Tmprss6, An Inhibitor of Hepatic Bmp/Smad Signaling, Is Required for Hepcidin Suppression and Iron Loading In a Mouse Model of β-Thalassemia

Blood ◽  
2010 ◽  
Vol 116 (21) ◽  
pp. 164-164
Author(s):  
Karin E. Finberg ◽  
Rebecca L. Whittlesey ◽  
Stefano Rivella ◽  
Nancy C. Andrews

Abstract Abstract 164 TMPRSS6, a transmembrane protease produced by the liver, is an essential regulator of mammalian iron homeostasis. TMPRSS6 inhibits the expression of hepcidin, a circulating peptide that decreases intestinal iron absorption and macrophage iron release, by down-regulating hepatic BMP/SMAD signaling for hepcidin production. Accordingly, TMPRSS6 mutations result in elevated hepcidin levels, impaired absorption of dietary iron, and systemic iron deficiency. Interestingly, in congenital iron loading anemias such as β-thalassemia, hepcidin levels are inappropriately low relative to body iron stores, a finding that has been postulated to result from the production of a hepcidin-repressing factor in the setting of ineffective erythropoiesis. Here we asked if Tmprss6 is required to achieve the hepcidin suppression present in Hbbth3/+ mice, a model of β-thalassemia intermedia. To test this, we bred Hbbth3/+ mice to mice harboring a targeted disruption of the Tmprss6 serine protease domain. We generated mice of various Hbb-Tmprss6 genotype combinations and compared parameters of systemic iron homeostasis at 8 weeks of age. Consistent with prior studies of Hbbth3/+ mice, Hbbth3/+ mice harboring 2 wild-type Tmprss6 alleles (Hbbth3/+Tmprss6+/+ mice) showed non-heme iron concentrations of liver, spleen, and kidney that were significantly elevated compared to wild-type controls. Homozygosity for Tmprss6 mutation, however, ameliorated the iron overload phenotype of Hbbth3/+ mice and led to systemic iron deficiency. Tissue non-heme iron concentrations were markedly reduced in Hbbth3/+Tmprss6−/− mice as compared to Hbbth3/+Tmprss6+/+ mice and were similar to levels observed in Tmprss6−/− mice harboring 2 wild-type Hbb alleles. Hbbth3/+Tmprss6−/− mice had hemoglobin levels similar to the thalassemic levels present in Hbbth3/+Tmprss6+/+ mice. However, compared to Hbbth3/+Tmprss6+/+ mice, Hbbth3/+Tmprss6−/− mice showed markedly reduced erythrocyte mean corpuscular volume and serum transferrin saturation, as well as increased red blood cell count. Interestingly, homozygous loss of Tmprss6 in Hbbth3/+ mice also led to marked reduction in splenomegaly and improvement in peripheral red blood cell morphology. Consistent with prior studies of Hbbth3/+ mice, Hbbth3/+Tmprss6+/+ mice displayed hepatic hepcidin mRNA levels that were similar to wild-type and were, therefore, inappropriately decreased relative to their increased hepatic iron stores. Hepatic mRNA levels of Bmp6, encoding a Bmp ligand that is transcriptionally regulated by iron and acts as a key regulator of hepcidin expression in vivo, were significantly elevated in Hbbth3/+Tmprss6+/+ mice, suggesting that their relative hepcidin deficiency does not result from impaired Bmp6 transcription. While Hbbth3/+Tmprss6+/+ mice showed suppressed hepcidin levels, homozygous loss of Tmprss6 alleviated their hepcidin suppression and led to elevated hepcidin mRNA levels similar to Tmprss6−/− mice harboring 2 wild-type Hbb alleles. Hbbth3/+Tmprss6−/− mice also showed elevated hepatic mRNA encoding Id1, another transcriptional target of Bmp/Smad signaling. These findings indicate that Tmprss6 is required to achieve the suppression of hepatic hepcidin expression that underlies systemic iron overload in Hbbth3/+ mice. Furthermore, our results demonstrate that, by up-regulating hepatic Bmp/Smad signaling for hepcidin production, genetic loss of Tmprss6 induces profound changes in systemic iron homeostasis in this thalassemia model. Disclosures: No relevant conflicts of interest to declare.

Blood ◽  
2010 ◽  
Vol 116 (21) ◽  
pp. 4258-4258
Author(s):  
Ramsey M. Wehbe ◽  
Rebecca L. Whittlesey ◽  
Nancy C. Andrews ◽  
Karin E. Finberg

Abstract Abstract 4258 Mutations in TMPRSS6 (matriptase-2), a transmembrane serine protease expressed by the liver, result in the clinical phenotype of iron refractory iron deficiency anemia (IRIDA). Additionally, common polymorphisms in TMPRSS6 have been associated with variation in laboratory parameters of iron homeostasis in healthy populations. TMPRSS6 increases iron absorption by reducing expression of the hepatic hormone, hepcidin, via down-regulation of a BMP/SMAD signaling cascade. Hepcidin promotes the internalization and degradation of the duodenal iron transporter, ferroportin, thereby inhibiting iron absorption. Previous studies have demonstrated that adult mice with Tmprss6 deficiency exhibit elevated hepatic hepcidin mRNA levels that are associated with decreased hepatic iron stores. In one study, genetic loss of Tmprss6 was shown to result in significant elevation of hepatic hepcidin expression in mice at birth; however, whether this hepcidin elevation was associated with abnormalities in iron homeostasis was not reported. We therefore asked if the elevated hepcidin levels present in newborn Tmprss6-/- pups correlate with abnormal parameters of iron homeostasis in the fetal or neonatal periods. To answer this question, we intercrossed Tmprss6+/− mice to generate Tmprss6+/+, Tmprss6+/−, and Tmprss6-/- progeny for phenotypic characterization at either gestational day 17.5 (E17.5) or postnatal day 0 (P0). Consistent with prior observations, Tmprss6-/- pups at P0 showed a 4.6-fold increase in hepatic hepcidin mRNA compared to Tmprss6+/+ littermates (p=.006). However, despite this elevation in hepcidin expression, Tmprss6-/- pups were not pale, and they showed no significant differences in body mass or hepatic non-heme iron concentration compared to Tmprss6+/+ and Tmprss6+/− littermates. At E17.5, Tmprss6-/- fetuses showed a 50-fold increase in hepatic hepcidin mRNA compared to Tmprss6+/+ littermates (p=.005). However, Tmprss6-/- fetuses also were not pale, and they showed no significant difference in body mass compared to Tmprss6+/+ and Tmprss6+/− littermates. Surprisingly, hepatic non-heme iron concentration at E17.5 was significantly higher in Tmprss6-/- fetuses than in Tmprss6+/+ fetuses (p=.003). To determine if the increased hepcidin expression of Tmprss6-/- fetuses might affect iron homeostasis in their pregnant mothers, we measured iron parameters in Tmprss6+/− females gestating E17.5 litters that were enriched for either Tmprss6+/+ or Tmprss6-/- fetuses. No significant effects of fetal genotype on maternal iron parameters were observed. In summary, our results demonstrate that Tmprss6 regulates hepcidin expression in the fetal and neonatal periods in mice. However, Tmprss6 deficiency does not appear to be associated with systemic iron deficiency at these stages of development, and fetal Tmprss6 expression does not have a significant effect on maternal iron homeostasis in late gestation. These results may have implications for understanding the maintenance of iron homeostasis in early development, and may provide insight into the evolution of IRIDA as well as other disorders of iron homeostasis. Disclosures: No relevant conflicts of interest to declare.


Blood ◽  
2009 ◽  
Vol 114 (12) ◽  
pp. 2515-2520 ◽  
Author(s):  
Léon Kautz ◽  
Delphine Meynard ◽  
Céline Besson-Fournier ◽  
Valérie Darnaud ◽  
Talal Al Saati ◽  
...  

Abstract Impaired regulation of hepcidin expression in response to iron loading appears to be the pathogenic mechanism for hereditary hemochromatosis. Iron normally induces expression of the BMP6 ligand, which, in turn, activates the BMP/Smad signaling cascade directing hepcidin expression. The molecular function of the HFE protein, involved in the most common form of hereditary hemochromatosis, is still unknown. We have used Hfe-deficient mice of different genetic backgrounds to test whether HFE has a role in the signaling cascade induced by BMP6. At 7 weeks of age, these mice have accumulated iron in their liver and have increased Bmp6 mRNA and protein. However, in contrast to mice with secondary iron overload, levels of phosphorylated Smads 1/5/8 and of Id1 mRNA, both indicators of BMP signaling, are not significantly higher in the liver of these mice than in wild-type livers. As a consequence, hepcidin mRNA levels in Hfe-deficient mice are similar or marginally reduced, compared with 7-week-old wild-type mice. The inappropriately low levels of Id1 and hepcidin mRNA observed at weaning further suggest that Hfe deficiency triggers iron overload by impairing hepatic Bmp/Smad signaling. HFE therefore appears to facilitate signal transduction induced by the BMP6 ligand.


Blood ◽  
2010 ◽  
Vol 115 (18) ◽  
pp. 3817-3826 ◽  
Author(s):  
Karin E. Finberg ◽  
Rebecca L. Whittlesey ◽  
Mark D. Fleming ◽  
Nancy C. Andrews

Abstract Iron-refractory, iron-deficiency anemia (IRIDA) is a familial disorder characterized by iron deficiency anemia unresponsive to oral iron treatment but partially responsive to intravenous iron therapy. Previously, we showed that IRIDA patients harbor loss-of-function mutations in TMPRSS6, a type II transmembrane serine protease primarily expressed by the liver. Both humans and mice with TMPRSS6 mutations show inappropriately elevated levels of the iron-regulatory hormone hepcidin, suggesting that TMPRSS6 acts to negatively regulate hepcidin expression. Here we investigate the relationship between Tmprss6 and the bone morphogenetic protein (BMP)–Smad signaling pathway, a key pathway promoting hepcidin transcription in hepatocytes. We show that livers from mice deficient for Tmprss6 have decreased iron stores and decreased Bmp6 mRNA, but markedly increased mRNA for Id1, a target gene of Bmp6 signaling. In contrast, mice deficient for both Tmprss6 and hemojuvelin (Hjv), a BMP coreceptor that augments hepcidin expression in hepatocytes, showed markedly decreased hepatic levels of hepcidin and Id1 mRNA, markedly increased hepatic Bmp6 mRNA levels, and systemic iron overload similar to mice deficient for Hjv alone. These findings suggest that down-regulation of Bmp/Smad signaling by Tmprss6 is required for regulation of hepcidin expression and maintenance of systemic iron homeostasis.


Blood ◽  
2012 ◽  
Vol 120 (16) ◽  
pp. 3336-3344 ◽  
Author(s):  
Anu Laitala ◽  
Ellinoora Aro ◽  
Gail Walkinshaw ◽  
Joni M. Mäki ◽  
Maarit Rossi ◽  
...  

AbstractAn endoplasmic reticulum transmembrane prolyl 4-hydroxylase (P4H-TM) is able to hydroxylate the α subunit of the hypoxia-inducible factor (HIF) in vitro and in cultured cells, but nothing is known about its roles in mammalian erythropoiesis. We studied such roles here by administering a HIF-P4H inhibitor, FG-4497, to P4h-tm−/− mice. This caused larger increases in serum Epo concentration and kidney but not liver Hif-1α and Hif-2α protein and Epo mRNA levels than in wild-type mice, while the liver Hepcidin mRNA level was lower in the P4h-tm−/− mice than in the wild-type. Similar, but not identical, differences were also seen between FG-4497–treated Hif-p4h-2 hypomorphic (Hif-p4h-2gt/gt) and Hif-p4h-3−/− mice versus wild-type mice. FG-4497 administration increased hemoglobin and hematocrit values similarly in the P4h-tm−/− and wild-type mice, but caused higher increases in both values in the Hif-p4h-2gt/gt mice and in hematocrit value in the Hif-p4h-3−/− mice than in the wild-type. Hif-p4h-2gt/gt/P4h-tm−/− double gene-modified mice nevertheless had increased hemoglobin and hematocrit values without any FG-4497 administration, although no such abnormalities were seen in the Hif-p4h-2gt/gt or P4h-tm−/− mice. Our data thus indicate that P4H-TM plays a role in the regulation of EPO production, hepcidin expression, and erythropoiesis.


Blood ◽  
2005 ◽  
Vol 106 (11) ◽  
pp. 512-512
Author(s):  
Lan Lin ◽  
Y. Paul Goldberg ◽  
Tomas Ganz

Abstract Human genetic studies identified HJV (also called HFE2) as the major cause for juvenile hemochromatosis (JH). Patients with HJV hemochromatosis have low urinary levels of hepcidin, the principal iron-regulatory hormone secreted by the liver. We attempted to establish the specific roles of HJV in iron metabolism, especially its relationship with hepcidin. Translation of the genomic sequence indicated a C-terminal GPI anchor for the protein product of HJV, hemojuvelin. This suggested that hemojuvelin may have either a soluble or a cell-associated form. In human hepatoma cell line Hep3B, knockdown of cellular HJV by siRNA decreased hepcidin expression, independently of the IL-6 pathway. Intriguingly, the addition of recombinant soluble hemojuvelin (rs-hemojuvelin) also suppressed hepcidin expression in primary human hepatocytes, in a log-linear dose-dependent manner, suggesting competition between soluble and cell-associated forms of hemojuvelin. Soluble hemojuvelin was found in human sera at concentrations similar to those required to suppress hepcidin mRNA in vitro. In cells engineered to express hemojuvelin, soluble hemojuvelin release was progressively inhibited by increasing iron or holotransferrin concentrations. Our study suggests that soluble and cell-associated hemojuvelin reciprocally regulate hepcidin mRNA levels, and that hemojuvelin may serve as a molecular messenger for iron homeostasis. Even in hepatocytes stimulated with IL-6, we observed strong suppression of hepcidin mRNA by rs-hemojuvelin. If rs-hemojuvelin or its active fragments also suppress hepcidin production in vivo, they could be used to alleviate anemia of inflammation.


Blood ◽  
2007 ◽  
Vol 110 (11) ◽  
pp. 2658-2658
Author(s):  
Sioban B. Keel ◽  
Raymond T. Doty ◽  
Sue Knoblaugh ◽  
Ivana De Domenico ◽  
Jerry Kaplan ◽  
...  

Abstract Heme is required by all aerobic cells, yet toxic, so its intracellular concentration must be tightly regulated. We previously determined that the Feline Leukemia Virus, subgroup C, cell surface Receptor (FLVCR), is a heme export protein (Cell; 118:6, 2004), and characterized the erythropoietic phenotype of inducible FLVCR null mice (Flvcrflox/flox;Mx-cre, ASH abstract 2006). Deleted mice develop a severe hyperchromic macrocytic anemia (HGB 3.8±0.2 g/dl, MCV 65.5±2.1 fL, MCH 22.7±0.6 pg vs. HGB 15.4±0.6, MCV 50.8±1.5, MCH 15.9±0.5). Morphologic, flow cytometric, and erythroid colony analyses of spleen and bone marrow cells showed a block in erythroid differentiation at the CFU-E/proerythroblast stage, a phenotype identical to that observed in cats with pure red cell aplasia (PRCA) due to retroviral inhibition of FLVCR. Mice transplanted with Flvcrflox/flox;Mx-cre marrow, and then treated with p(I)p(C) to delete Flvcr in hematopoietic cells, also developed PRCA. These studies show that FLVCR is required by CFU-E/proerythroblasts, likely to export excess heme and to ensure cell survival, and show that PRCA results from a lack of FLVCR in hematopoietic, and not microenvironmental cells. By western blot, FLVCR is highly expressed in tissues with high heme flux, like the placenta, uterus, duodenum, liver, and cultured macrophages, which suggests that it also has a role in heme-iron trafficking or in the prevention of heme toxicity in nonerythroid cells. To define its macrophage function, we exposed marrow-derived macrophages from deleted and control mice to ferric ammonium citrate (FAC) or IgG-coated red blood cells ± hepcidin and measured ferritin accumulation. Deleted and control macrophages exposed to FAC showed equivalent increases in ferritin which as predicted, increased further with hepcidin treatment. However, after exposure to opsonized red blood cells, deleted macrophages accumulated significantly more ferritin than controls (122.3±0.8 ng/mh protein vs. 67.3±1.3), which increased further with hepcidin treatment. Therefore, not all heme in macrophages is degraded to iron, but rather some traverses the cell intact via FLVCR. We next evaluated the role of FLVCR in iron homeostasis by examining all tissues in deleted mice. Within 5 weeks, deleted mice developed pronounced iron loading in hepatocytes and subsequently within duodenal enterocytes and splenic macrophages. By 7 months, there was swelling of hepatocytes lining bile canaliculi and bile stasis. In contrast, mice in which Flvcr was deleted only in hematopoietic cells showed no iron overload after 5–6 weeks. Liver hepcidin expression by quantitative RT-PCR was significantly increased in both deleted mice and in mice lacking FLVCR only in their hematopoietic cells. These data demonstrate that hepcidin expression alone does not account for the iron overload, and suggest that FLVCR exports heme from liver into bile, thus providing a mechanism for iron to exit the body. Since high hepcidin levels are in contrast to other iron loading anemias with ineffective erythropoiesis, the “erythropoietic regulator” of liver hepcidin expression must require cells more differentiated than proerythroblasts. Together, our work establishes that FLVCR is required for terminal red blood cell development and argues that systemic iron balance involves heme-iron trafficking via FLVCR, in addition to the well-described elemental iron pathways.


Blood ◽  
2005 ◽  
Vol 105 (1) ◽  
pp. 376-381 ◽  
Author(s):  
Hiroshi Kawabata ◽  
Robert E. Fleming ◽  
Dorina Gui ◽  
Seo Y. Moon ◽  
Takayuki Saitoh ◽  
...  

Abstract Transferrin receptor 2 (TfR2) is a membrane glycoprotein that mediates cellular iron uptake from holotransferrin. Homozygous mutations of this gene cause one form of hereditary hemochromatosis in humans. We recently reported that homozygous TfR2(Y245X) mutant mice, which correspond to the TfR2(Y250X) mutation in humans, showed a phenotype similar to hereditary hemochromatosis. In this study, we further analyzed the phenotype as well as iron-related gene expression in these mice by comparing the TfR2-mutant and wild-type siblings. Northern blot analyses showed that the levels of expression of hepcidin mRNA in the liver were generally lower, whereas those of duodenal DMT1, the main transporter for uptake of dietary iron, were higher in the TfR2-mutant mice as compared to the wild-type siblings. Expression of hepcidin mRNA in the TfR2 mutant mice remained low even after intraperitoneal iron loading. In isolated hepatocytes from both wild-type and TfR2 mutant mice, interleukin-6 and lipopolysaccharide each induced expression of hepcidin mRNA. These results suggest that up-regulation of hepcidin expression by inflammatory stimuli is independent of TfR2 and that TfR2 is upstream of hepcidin in the regulatory pathway of body iron homeostasis. (Blood. 2005;105:376-381)


Blood ◽  
2009 ◽  
Vol 114 (22) ◽  
pp. 625-625
Author(s):  
Karin E. Finberg ◽  
Rebecca Whittlesey ◽  
Mark D. Fleming ◽  
Nancy C. Andrews

Abstract Abstract 625 HFE-associated hereditary hemochromatosis is an autosomal recessive disorder characterized by inappropriately elevated absorption of dietary iron by the gastrointestinal mucosa, resulting in excessive storage of iron in multiple organs. A significant proportion of individuals who are homozygous for HFE mutations fail to develop clinical symptoms, suggesting that environmental and/or genetic factors may influence the penetrance of this disorder. In vitro and animal studies have revealed that HFE promotes the expression of hepcidin, a circulating hormone produced by the liver that acts to inhibit iron absorption by the duodenum. In contrast, TMPRSS6, a transmembrane serine protease produced by the liver, acts to inhibit hepcidin expression; both humans and mice harboring TMPRSS6 mutations display impaired intestinal iron absorption, resulting in a phenotype of iron-refractory iron deficiency anemia (IRIDA). Here we asked if heterozygous or homozygous loss of Tmprss6 function could modify the iron overload phenotype of Hfe null (Hfe-/-) mice, a mouse model of human HFE-hemochromatosis. To test this, we bred Hfe-/- mice to Tmprss6-/- mice; the latter harbor a targeted disruption of the Tmprss6 serine protease domain and exhibit an IRIDA phenotype. We generated Hfe-/-Tmprss6+/+, Hfe-/-Tmprss6+/-, and Hfe-/-Tmprss6-/- female mice (6-10 mice per genotype), in which parameters of systemic iron homeostasis were compared at eight weeks of age by Student's t test. Consistent with previous study of Hfe-/- mice, Hfe-/- mice harboring two wild type Tmprss6 alleles (Hfe-/-Tmprss6+/+ mice) showed serum iron concentration, transferrin saturation, and hepatic non-heme iron content that were significantly elevated compared to wild type mice of similar genetic background. Heterozygosity for Tmprss6 mutation, however, markedly reduced the severity of the hemochromatosis phenotype of Hfe-/- mice. Compared to Hfe-/- mice with two wild type Tmprss6 alleles, Hfe-/- mice that were heterozygous for Tmprss6 mutation (Hfe-/-Tmprss6+/- mice) showed significant reductions in serum iron concentration (p<0.01), transferrin saturation (p<0.005), and non-heme iron content of liver (p<10-4). Furthermore, homozygosity for Tmprss6 mutation completely ameliorated the iron overload phenotype of Hfe-/- mice and in fact led to systemic iron deficiency. Compared to both Hfe-/-Tmprss6+/+ and Hfe-/-Tmprss6+/- mice, Hfe-/-Tmprss6-/- mice showed markedly reduced serum iron concentration (p<10-7), transferrin saturation (p<10-10), and non-heme iron content of liver (p<10-4). Hfe-/-Tmprss6-/- mice also displayed iron deficiency anemia and appeared phenotypically similar to previously characterized Tmprss6-/- mice harboring two wild type copies of Hfe. In summary, these results demonstrate that Tmprss6 is a genetic modifier of the Hfe-hemochromatosis phenotype in mice. These findings suggest that natural genetic variation in the human ortholog TMPRSS6 might modify the clinical penetrance of HFE-hemochromatosis and raise the possibility that pharmacological inhibition of TMPRSS6 activity might prove an effective therapy in this disorder. Disclosures: No relevant conflicts of interest to declare.


Blood ◽  
2012 ◽  
Vol 119 (3) ◽  
pp. 857-860 ◽  
Author(s):  
Nick P. Talbot ◽  
Samira Lakhal ◽  
Thomas G. Smith ◽  
Catherine Privat ◽  
Annabel H. Nickol ◽  
...  

Abstract Enhanced erythropoietic drive and iron deficiency both influence iron homeostasis through the suppression of the iron regulatory hormone hepcidin. Hypoxia also suppresses hepcidin through a mechanism that is unknown. We measured iron indices and plasma hepcidin levels in healthy volunteers during a 7-day sojourn to high altitude (4340 m above sea level), with and without prior intravenous iron loading. Without prior iron loading, a rapid reduction in plasma hepcidin was observed that was almost complete by the second day at altitude. This occurred before any index of iron availability had changed. Prior iron loading delayed the decrease in hepcidin until after the transferrin saturation, but not the ferritin concentration, had normalized. We conclude that hepcidin suppression by the hypoxia of high altitude is not driven by a reduction in iron stores.


PeerJ ◽  
2021 ◽  
Vol 9 ◽  
pp. e11367
Author(s):  
Chanita Sanyear ◽  
Buraporn Chiawtada ◽  
Punnee Butthep ◽  
Saovaros Svasti ◽  
Suthat Fucharoen ◽  
...  

Background Hepcidin controls iron homeostasis by inducing the degradation of the iron efflux protein, ferroportin (FPN1), and subsequently reducing serum iron levels. Hepcidin expression is influenced by multiple factors, including iron stores, ineffective erythropoiesis, and inflammation. However, the interactions between these factors under thalassemic condition remain unclear. This study aimed to determine the hypoferremic and transcriptional responses of iron homeostasis to acute inflammatory induction by lipopolysaccharide (LPS) in thalassemic (Hbbth3/+) mice with/without parenteral iron loading with iron dextran. Methods Wild type and Hbbth3/+ mice were intramuscularly injected with 5 mg of iron dextran once daily for two consecutive days. After a 2-week equilibration, acute inflammation was induced by an intraperitoneal injection of a single dose of 1 µg/g body weight of LPS. Control groups for both iron loading and acute inflammation received equal volume(s) of saline solution. Blood and tissue samples were collected at 6 hours after LPS (or saline) injection. Iron parameters and mRNA expression of hepcidin as well as genes involved in iron transport and metabolism in wild type and Hbbth3/+ mice were analyzed and compared by Kruskal–Wallis test with pairwise Mann–Whitney U test. Results We found the inductive effects of LPS on liver IL-6 mRNA expression to be more pronounced under parenteral iron loading. Upon LPS administration, splenic erythroferrone (ERFE) mRNA levels were reduced only in iron-treated mice, whereas, liver bone morphogenetic protein 6 (BMP6) mRNA levels were decreased under both control and parenteral iron loading conditions. Despite the altered expression of the aforementioned hepcidin regulators, the stimulatory effect of LPS on hepcidin mRNA expression was blunt in iron-treated Hbbth3/+ mice. Contrary to the blunted hepcidin response, LPS treatment suppressed FPN1 mRNA expression in the liver, spleen, and duodenum, as well as reduced serum iron levels of Hbbth3/+ mice with parenteral iron loading. Conclusion Our study suggests that a hypoferremic response to LPS-induced acute inflammation is maintained in thalassemic mice with parenteral iron loading in a hepcidin-independent manner.


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