Transfusion et maladies du globule rouge
Our team, created in January 2015, is composed of 3 former entities: Etablissement Français du Sang (EFS), Inserm and UPEC. Our 3 entities are involved in red blood cell (RBC) disease pathophysiology and treatment, with a specific focus on sickle cell disease (SCD) and thalassemia. All 3 entities already worked with the referral center of genetic disease of RBC in the H. Mondor Hospital
The former entities are:
– The EFS team directed by Pr F. Pirenne (team leader of the Eq2), which has developed, since 2008 in the H.Mondor Hospital, research projects on transfusion risks in SCD patients and antibody mediated hemolysis in autoimmune haemolytic anemia.
– The Inserm team (ex Inserm U779) specialized in protein polymerisation, blood substitutes and rare RBC diseases. The projects of this team have historically been centred on the RBC, with much of the experimental work at the protein level. The themes include hemoglobin (Hb)-based blood substitutes, the Alpha-Hemoglobin Stabilizing Protein (AHSP), chaperone of alpha chains, and neuroglobin (Ngb).
– The UPEC team specialized in RBC genetic and physiopathology SCD.
The new projects of our group combine the expertise of all members with a specific focus on :
– mechanism of allo immunization against red blood cells
– pathophysiology of post-transfusion hemolysis in sickle cell disease
– role of dense red blood cells in the pathophysiology of sickle cell disease
– study of the free pool alpha in thalassemia and other red blood cell disease
Epidemiological, transversal and fundamental studies are developed on thesis themes.
Our team is a member of the Laboratoire d’Excellence du Globule Rouge, GR-Ex (http://www.labex-grex.com)
Publications récentes
Pirenne F and Yazdanbakhsh K. How I safely transfuse patients with sickle-cell disease and manage delayed hemolytic transfusion reactions
Blood 2018 131:2773-2781Rakotoson MG, Di Liberto G, Audureau E, Habibi A, Fauroux C, Khorgami S, Hulin A, Loric S, Noizat-Pirenne F, Galacteros F, Bartolucci P. Biological parameters predictive of percent dense red blood cell decrease under hydroxyurea.
Orphanet J Rare Dis. 2015 May 9;10(1):57.Noizat-Pirenne F, Habibi A, Mekontso-Dessap A, Razazi K, Chadebech P, Mahevas M, Vingert B, Bierling P, Galactéros F, Bartolucci P, Michel M. The use of rituximab to prevent severe delayed haemolytic transfusion reaction in immunized patients with sickle cell disease.
Vox Sang. 2015 Apr;108(3):262-7.Vingert B, Tamagne M, Habibi A, Pakdaman S, Ripa J, Elayeb R, Galacteros F, Bierling P, Ansart-Pirenne H, Bartolucci P, Noizat-Pirenne F. Phenotypic differences of CD4+ T cells in response to red blood cell immunization in transfused sickle cell disease patients.
Eur J Immunol. 2015 Jun;45(6):1868-1879.Burin des Roziers N, Chadebech P, Bodivit G, Guinchard E, Bruneel A, Dupré T, Chevret L, Jugie M, Gallon P, Bierling P, Noizat-Pirenne F. Red blood cell Thomsen-Friedenreich antigen expression and galectin-3 plasma concentrations in Streptococcus pneumoniae-associated hemolytic uremic syndrome and hemolytic anemia.
Transfusion. 2014 Dec 30. doi: 10.1111/trf.12981.Domingues-Hamdi E, Vasseur C, Fournier JB, Marden MC, Wajcman H, Baudin-Creuza V. Role of α-globin H helix in the building of tetrameric human hemoglobin: interaction with α-hemoglobin stabilizing protein (AHSP) and heme molecule.
PLoS One. 2014 Nov 4;9(11):e111395.Arlet JB, Ribeil JA, Guillem F, Negre O, Hazoume A, Marcion G, Beuzard Y, Dussiot M, Moura IC, Demarest S, de Beauchêne IC, Belaid-Choucair Z, Sevin M, Maciel TT, Auclair C, Leboulch P, Chretien S, Tchertanov L, Baudin-Creuza V, Seigneuric R, Fontenay M, Garrido C, Hermine O, Courtois G. HSP70 sequestration by free α-globin promotes ineffective erythropoiesis in β-thalassaemia.
Nature. 2014 Oct 9;514(7521):242-6.Silvy M, Tournamille C, Babinet J, Pakdaman S, Cohen S, Chiaroni J, Galactéros F, Bierling P, Bailly P, Noizat-Pirenne F. Red blood cell immunization in sickle cell disease: evidence of a large responder group and a low rate of anti-Rh linked to partial Rh phenotype.
Haematologica. 2014 Jul;99(7):e115-7.Mellerio C, Farhat WH, Calvet D, Oppenheim C, Lefaucheur JP, Bartolucci P. Cerebral reorganization of language and motor control secondary to chronic hemispheric vasculopathy in a patient with homozygous sickle-cell disease.
Am J Hematol. 2014 Jun;89(6):662-3.Vingert B, Tamagne M, Desmarets M, Pakdaman S, Elayeb R, Habibi A, Bernaudin F, Galacteros F, Bierling P, Noizat-Pirenne F, Cohen JL. Partial dysfunction of Treg activation in sickle cell disease.
Am J Hematol. 2014 Mar;89(3):261-6.
Documentation
L'équipe
Composition
- Responsable : France Pirenne
- Chercheur : Véronique Baudin-Creuza, Philippe Chadebech, Laurent Kiger, Kim-Anh Nguyen-Peyre, Christophe Tournamille, Benoit Vingert
- Enseignant-Chercheur : Pablo Bartolucci, Frédéric Galacteros, Mehdi Khellaf, Matthieu Mahevas, France Pirenne, Serge Pissard, Corinne Pondarre
- Praticien hospitalier : Anoosha Habibi, Suella Martino, Stéphane Moutereau
- Post doctorant : Deborah Neyrinck, Meghan Perkins
- Doctorant : Nassima Djouder, Aline Floc'h, Nicolas Hebert, Christian Kassasseya, Mehdi Khelfa, Lamisse Mansour-Hendili
- Ingénieur : Emmanuel Adu, Imane Azzaoui, Laura Bencheikh, Gwellaouen Bodivit, Elisa Domingues-Hamdi, Sadaf Pakdaman, Marie Tamagne, Corinne Vasseur
- Technicien : Aurélie Barrault, Alicia Jouard, Alexis Vandenberghe
- Stagiaire : Roxane Kponou-Johnson, Romain Rinck
Adresse
IMRB – Inserm U955
Transfusion et maladies du globule rouge (Equipe 2)
Unité d’Ingénierie et de Thérapie Cellulaire Ile-de-France
Etablissement Français du Sang
5, rue Gustave Eiffel
94017 Créteil Cédex
Contact
Tél. : 01 49 81 37 71
Plan d'accès
Actualités du département
L’édition de l’ARN de l’adénosine en inosine (A-I), médiée par des enzymes de la famille ADAR, contribue à la diversité transcriptomique et, dans une moindre mesure, protéomique.
En savoir +Les dyskinésies ciliaires respiratoires forment un groupe hétérogène de maladies qui se caractérisent par une altération du battement ciliaire pouvant conduire à une dégradation de l’épuration muco-ciliaire qui est la première ligne de défense de l’appareil respiratoire.
En savoir +La cause moléculaire de la drépanocytose est la polymérisation de l’hémoglobine S mutante lors de la désoxygénation qui est la cause des atteintes multiples de la maladie. La quantité de fibres à l’équilibre et la cinétique de la formation des fibres dépendent toutes deux de la concentration en hémoglobine S et de la pression partielle […]
En savoir +