The DOI matches its Crossref record; 12 of the 12 references it cites were found in a registry or an index.
Regulation of erythropoietin production
Open accessAbstract
The hormone erythropoietin (Epo) maintains red blood cell mass by promoting the survival, proliferation and differentiation of erythrocytic progenitors. Circulating Epo originates mainly from fibroblasts in the renal cortex. Epo production is controlled at the transcriptional level. Hypoxia attenuates the inhibition of the Epo promoter by GATA‐2. More importantly, hypoxia promotes the availability of heterodimeric (α/β) hypoxia‐inducible transcription factors (predominantly HIF‐2) which stimulate the Epo enhancer. The HIFs are inactivated in normoxia by enzymatic hydroxylation of their α‐subunits. Three HIF‐α prolyl hydroxylases (PHD‐1, ‐2 and ‐3) initiate proteasomal degradation of HIF‐α, while an asparaginyl hydroxylase (‘factor inhibiting HIF‐1’, FIH‐1) inhibits the transactivation potential. The HIF‐α hydroxylases contain Fe 2+ and require 2‐oxoglutarate as co‐factor. The in vivo response is dynamic, i.e. the concentration of circulating Epo increases initially greatly following an anaemic or hypoxaemic stimulus and then declines despite continued hypoxia. Epo and angiotensin II collaborate in the maintenance of the blood volume. Whether extra‐renal sites (brain, skin) modulate renal Epo production is a matter of debate. Epo overproduction results in erythrocytosis. Epo deficiency is the primary cause of the anaemia in chronic kidney disease and a contributing factor in the anaemias of chronic inflammation and cancer. Here, recombinant analogues can substitute for the hormone.
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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
The tumour suppressor protein VHL targets hypoxia-inducible factors for oxygen-dependent proteolysis
Maxwell, P. H., Wiesener, M. S., Chang, G.-W., Clifford, S. C., Vaux, E. C., Cockman, M. E., Wykoff, C. C., Pugh, C. W., Maher, E. R., & Ratcliffe, P. J. (1999) · Nature · doi:10.1038/20459 · Cited by 5,180
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 · cited 2×
“The C-terminus of the HIF-α subunits comprises O2-dependent degradation domains (O-DDD) that are prolyl hydroxylated (at Pro(402) and Pro(564) in HIF-1α, and Pro(405) and Pro(531) in HIF-2α) in the presence of O2 (Epstein et al. 2001; Bruick & McKnight, 2001; Jaakkola et al. 2001; Ivan et al. 2001; Yu et al. 2001).”
BackgroundHuang, L. E., Gu, J., Schau, M., & Bunn, H. F. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.14.7987 · Cited by 2,113
Mahon, P. C., Hirota, K., & Semenza, G. L. (2001) · Genes & Development · doi:10.1101/gad.924501 · Cited by 1,385
HIF-1α binding to VHL is regulated by stimulus-sensitive proline hydroxylation
Yu, F., White, S. B., Zhao, Q., & Lee, F. S. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.181341498 · Cited by 796
Koivunen, P., Hirsilä, M., Günzler, V., Kivirikko, K. I., & Myllyharju, J. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m312254200 · Cited by 447
Proinflammatory Cytokines Lowering Erythropoietin Production
JELKMANN, W. (1998) · Journal of Interferon & Cytokine Research · doi:10.1089/jir.1998.18.555 · Cited by 422
Self-citationMARXSEN, J. H., STENGEL, P., DOEGE, K., HEIKKINEN, P., JOKILEHTO, T., WAGNER, T., JELKMANN, W., JAAKKOLA, P., & METZEN, E. (2004) · Biochemical Journal · doi:10.1042/bj20040620 · Cited by 386
Self-citationHypoxic regulation of erythropoiesis and iron metabolism
Haase, V. H. (2010) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.00174.2010 · Cited by 347
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The sex difference in haemoglobin levels in adults—mechanisms, causes, and consequences
Murphy, W. G. (2014) · Blood Reviews · doi:10.1016/j.blre.2013.12.003 · Cited by 463
The Iron age of host–microbe interactions
Soares, M. P., & Weiss, G. (2015) · The EMBO Reports · doi:10.15252/embr.201540558 · Cited by 227
Hemoglobin mass and intravascular volume kinetics during and after exposure to 3,454-m altitude
Siebenmann, C., Cathomen, A., Hug, M., Keiser, S., Lundby, A. K., Hilty, M. P., Goetze, J. P., Rasmussen, P., & Lundby, C. (2015) · Journal of Applied Physiology · doi:10.1152/japplphysiol.01121.2014 · Cited by 128
Anemia of chronic disorders: new diagnostic tools and new treatment strategies
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Metadata
- Authors
- Jelkmann, W.
- Venue
- The Journal of Physiology
- Publisher
- Wiley
- Published
- 2011-03-14
- Volume
- 589
- Issue
- 6
- Pages
- 1251-1258
- ISSN
- 0022-3751 (ISSN-L)
- 1469-7793
- OpenAlex
- W1515497590
- Cited by
- 599
- References
- 12
- FWCI
- 11.67
- Type
- journal article
- Language
- en
- Open access
- green
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