{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,11,7]],"date-time":"2026-11-07T10:29:11Z","timestamp":1794047351090,"version":"4.8.0"},"reference-count":73,"publisher":"Ferrata Storti Foundation (Haematologica)","issue":"2","license":[{"start":{"date-parts":[[2020,3,19]],"date-time":"2020-03-19T00:00:00Z","timestamp":1584576000000},"content-version":"unspecified","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by-nc\/4.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["haematol"],"abstract":"<jats:p>Hypoferremia results as an acute phase response to infection and inflammation aiming to reduce iron availability to pathogens. Activation of toll-like receptors (TLRs), the key sensors of the innate immune system, induces hypoferremia mainly through the rise of the iron hormone hepcidin. Conversely, stimulation of erythropoiesis suppresses hepcidin expression via induction of the erythropoietin-responsive hormone erythroferrone. Iron deficiency stimulates transcription of the osteocyte-secreted protein FGF23. Here we hypothesized that induction of FGF23 in response to TLR4 activation is a potent contributor to hypoferremia and, thus, impairment of its activity may alleviate hypoferremia induced by lipopolysaccharide (LPS), a TLR 4 agonist. We used the C-terminal tail of FGF23 to impair endogenous full-length FGF23 signaling in wild-type mice, and investigated its impact on hypoferremia. Our data show that FGF23 is induced as early as pro-inflammatory cytokines in response to LPS, followed by upregulation of hepcidin and downregulation of erythropoietin (Epo) expression in addition to decreased serum iron and transferrin saturation. Further, LPS-induced hepatic and circulating hepcidin were significantly reduced by FGF23 signaling disruption. Accordingly, iron sequestration in liver and spleen caused by TLR4 activation was completely abrogated by FGF23 signaling inhibition, resulting in alleviation of serum iron and transferrin saturation deficit. Taken together, our studies highlight for the first time that inhibition of FGF23 signaling alleviates LPS-induced acute hypoferremia.<\/jats:p>","DOI":"10.3324\/haematol.2019.237040","type":"journal-article","created":{"date-parts":[[2020,3,19]],"date-time":"2020-03-19T16:35:18Z","timestamp":1584635718000},"page":"391-403","source":"Crossref","is-referenced-by-count":29,"title":["C-FGF23 peptide alleviates hypoferremia during acute inflammation"],"prefix":"10.3324","volume":"106","author":[{"family":"Rafiou Agoro","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"family":"Min Young Park","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"family":"Carole Le Henaff","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"family":"Stanislovas Jankauskas","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"family":"Alina Gaias","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"family":"Gaozhi Chen","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"family":"Moosa Mohammadi","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"family":"Despina Sitara","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1856","published-online":{"date-parts":[[2020,3,19]]},"reference":[{"key":"19809","doi-asserted-by":"crossref","unstructured":"Gozzelino R, Arosio P. Iron homeostasis in health and disease. Int J Mol Sci. 2016; 17(1)Google Scholar","DOI":"10.3390\/ijms17010130"},{"key":"19810","doi-asserted-by":"crossref","unstructured":"Layoun A, Huang H, Calve A, Santos MM. Toll-like receptor signal adaptor protein MyD88 is required for sustained endotoxin- induced acute hypoferremic response in mice. Am J Pathol. 2012; 180(6):2340-2350.","DOI":"10.1016\/j.ajpath.2012.01.046"},{"key":"19811","doi-asserted-by":"crossref","unstructured":"Schmidt PJ. Regulation of iron metabolism by hepcidin under conditions of inflammation. J Biol Chem. 2015; 290(31):18975-18983.","DOI":"10.1074\/jbc.R115.650150"},{"key":"19812","doi-asserted-by":"crossref","unstructured":"Ganz T. Hepcidin, a key regulator of iron metabolism and mediator of anemia of inflammation. Blood. 2003; 102(3):783-788.","DOI":"10.1182\/blood-2003-03-0672"},{"key":"19813","doi-asserted-by":"crossref","unstructured":"Kemna E, Pickkers P, Nemeth E, van der Hoeven H, Swinkels D. Time-course analysis of hepcidin, serum iron, and plasma cytokine levels in humans injected with LPS. Blood. 2005; 106(5):1864-1866.","DOI":"10.1182\/blood-2005-03-1159"},{"key":"19814","doi-asserted-by":"crossref","unstructured":"Nemeth E, Valore EV, Territo M, Schiller G, Lichtenstein A, Ganz T. Hepcidin, a putative mediator of anemia of inflammation, is a type II acute-phase protein. Blood. 2003; 101(7):2461-2463.","DOI":"10.1182\/blood-2002-10-3235"},{"key":"19815","doi-asserted-by":"crossref","unstructured":"Nemeth E, Tuttle MS, Powelson J. Hepcidin regulates cellular iron efflux by binding to ferroportin and inducing its internalization. Science. 2004; 306(5704):2090-2093.","DOI":"10.1126\/science.1104742"},{"key":"19816","doi-asserted-by":"crossref","unstructured":"Ganz T, Nemeth E. Iron homeostasis in host defence and inflammation. Nat Rev Immunol. 2015; 15(8):500-510.","DOI":"10.1038\/nri3863"},{"key":"19817","doi-asserted-by":"crossref","unstructured":"Weiss G. Iron metabolism in the anemia of chronic disease. Biochim Biophys Acta. 2009; 1790(7):682-693.","DOI":"10.1016\/j.bbagen.2008.08.006"},{"key":"19818","doi-asserted-by":"crossref","unstructured":"Babitt JL, Lin HY. Mechanisms of anemia in CKD. J Am Soc Nephrol. 2012; 23(10):1631-1634.","DOI":"10.1681\/ASN.2011111078"},{"key":"19819","doi-asserted-by":"crossref","unstructured":"Wolf M. Update on fibroblast growth factor 23 in chronic kidney disease. Kidney Int. 2012; 82(7):737-747.","DOI":"10.1038\/ki.2012.176"},{"key":"19820","doi-asserted-by":"crossref","unstructured":"David V, Martin A, Isakova T, Spaulding C, Qi L, Ramirez V. Inflammation and functional iron deficiency regulate fibroblast growth factor 23 production. Kidney Int. 2016; 89(1):135-146.","DOI":"10.1038\/ki.2015.290"},{"key":"19821","doi-asserted-by":"crossref","unstructured":"Farrow EG, Yu X, Summers LJ. Iron deficiency drives an autosomal dominant hypophosphatemic rickets (ADHR) phenotype in fibroblast growth factor-23 (Fgf23) knock-in mice. Proc Natl Acad Sci U S A. 2011; 108(46):E1146-55.","DOI":"10.1073\/pnas.1110905108"},{"key":"19822","doi-asserted-by":"crossref","unstructured":"White KE, Carn G, Lorenz-Depiereux B, Benet-Pages A, Strom TM, Econs MJ. Autosomal-dominant hypophosphatemic rickets (ADHR) mutations stabilize FGF-23. Kidney Int. 2001; 60(6):2079-2086.","DOI":"10.1046\/j.1523-1755.2001.00064.x"},{"key":"19823","doi-asserted-by":"crossref","unstructured":"Shimada T, Mizutani S, Muto T. Cloning and characterization of FGF23 as a causative factor of tumor-induced osteomalacia. Proc Natl Acad Sci U S A. 2001; 98(11):6500-6505.","DOI":"10.1073\/pnas.101545198"},{"key":"19824","doi-asserted-by":"crossref","unstructured":"Perwad F, Zhang MY, Tenenhouse HS, Portale AA. Fibroblast growth factor 23 impairs phosphorus and vitamin D metabolism in vivo and suppresses 25-hydroxyvitamin D-1alpha-hydroxylase expression in vitro. Am J Physiol Renal Physiol. 2007; 293(5):F1577-1583.","DOI":"10.1152\/ajprenal.00463.2006"},{"key":"19825","doi-asserted-by":"crossref","unstructured":"Shimada T, Hasegawa H, Yamazaki Y. FGF-23 is a potent regulator of vitamin D metabolism and phosphate homeostasis. J Bone Miner Res. 2004; 19(3):429-435.","DOI":"10.1359\/JBMR.0301264"},{"key":"19826","doi-asserted-by":"crossref","unstructured":"Sitara D, Kim S, Razzaque MS. Genetic evidence of serum phosphateindependent functions of FGF-23 on bone. PLoS Genet. 2008; 4(8):e1000154.","DOI":"10.1371\/journal.pgen.1000154"},{"key":"19827","doi-asserted-by":"crossref","unstructured":"Sitara D, Razzaque MS, Hesse M. Homozygous ablation of fibroblast growth factor-23 results in hyperphosphatemia and impaired skeletogenesis, and reverses hypophosphatemia in Phex-deficient mice. Matrix Biol. 2004; 23(7):421-432.","DOI":"10.1016\/j.matbio.2004.09.007"},{"key":"19828","doi-asserted-by":"crossref","unstructured":"Sitara D, Razzaque MS, St-Arnaud R. Genetic ablation of vitamin D activation pathway reverses biochemical and skeletal anomalies in Fgf-23-null animals. Am J Pathol. 2006; 169(6):2161-2170.","DOI":"10.2353\/ajpath.2006.060329"},{"key":"19829","doi-asserted-by":"crossref","unstructured":"Eicher EM, Southard JL, Scriver CR, Glorieux FH. Hypophosphatemia: mouse model for human familial hypophosphatemic (vitamin D-resistant) rickets. Proc Natl Acad Sci U S A. 1976; 73(12):4667-4671.","DOI":"10.1073\/pnas.73.12.4667"},{"key":"19830","doi-asserted-by":"crossref","unstructured":"Loffing J, Lotscher M, Kaissling B. Renal Na\/H exchanger NHE-3 and Na-PO4 cotransporter NaPi-2 protein expression in glucocorticoid excess and deficient states. J Am Soc Nephrol. 1998; 9(9):1560-1567.","DOI":"10.1681\/ASN.V991560"},{"key":"19831","doi-asserted-by":"crossref","unstructured":"Strom TM, Francis F, Lorenz B. Pex gene deletions in Gy and Hyp mice provide mouse models for X-linked hypophosphatemia. Hum Mol Genet. 1997; 6(2):165-171.","DOI":"10.1093\/hmg\/6.2.165"},{"key":"19832","doi-asserted-by":"crossref","unstructured":"Martin A, David V, Quarles LD. Regulation and function of the FGF23\/klotho endocrine pathways. Physiol Rev. 2012; 92(1):131-155.","DOI":"10.1152\/physrev.00002.2011"},{"key":"19833","doi-asserted-by":"crossref","unstructured":"Faul C, Amaral AP, Oskouei B. FGF23 induces left ventricular hypertrophy. J Clin Invest. 2011; 121(11):4393-4408.","DOI":"10.1172\/JCI46122"},{"key":"19834","doi-asserted-by":"crossref","unstructured":"Bacic D, Capuano P, Baum M. Activation of dopamine D1-like receptors induces acute internalization of the renal Na+\/phosphate cotransporter NaPi-IIa in mouse kidney and OK cells. Am J Physiol Renal Physiol. 2005; 288(4):F740-F747.","DOI":"10.1152\/ajprenal.00380.2004"},{"key":"19835","doi-asserted-by":"crossref","unstructured":"Goetz R, Nakada Y, Hu MC. Isolated C-terminal tail of FGF23 alleviates hypophosphatemia by inhibiting FGF23- FGFR-Klotho complex formation. Proc Natl Acad Sci U S A. 2010; 107(1):407-412.","DOI":"10.1073\/pnas.0902006107"},{"key":"19836","doi-asserted-by":"crossref","unstructured":"Moe OW, Tejedor A, Levi M, Seldin DW, Preisig PA, Alpern RJ. Dietary NaCl modulates Na(+)-H+ antiporter activity in renal cortical apical membrane vesicles. Am J Physiol. 1991; 260(1 Pt 2):F130-137.","DOI":"10.1152\/ajprenal.1991.260.1.F130"},{"key":"19837","doi-asserted-by":"crossref","unstructured":"Agoro R, Montagna A, Goetz R. Inhibition of fibroblast growth factor 23 (FGF23) signaling rescues renal anemia. FASEB J. 2018; 32(7):3752-3764.","DOI":"10.1096\/fj.201700667R"},{"key":"19838","doi-asserted-by":"crossref","unstructured":"Agoro R, Taleb M, Quesniaux VFJ, Mura C. Cell iron status influences macrophage polarization. PLoS One. 2018; 13(5):e0196921.","DOI":"10.1371\/journal.pone.0196921"},{"key":"19839","doi-asserted-by":"crossref","unstructured":"Barry M, Sherlock S. Measurement of liveriron concentration in needle-biopsy specimens. Lancet. 1971; 1(7690):100-103.","DOI":"10.1016\/S0140-6736(71)90838-5"},{"key":"19840","doi-asserted-by":"crossref","unstructured":"Pigeon C, Ilyin G, Courselaud B. A new mouse liver-specific gene, encoding a protein homologous to human antimicrobial peptide hepcidin, is overexpressed during iron overload. J Biol Chem. 2001; 276(11):7811-7819.","DOI":"10.1074\/jbc.M008923200"},{"key":"19841","doi-asserted-by":"crossref","unstructured":"Rishi G, Wallace DF, Subramaniam VN. Hepcidin: regulation of the master iron regulator. Biosci Rep. 2015; 35(3)Google Scholar","DOI":"10.1042\/BSR20150014"},{"key":"19842","doi-asserted-by":"crossref","unstructured":"Flo TH, Smith KD, Sato S. Lipocalin 2 mediates an innate immune response to bacterial infection by sequestrating iron. Nature. 2004; 432(7019):917-21.","DOI":"10.1038\/nature03104"},{"key":"19843","doi-asserted-by":"crossref","unstructured":"Faquin WC, Schneider TJ, Goldberg MA. Effect of inflammatory cytokines on hypoxia-induced erythropoietin production. Blood. 1992; 79(8):1987-1994.","DOI":"10.1182\/blood.V79.8.1987.1987"},{"key":"19844","doi-asserted-by":"crossref","unstructured":"Frede S, Fandrey J, Pagel H, Hellwig T, Jelkmann W. Erythropoietin gene expression is suppressed after lipopolysaccharide or interleukin-1 beta injections in rats. Am J Physiol. 1997; 273(3 Pt 2):R1067-1071.","DOI":"10.1152\/ajpregu.1997.273.3.R1067"},{"key":"19845","doi-asserted-by":"crossref","unstructured":"Vannucchi AM, Grossi A, Rafanelli D, Statello M, Cinotti S, Rossi-Ferrini P. Inhibition of erythropoietin production in vitro by human interferon gamma. Br J Haematol. 1994; 87(1):18-23.","DOI":"10.1111\/j.1365-2141.1994.tb04864.x"},{"key":"19846","doi-asserted-by":"crossref","unstructured":"Goetz R, Beenken A, Ibrahimi OA. Molecular insights into the klotho-dependent, endocrine mode of action of fibroblast growth factor 19 subfamily members. Mol Cell Biol. 2007; 27(9):3417-3428.","DOI":"10.1128\/MCB.02249-06"},{"key":"19847","doi-asserted-by":"crossref","unstructured":"Rivera S, Nemeth E, Gabayan V, Lopez MA, Farshidi D, Ganz T. Synthetic hepcidin causes rapid dose-dependent hypoferremia and is concentrated in ferroportincontaining organs. Blood. 2005; 106(6):2196-2199.","DOI":"10.1182\/blood-2005-04-1766"},{"key":"19848","doi-asserted-by":"crossref","unstructured":"Haase VH. Regulation of erythropoiesis by hypoxia-inducible factors. Blood Rev. 2013; 27(1):41-53.","DOI":"10.1016\/j.blre.2012.12.003"},{"key":"19849","doi-asserted-by":"crossref","unstructured":"Ward RJ, Crichton RR, Taylor DL, Della Corte L, Srai SK, Dexter DT. Iron and the immune system. J Neural Transm (Vienna). 2011; 118(3):315-328.","DOI":"10.1007\/s00702-010-0479-3"},{"key":"19850","doi-asserted-by":"crossref","unstructured":"Hennigar SR, McClung JP. Nutritional immunity: starving pathogens of trace minerals. Am J Lifestyle Med. 2016; 10(3):170-173.","DOI":"10.1177\/1559827616629117"},{"key":"19851","doi-asserted-by":"crossref","unstructured":"Ganz T. Hepcidin and iron regulation, 10 years later. Blood. 2011; 117(17):4425-4433.","DOI":"10.1182\/blood-2011-01-258467"},{"key":"19852","doi-asserted-by":"crossref","unstructured":"Agoro R, Mura C. Inflammation-induced up-regulation of hepcidin and down-regulation of ferroportin transcription are dependent on macrophage polarization. Blood Cells, Molecules and Diseases. 2016; 61:16-25.","DOI":"10.1016\/j.bcmd.2016.07.006"},{"key":"19853","doi-asserted-by":"crossref","unstructured":"Hanudel MR, Laster M, Salusky IB. Nonrenal- related mechanisms of FGF23 pathophysiology. Curr Osteoporos Rep. 2018; 16(6):724-729.","DOI":"10.1007\/s11914-018-0492-2"},{"key":"19854","doi-asserted-by":"crossref","unstructured":"Han X, Li L, Yang J, King G, Xiao Z, Quarles LD. Counter-regulatory paracrine actions of FGF-23 and 1,25(OH)2 D in macrophages. FEBS Lett. 2016; 590(1):53-67.","DOI":"10.1002\/1873-3468.12040"},{"key":"19855","doi-asserted-by":"crossref","unstructured":"Babitt JL, Sitara D. Crosstalk between fibroblast growth factor 23, iron, erythropoietin, and inflammation in kidney disease. Curr Opin Nephrol Hypertens. 2019; 28(4):304-310.","DOI":"10.1097\/MNH.0000000000000514"},{"key":"19856","doi-asserted-by":"crossref","unstructured":"Gattineni J, Bates C, Twombley K. FGF23 decreases renal NaPi-2a and NaPi-2c expression and induces hypophosphatemia in vivo predominantly via FGF receptor 1. Am J Physiol Renal Physiol. 2009; 297(2):F282-F291.","DOI":"10.1152\/ajprenal.90742.2008"},{"key":"19857","doi-asserted-by":"crossref","unstructured":"Razzaque MS, Sitara D, Taguchi T, St-Arnaud R, Lanske B. Premature aging-like phenotype in fibroblast growth factor 23 null mice is a vitamin D-mediated process. FASEB J. 2006; 20(6):720-722.","DOI":"10.1096\/fj.05-5432fje"},{"key":"19858","doi-asserted-by":"crossref","unstructured":"Shimada T, Kakitani M, Yamazaki Y. Targeted ablation of Fgf23 demonstrates an essential physiological role of FGF23 in phosphate and vitamin D metabolism. J Clin Invest. 2004; 113(4):561-568.","DOI":"10.1172\/JCI200419081"},{"key":"19859","doi-asserted-by":"crossref","unstructured":"Leaf DE, Siew ED, Eisenga MF. Fibroblast growth factor 23 associates with death in critically ill patients. Clin J Am Soc Nephrol. 2018; 13(4):531-541.","DOI":"10.2215\/CJN.10810917"},{"key":"19860","doi-asserted-by":"crossref","unstructured":"Clinkenbeard EL, Hanudel MR, Stayrook KR. Erythropoietin stimulates murine and human fibroblast growth factor-23, revealing novel roles for bone and bone marrow. Haematologica. 2017; 102(11):e427-e430.","DOI":"10.3324\/haematol.2017.167882"},{"key":"19861","doi-asserted-by":"crossref","unstructured":"Coe LM, Madathil SV, Casu C, Lanske B, Rivella S, Sitara D. FGF-23 is a negative regulator of prenatal and postnatal erythropoiesis. J Biol Chem. 2014; 289(14):9795-9810.","DOI":"10.1074\/jbc.M113.527150"},{"key":"19862","doi-asserted-by":"crossref","unstructured":"Daryadel A, Bettoni C, Haider T. Erythropoietin stimulates fibroblast growth factor 23 (FGF23) in mice and men. Pflugers Arch. 2018; 470(10):1569-1582.","DOI":"10.1007\/s00424-018-2171-7"},{"key":"19863","doi-asserted-by":"crossref","unstructured":"Hanudel MR, Eisenga MF, Rappaport M. Effects of erythropoietin on fibroblast growth factor 23 in mice and humans. Nephrol Dial Transplant. 2019; 34(12):2057-2065.","DOI":"10.1093\/ndt\/gfy189"},{"key":"19864","doi-asserted-by":"crossref","unstructured":"Imel EA, Peacock M, Gray AK, Padgett LR, Hui SL, Econs MJ. Iron modifies plasma FGF23 differently in autosomal dominant hypophosphatemic rickets and healthy humans. J Clin Endocrinol Metab. 2011; 96(11):3541-3549.","DOI":"10.1210\/jc.2011-1239"},{"key":"19865","doi-asserted-by":"crossref","unstructured":"Nam KH, Kim H, An SY. Circulating fibroblast growth factor-23 levels are associated with an increased risk of anemia development in patients with nondialysis chronic kidney disease. Sci Rep. 2018; 8(1):7294.","DOI":"10.1038\/s41598-018-25439-z"},{"key":"19866","doi-asserted-by":"crossref","unstructured":"Singh S, Grabner A, Yanucil C. Fibroblast growth factor 23 directly targets hepatocytes to promote inflammation in chronic kidney disease. Kidney Int. 2016; 90(5):985-996.","DOI":"10.1016\/j.kint.2016.05.019"},{"key":"19867","doi-asserted-by":"crossref","unstructured":"Durlacher-Betzer K, Hassan A, Levi R, Axelrod J, Silver J, Naveh-Many T. Interleukin-6 contributes to the increase in fibroblast growth factor 23 expression in acute and chronic kidney disease. Kidney Int. 2018; 94(2):315-325.","DOI":"10.1016\/j.kint.2018.02.026"},{"key":"19868","doi-asserted-by":"crossref","unstructured":"Onal M, Carlson AH, Thostenson JD. A novel distal enhancer mediates inflammation-, PTH-, and early onset murine kidney disease-induced expression of the mouse Fgf23 gene. JBMR Plus. 2018; 2(1):32-47.","DOI":"10.1002\/jbm4.10023"},{"key":"19869","doi-asserted-by":"crossref","unstructured":"Richter B, Faul C. FGF23 actions on target tissues-with and without Klotho. Front Endocrinol (Lausanne). 2018; 9:189.","DOI":"10.3389\/fendo.2018.00189"},{"key":"19870","doi-asserted-by":"crossref","unstructured":"Krick S, Grabner A, Baumlin N. Fibroblast growth factor 23 and Klotho contribute to airway inflammation. Eur Respir J. 2018; 52(1)Google Scholar","DOI":"10.1183\/13993003.00236-2018"},{"key":"19871","doi-asserted-by":"crossref","unstructured":"Ikeda S, Yamamoto H, Masuda M. Downregulation of renal type IIa sodiumdependent phosphate cotransporter during lipopolysaccharide-induced acute inflammation. Am J Physiol Renal Physiol. 2014; 306(7):F744-F750.","DOI":"10.1152\/ajprenal.00474.2013"},{"key":"19872","doi-asserted-by":"crossref","unstructured":"Abu-Amer Y, Ross FP, Edwards J, Teitelbaum SL. Lipopolysaccharide-stimulated osteoclastogenesis is mediated by tumor necrosis factor via its P55 receptor. J Clin Invest. 1997; 100(6):1557-1565.","DOI":"10.1172\/JCI119679"},{"key":"19873","doi-asserted-by":"crossref","unstructured":"Bansal S, Friedrichs WE, Velagapudi C. Spleen contributes significantly to increased circulating levels of fibroblast growth factor 23 in response to lipopolysaccharideinduced inflammation. Nephrol Dial Transplant. 2017; 32(6):960-968.","DOI":"10.1093\/ndt\/gfw376"},{"key":"19874","doi-asserted-by":"crossref","unstructured":"Masuda Y, Ohta H, Morita Y. Expression of Fgf23 in activated dendritic cells and macrophages in response to immunological stimuli in mice. Biol Pharm Bull. 2015; 38(5):687-693.","DOI":"10.1248\/bpb.b14-00276"},{"key":"19875","doi-asserted-by":"crossref","unstructured":"Okada S, Yoshida T, Hong Z. Impairment of B lymphopoiesis in precocious aging (klotho) mice. Int Immunol. 2000; 12(6):861-871.","DOI":"10.1093\/intimm\/12.6.861"},{"key":"19876","doi-asserted-by":"crossref","unstructured":"Deschemin JC, Vaulont S. Role of hepcidin in the setting of hypoferremia during acute inflammation. PLoS One. 2013; 8(4):e61050.","DOI":"10.1371\/journal.pone.0061050"},{"key":"19877","doi-asserted-by":"crossref","unstructured":"Wang CY, Babitt JL. Hepcidin regulation in the anemia of inflammation. Curr Opin Hematol. 2016; 23(3):189-197.","DOI":"10.1097\/MOH.0000000000000236"},{"key":"19878","doi-asserted-by":"crossref","unstructured":"Srai SK, Chung B, Marks J. Erythropoietin regulates intestinal iron absorption in a rat model of chronic renal failure. Kidney Int. 2010; 78(7):660-667.","DOI":"10.1038\/ki.2010.217"},{"key":"19879","doi-asserted-by":"crossref","unstructured":"Mastrogiannaki M, Matak P, Keith B, Simon MC, Vaulont S, Peyssonnaux C. HIF-2alpha, but not HIF-1alpha, promotes iron absorption in mice. J Clin Invest. 2009; 119(5):1159-1166.","DOI":"10.1172\/JCI38499"},{"key":"19880","doi-asserted-by":"crossref","unstructured":"Taylor M, Qu A, Anderson ER. Hypoxia-inducible factor-2alpha mediates the adaptive increase of intestinal ferroportin during iron deficiency in mice. Gastroenterology. 2011; 140(7):2044-2055.","DOI":"10.1053\/j.gastro.2011.03.007"},{"key":"19881","doi-asserted-by":"crossref","unstructured":"Arezes J, Foy N, McHugh K. Erythroferrone inhibits the induction of hepcidin by BMP6. Blood. 2018; 132(14):1473-1477.","DOI":"10.1182\/blood-2018-06-857995"}],"container-title":["Haematologica"],"original-title":[],"link":[{"URL":"https:\/\/haematologica.org\/article\/download\/9694\/70703","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/haematologica.org\/article\/download\/9694\/70704","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/haematologica.org\/article\/download\/9694\/70703","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2026,11,7]],"date-time":"2026-11-07T09:56:31Z","timestamp":1794045391000},"score":1,"resource":{"primary":{"URL":"https:\/\/haematologica.org\/article\/view\/9694"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2020,3,19]]},"references-count":73,"journal-issue":{"issue":"2","published-online":{"date-parts":[[2021,2,1]]}},"URL":"https:\/\/doi.org\/10.3324\/haematol.2019.237040","relation":{},"ISSN":["1592-8721","0390-6078"],"issn-type":[{"value":"1592-8721","type":"electronic"},{"value":"0390-6078","type":"print"}],"subject":[],"published":{"date-parts":[[2020,3,19]]}}}