67 research outputs found
Electrical Detection of the Mechanical Alteration of Sickling Red Blood Cells within a Microfluidic Capillary Network
International audienceIn this paper we demonstrate the capability to detect red blood cells mechanical disorders, in particular the sickle cell disease, using the electrical signature of the cell transit within a microfluidic restriction mimicking the blood capillaries
ABCG2 Is Overexpressed on Red Blood Cells in Ph-Negative Myeloproliferative Neoplasms and Potentiates Ruxolitinib-Induced Apoptosis
Acknowledgments: The authors would like to thank Dominique Gien, Sirandou Tounkara, and Eliane VĂ©ra at Centre National de RĂ©fĂ©rence pour les Groupes Sanguins for the management of blood samples. Funding: The work was supported by Institut National de la SantĂ© et de la Recherche MĂ©dicale (Inserm), Institut National de la Transfusion Sanguine (INTS), the University of Paris, and grants from Laboratory of Excellence (Labex) GR-Ex, reference No. ANR-11-LABX-0051. The Labex GR-Ex is funded by the IdEx program âInvestissements dâavenirâ of the French National Research Agency, reference No. ANR-18-IDEX-0001. R.B. was funded by the European Unionâs Horizon 2020 Research and Innovation Program under grant agreement No. 675115-RELEVANCE-H2020-MSCA-ITN-2015. M.B. was funded by MinistĂšre de lâEnseignement SupĂ©rieur et de la Recherche at the BioSPC Doctoral School. R.B. and M.B. also received financial support from SociĂ©tĂ© Française dâHĂ©matologie (SFH) and Club du Globule Rouge et du Fer (CGRF).Peer reviewedPublisher PD
Altered Ca2+ Homeostasis in Red Blood Cells of Polycythemia Vera Patients Following Disturbed Organelle Sorting during Terminal Erythropoiesis
The authors thank Thierry Peyrard, Dominique Gien, Sirandou Tounkara, and Eliane VĂ©ra at Centre National de RĂ©fĂ©rence pour les Groupes Sanguins for the management of blood samples. The authors thank Sandrine Genetet and Isabelle Mouro-Chanteloup at the Inserm UMR_S1134 unit for their assistance in experiments. The authors also thank MichaĂ«l Dussiot at the Institute Imagine for his assistance in imaging flow cytometry. We thank Johanna Bruce and Virginie Salnot at 3P5 Proteomics Platform for sample preparation and analysis, and François Guillonneau and Patrick Mayeux for their management and strategies. Funding: The work was supported by Institut National de la SantĂ© et de la Recherche MĂ©dicale (Inserm); Institut National de la Transfusion Sanguine (INTS); the University of Paris; and grants from Laboratory of Excellence (Labex) GR-Ex, reference No. ANR-11-LABX-0051. The Labex GR- Ex is funded by the IdEx program âInvestissements dâavenirâ of the French National Research Agency, reference No. ANR-11-IDEX-0005-02 and ANR-18-IDEX-0001. R.B., M.G.R., and D.M.A. were funded by the European Unionâs Horizon 2020 Research and Innovation Program under grant agreement No. 675115-RELEVANCE-H2020-MSCA-ITN-2015. R.B. also received financial support from SociĂ©tĂ© Française dâHĂ©matologie (SFH) and Club du Globule Rouge et du Fer (CGRF). R.B. is currently funded by the Innovate UK Research and Innovation Knowledge Transfer Partnership (KTP) between University of Aberdeen and Vertebrate Antibodies Ltd. (Partnership No. KTP12327). T.D. was supported by PhD grants from UniversitĂ© Paris Saclay MESR (MinistĂšre Enseignement SupĂ©rieur et de la Recherche) and then FRM (Fondation recherche mĂ©dicale). The Orbitrap Fusion mass spectrometer was acquired with funds from Fonds Europeen de Developpement Regional (FEDER) through the Operational Program for Competitiveness Factors and Employment 2007-2013 and from the Canceropole Ile de France.Peer reviewedPublisher PD
BASES MOLECULAIRES ET RELATIONS STRUCTURE/FONCTION DES ANTIGENES DE GROUPE SANGUIN LUTHERAN (FONCTION D'ADHERENCE A LA LAMININE ET POLARISATION MEMBRANAIRE EPITHELIALE)
PARIS7-BibliothĂšque centrale (751132105) / SudocSudocFranceF
High Affinity Binding of Escherichia coli Cytotoxic Necrotizing Factor 1 (CNF1) to Lu/BCAM Adhesion Glycoprotein
High Affinity Binding of Escherichia coli Cytotoxic Necrotizing Factor 1 (CNF1) to Lu/BCAM Adhesion Glycoprotein
The protein toxin Cytotoxic Necrotizing Factor 1 (CNF1) is a major virulence factor of pathogenic Escherichia coli strains. It belongs to a family of single chain AB-toxins, which enter mammalian cells by receptor-mediated endocytosis. Recently, we identified the Lutheran (Lu) adhesion glycoprotein/basal cell adhesion molecule (BCAM) as a cellular receptor for CNF1. Here, we identified the Ig-like domain 2 of Lu/BCAM as main interaction site of the toxin by direct protein-protein interaction and competition studies. Using surface plasmon resonance, we showed a high affinity CNF-Lu/BCAM interaction with a KD of 2.8 nM. Furthermore, we performed small-angle X-ray scattering to define the molecular envelope of the Lu/BCAM-CNF1 complex, suggesting a 6:1 ratio of Lu/BCAM to CNF1 in the receptor-toxin complex. This study leads to a deeper understanding of the interaction between CNF1 and Lu/BCAM, and presents novel opportunities for the development of future anti-toxin strategies
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