deferoxamine, erythropoietin gene expression, HIF-1, iron chelation, cobalt chloride, Hep3B cells, ferrous ammonium sulfate, cycloheximide, de novo protein synthesis
- MeSH terms
- Base Sequence, Cell Line, Cell Nucleus, Cobalt, Deferoxamine, DNA-Binding Proteins, Erythropoietin, Humans, Liver Neoplasms, Molecular Sequence Data, Nuclear Proteins, RNA, Neoplasm, Transcription Factors, Tumor Cells, Cultured, Oligonucleotide Probes, Signal Transduction, Cell Hypoxia, Gene Expression, Hepatoblastoma, Hypoxia-Inducible Factor 1, Hypoxia-Inducible Factor 1, alpha Subunit
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