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3. Endoplasmic reticulum stress controls iron metabolism through TMPRSS6 repression and hepcidin mRNA stabilization by RNA-binding protein HuR

Author

Belot, Audrey, Gourbeyre, Ophélie, Palin, Anais, Rubio, Aude, Largounez, Amélie, Besson-Fournier, Celine, Latour, Chloé, Lorgouilloux, Megane, Gallitz, Inka, Montagner, Alexandra, Polizzi, Arnaud, Régnier, Marion, Smati, Sarra, Zhang, An-Sheng, Diaz-Munoz, Manuel, Steinbicker, Andrea, Guillou, Hervé, Roth, Marie-Paule, Coppin, Hélène, Meynard, Delphine, Institut de Recherche en Santé Digestive (IRSD ), Université Toulouse III - Paul Sabatier (UT3), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Ecole Nationale Vétérinaire de Toulouse (ENVT), Institut National Polytechnique (Toulouse) (Toulouse INP), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Institut National Polytechnique (Toulouse) (Toulouse INP), Université Fédérale Toulouse Midi-Pyrénées-Institut National de la Santé et de la Recherche Médicale (INSERM)-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE), University Hospital Münster - Universitaetsklinikum Muenster [Germany] (UKM), ToxAlim (ToxAlim), Université Fédérale Toulouse Midi-Pyrénées-Ecole d'Ingénieurs de Purpan (INPT - EI Purpan), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE), Toxicologie Intégrative & Métabolisme (ToxAlim-TIM), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE)-Université Toulouse III - Paul Sabatier (UT3), Oregon Health and Science University [Portland] (OHSU), Centre de Physiopathologie Toulouse Purpan (CPTP), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Cooley's Anemia Foundation, French Foundation for Rare Diseases, German Research Foundation (DFG) : STE-1985/4-1, United States Department of Health & Human Services, National Institutes of Health (NIH) - USA : R01DK102791, ATIP-AVENIR (INSERM/CNRS) program, Plan-Cancer : C18003BS, ANR-15-CE14-0026,Hepatokind,FGF21 contrôle homéostasie glucidique via les facteurs de transcription ChREBP et PPARa(2015), ANR-17-CE14-0036,IRONASH,Rôle du fer dans la pathologie du NASH(2017), ANR-17-CE14-0031,MTREAT-2,Manipuler la Matriptase-2 pour traiter les pathologies associées à une dérégulation du métabolisme du fer(2017), ANR-11-EQPX-0003,ANINFIMIP,Equipements plateforme animalerie infectieuse de haute-sécurité de Midi Pyrénées(2011), LESUR, Hélène, FGF21 contrôle homéostasie glucidique via les facteurs de transcription ChREBP et PPARa - - Hepatokind2015 - ANR-15-CE14-0026 - AAPG2015 - VALID, Rôle du fer dans la pathologie du NASH - - IRONASH2017 - ANR-17-CE14-0036 - AAPG2017 - VALID, Manipuler la Matriptase-2 pour traiter les pathologies associées à une dérégulation du métabolisme du fer - - MTREAT-22017 - ANR-17-CE14-0031 - AAPG2017 - VALID, Equipements plateforme animalerie infectieuse de haute-sécurité de Midi Pyrénées - - ANINFIMIP2011 - ANR-11-EQPX-0003 - EQPX - VALID, and Institut Toulousain des Maladies Infectieuses et Inflammatoires (Infinity)

Subjects
MESH: Humans, MESH: Membrane Proteins / genetics, Iron, Serine Endopeptidases, Membrane Proteins, RNA-Binding Proteins, [SDV.BC]Life Sciences [q-bio]/Cellular Biology, Endoplasmic Reticulum Stress, MESH: Serine Endopeptidases / genetics, MESH: Hepcidins* / metabolism, MESH: RNA-Binding Proteins, Hepcidins, [SDV.BBM.GTP]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Genomics [q-bio.GN], MESH: RNA, Messenger / genetics, [SDV.BBM.GTP] Life Sciences [q-bio]/Biochemistry, Molecular Biology/Genomics [q-bio.GN], Humans, MESH: Endoplasmic Reticulum Stress* / genetics, MESH: Membrane Proteins / metabolism, RNA, Messenger, MESH: Hepcidins* / genetics, MESH: Iron / metabolism, Letters to the Editor, [SDV.BC] Life Sciences [q-bio]/Cellular Biology, ComputingMilieux_MISCELLANEOUS
Abstract

International audience; The liver hormone hepcidin controls the main inflows of iron into plasma by binding to and inducing the degradation or the occlusion of the iron export activity of ferroportin, the only known cellular exporter of iron. When hepcidin concentrations are high, iron is trapped in enterocytes of the duodenum, hepatocytes, and macrophages. Hepcidin production by the hepatocytes is induced by a number of stimuli, most notably iron, through the BMP-SMAD signaling pathway, and inflammatory signals, through the IL-6/ STAT3 signaling axis. In addition, hepcidin has also been reported to respond to intracellular stress, namely endoplasmic reticulum (ER) stress which is involved in a number of pathophysiological states, including the inflammatory response, nutrient disorders and viral infection. A previous study has suggested that hepcidin induction by ER stress is controlled by the BMP-SMAD pathway,5 but the exact mechanism is still uncertain

Published
2021

5. Reconstitution of intestinal stem cell niche in vitro with pharmacological inhibitors or L-WRN conditioned medium differentially regulates epithelial proliferation, differentiation and barrier function in rabbit caecum organoids

Author

Mussard, Eloïse, primary, Pouzet, Cécile, additional, Helies, Virginie, additional, Pascal, Géraldine, additional, Fourre, Sandra, additional, Cherbuy, Claire, additional, Rubio, Aude, additional, Vergnolle, Nathalie, additional, Combes, Sylvie, additional, and Beaumont, Martin, additional

Published
2020
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7. An essential role for the bmp-smad pathway in hepcidin induction during ER stress and NAFLD/NASH

Author

Belot, Audrey, Gourbeyre, Ophélie, Rubio, Aude, Besson-Fournier, Celine, Latour, Chloé, Gallitz, Inka, Montagner, Alexandra, Polizzi, Arnaud, Régnier, Marion, Steinbicker, Andrea U., Guillou, Hervé, Roth, Marie-Paule, Coppin, Hélène, Meynard, Delphine, Institut de Recherche en Santé Digestive (IRSD ), Université Toulouse III - Paul Sabatier (UT3), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Institut National de la Recherche Agronomique (INRA)-Ecole Nationale Vétérinaire de Toulouse (ENVT), Institut National Polytechnique (Toulouse) (Toulouse INP), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Institut National Polytechnique (Toulouse) (Toulouse INP), Université Fédérale Toulouse Midi-Pyrénées-Institut National de la Santé et de la Recherche Médicale (INSERM), ToxAlim (ToxAlim), Université Fédérale Toulouse Midi-Pyrénées-Ecole Nationale Vétérinaire de Toulouse (ENVT), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Ecole d'Ingénieurs de Purpan (INPT - EI Purpan), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Institut National de la Recherche Agronomique (INRA), University of Münster, Institut National de la Recherche Agronomique (INRA)-Université Toulouse III - Paul Sabatier (UT3), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Ecole Nationale Vétérinaire de Toulouse (ENVT), Toxicologie Intégrative & Métabolisme (ToxAlim-TIM), Université Fédérale Toulouse Midi-Pyrénées-Ecole d'Ingénieurs de Purpan (INPT - EI Purpan), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Institut National de la Recherche Agronomique (INRA)-Université Toulouse III - Paul Sabatier (UT3), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées, Westfälische Wilhelms-Universität Münster = University of Münster (WWU), and ProdInra, Archive Ouverte

Subjects
[SDV.MHEP.HEM] Life Sciences [q-bio]/Human health and pathology/Hematology, analyse in vivo, expression génique, gene expression, [SDV.MHEP.HEM]Life Sciences [q-bio]/Human health and pathology/Hematology, Hematology, ergastoplasm, réticulum endoplasmique, hepcidine, métabolisme du fer, Hématologie
Abstract

An essential role for the bmp-smad pathway in hepcidin induction during ER stress and NAFLD/NASH. 7. Congress of the International Biolron Society (IBIS)

Published
2017

8. Iron- and Hepcidin-Independent Downregulation of the Iron Exporter Ferroportin in Macrophages during Salmonella Infection

Author

Willemetz, Alexandra, Beatty, Sean, Richer, Etienne, Rubio, Aude, Auriac, Anne, Milkereit, Ruth J., Thibaudeau, Olivier, Vaulont, Sophie, Malo, Danielle, Canonne-Hergaux, François, Institut de Chimie des Substances Naturelles (ICSN), Centre National de la Recherche Scientifique (CNRS)-Institut de Chimie du CNRS (INC), McGill University = Université McGill [Montréal, Canada], Institut de Recherche en Santé Digestive (IRSD ), Université Toulouse III - Paul Sabatier (UT3), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Institut National de la Recherche Agronomique (INRA)-Ecole Nationale Vétérinaire de Toulouse (ENVT), Institut National Polytechnique (Toulouse) (Toulouse INP), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Institut National Polytechnique (Toulouse) (Toulouse INP), Université Fédérale Toulouse Midi-Pyrénées-Institut National de la Santé et de la Recherche Médicale (INSERM), AP-HP - Hôpital Bichat - Claude Bernard [Paris], Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP), Institut Cochin (IC UM3 (UMR 8104 / U1016)), Université Paris Descartes - Paris 5 (UPD5)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Canadian Institutes of Health Research (MOP-15461), INSERM, 'Agence Nationale de la Recherche,' France (ANR-10-MIDI-004), and ANR-10-MIDI-0004,INFLAFER,Mécanismes de l'anémie inflammatoire : interférences entre inflammation et métabolisme du fer(2010)

Subjects
expression des protéines, Endocrinology and metabolism, anemia of inflammation, Immunology, homéostasie du fer, the iron regulatory hormone hepcidin, the iron exporter ferroportin, macrophage, [SDV.MHEP.EM]Life Sciences [q-bio]/Human health and pathology/Endocrinology and metabolism, macrophage iron recycling, Salmonella infection, Endocrinologie et métabolisme, Immunology and Allergy, iron homeostasis, hepcidine, salmonella enterica, Original Research
Abstract

International audience; Retention of iron in tissue macrophages via upregulation of hepcidin (HAMP) and downregulation of the iron exporter ferroportin (FPN) is thought to participate in the establishment of anemia of inflammation after infection. However, an upregulation of FPN has been proposed to limit macrophages iron access to intracellular pathogens. Therefore, we studied the iron homeostasis and in particular the regulation of FPN after infection with Salmonella enterica serovar Typhimurium in mice presenting tissue macrophages with high iron (AcB61), basal iron (A/J and wild-type mice), or low iron (Hamp knock out, Hamp(-/-)) levels. The presence of iron in AcB61 macrophages due to extravascular hemolysis and strong erythrophagocytosis activity favored the proliferation of Salmonella in the spleen and liver with a concomitant decrease of FPN protein expression. Despite systemic iron overload, no or slight increase in Salmonella burden was observed in Hamp(-/-) mice compared to controls. Importantly, FPN expression at both mRNA and protein levels was strongly decreased during Salmonella infection in Hamp(-/-) mice. The repression of Fpn mRNA was also observed in Salmonella-infected cultured macrophages. In addition, the downregulation of FPN was associated with decreased iron stores in both the liver and spleen in infected mice. Our findings show that during Salmonella infection, FPN is repressed through an iron and hepcidin-independent mechanism. Such regulation likely provides the cellular iron indispensable for the growth of Salmonella inside the macrophages.

Published
2017

9. Iron- and Hepcidin-lndependent Downregulation of the Iron Exporter Ferroportin in Macrophages during Salmonella Infection.

Author

Willemetz, Alexandra, Beatty, Sean, Richer, Etienne, Rubio, Aude, Auriac, Anne, Milkereit, Ruth J., Thibaudeau, Olivier, Vaulont, Sophie, Malo, Danielle, and Canonne-Hergaux, François

Subjects
PHYSIOLOGICAL effects of iron, MACROPHAGES, SALMONELLA diseases
Abstract

Retention of iron in tissue macrophages via upregulation of hepcidin (HAMP) and downregulation of the iron exporter ferroportin (FPN) is thought to participate in the establishment of anemia of inflammation after infection. However, an upregulation of FPN has been proposed to limit macrophages iron access to intracellular pathogens. Therefore, we studied the iron homeostasis and in particular the regulation of FPN after infection with Salmonella enterica serovar Typhimurium in mice presenting tissue macrophages with high iron (AcB61), basal iron (A/J and wild-type mice), or low iron (Hamp knock out, Hamp-/-) levels. The presence of iron in AcB61 macrophages due to extravascular hemolysis and strong erythrophagocytosis activity favored the proliferation of Salmonella in the spleen and liver with a concomitant decrease of FPN protein expression. Despite systemic iron overload, no or slight increase in Salmonella burden was observed in Hamp-/- mice compared to controls. Importantly, FPN expression at both mRNA and protein levels was strongly decreased during Salmonella infection in Hamp-/- mice. The repression of Fpn mRNA was also observed in Salmonella-infected cultured macrophages. In addition, the downregulation of FPN was associated with decreased iron stores in both the liver and spleen in infected mice. Our findings show that during Salmonella infection, FPN is repressed through an iron and hepcidin-independent mechanism. Such regulation likely provides the cellular iron indispensable for the growth of Salmonella inside the macrophages. [ABSTRACT FROM AUTHOR]

Published
2017
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11. Endoplasmic reticulum stress controls iron metabolism through TMPRSS6 repression and hepcidin mRNA stabilization by RNA-binding protein HuR.

Author

Belot A, Gourbeyre O, Palin A, Rubio A, Largounez A, Besson-Fournier C, Latour C, Lorgouilloux M, Gallitz I, Montagner A, Polizzi A, Régnier M, Smati S, Zhang AS, Diaz-Munoz MD, Steinbicker AU, Guillou H, Roth MP, Coppin H, and Meynard D

Subjects
Humans, Iron metabolism, Membrane Proteins genetics, Membrane Proteins metabolism, RNA, Messenger genetics, RNA-Binding Proteins, Serine Endopeptidases genetics, Endoplasmic Reticulum Stress genetics, Hepcidins genetics, Hepcidins metabolism
Published
2021
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12. Iron- and Hepcidin-Independent Downregulation of the Iron Exporter Ferroportin in Macrophages during Salmonella Infection.

Author

Willemetz A, Beatty S, Richer E, Rubio A, Auriac A, Milkereit RJ, Thibaudeau O, Vaulont S, Malo D, and Canonne-Hergaux F

Abstract

Retention of iron in tissue macrophages via upregulation of hepcidin (HAMP) and downregulation of the iron exporter ferroportin (FPN) is thought to participate in the establishment of anemia of inflammation after infection. However, an upregulation of FPN has been proposed to limit macrophages iron access to intracellular pathogens. Therefore, we studied the iron homeostasis and in particular the regulation of FPN after infection with Salmonella enterica serovar Typhimurium in mice presenting tissue macrophages with high iron (AcB61), basal iron (A/J and wild-type mice), or low iron ( Hamp knock out, Hamp -/- ) levels. The presence of iron in AcB61 macrophages due to extravascular hemolysis and strong erythrophagocytosis activity favored the proliferation of Salmonella in the spleen and liver with a concomitant decrease of FPN protein expression. Despite systemic iron overload, no or slight increase in Salmonella burden was observed in Hamp -/- mice compared to controls. Importantly, FPN expression at both mRNA and protein levels was strongly decreased during Salmonella infection in Hamp -/- mice. The repression of Fpn mRNA was also observed in Salmonella -infected cultured macrophages. In addition, the downregulation of FPN was associated with decreased iron stores in both the liver and spleen in infected mice. Our findings show that during Salmonella infection, FPN is repressed through an iron and hepcidin-independent mechanism. Such regulation likely provides the cellular iron indispensable for the growth of Salmonella inside the macrophages.

Published
2017
Full Text
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