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20 results on '"Croix, Cécile"'

2. Anticalin N- or C-Terminal on a Monoclonal Antibody Affects Both Production and In Vitro Functionality

Author

Aubrey, Nicolas, primary, Gouilleux-Gruart, Valérie, additional, Dhommée, Christine, additional, Mariot, Julie, additional, Boursin, Fanny, additional, Albrecht, Nicolas, additional, Bergua, Cécile, additional, Croix, Cécile, additional, Gilotin, Mäelle, additional, Haudebourg, Eloi, additional, Horiot, Catherine, additional, Matthias, Laetitia, additional, Mouline, Caroline, additional, Lajoie, Laurie, additional, Munos, Audrey, additional, Ferry, Gilles, additional, Viaud-Massuard, Marie-Claude, additional, Thibault, Gilles, additional, and Velge-Roussel, Florence, additional

Published
2022
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3. New Quinoxaline Derivatives as Dual Pim-1/2 Kinase Inhibitors: Design, Synthesis and Biological Evaluation

Author

Oyallon, Bruno, primary, Brachet-Botineau, Marie, additional, Logé, Cédric, additional, Robert, Thomas, additional, Bach, Stéphane, additional, Ibrahim, Sajida, additional, Raoul, William, additional, Croix, Cécile, additional, Berthelot, Pascal, additional, Guillon, Jean, additional, Pinaud, Noël, additional, Gouilleux, Fabrice, additional, Viaud-Massuard, Marie-Claude, additional, and Denevault-Sabourin, Caroline, additional

Published
2021
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7. Consequences of cathepsin C inactivation for membrane exposure of proteinase 3, the target antigen in autoimmune vasculitis

Author

Seren, Seda, Rashed Abouzaid, Maha, Eulenberg-Gustavus, Claudia, Hirschfeld, Josefine, Nasr Soliman, Hala, Jerke, Uwe, N'Guessan, Koffi, Dallet-Choisy, Sandrine, Lesner, Adam, Lauritzen, Conni, Schacher, Beate, Eickholz, Peter, Nagy, Nikoletta, Szell, Marta, Croix, Cécile, Viaud-Massuard, Marie-Claude, Al Farraj Aldosari, Abdullah, Ragunatha, Shivanna, Ibrahim Mostafa, Mostafa, Giampieri, Francesca, Battino, Maurizio, Cornillier, Hélène, Lorette, Gérard, Stephan, Jean-Louis, Goizet, Cyril, Pedersen, John, Gauthier, Francis, Jenne, Dieter E., Marchand-Adam, Sylvain, Chapple, Iain L., Kettritz, Ralph, Korkmaz, Brice, Pathologies Respiratoires : Protéolyse et Aérosolthérapie, Université de Tours (UT)-Institut National de la Santé et de la Recherche Médicale (INSERM), National Research Center, Helmholtz-Gemeinschaft = Helmholtz Association, University of Birmingham, Medical & Molecular Genetics, University of Birmingham, School of Clinical and Experimental Medicine, Faculty of Chemistry, Technion - Israel Institute of Technology [Haifa], Unizyme Laboratories A/S, Partenaires INRAE, Department of Periodontology, People's Liberation Army No. 309 Hospital, Department of Medical Genetics, University Hospital of North-Norway, Centre National de la Recherche Scientifique (CNRS), King Saud University [Riyadh] (KSU), Department of Dermatology, Venereology, and Leprosy, Sri Siddhartha Medical College, Department of Clinical Sciences, Swedish University of Agricultural Sciences (SLU), Service de dermatologie, Infectiologie et Santé Publique (UMR ISP), Institut National de la Recherche Agronomique (INRA)-Université de Tours (UT), Centre Hospitalier Universitaire de Saint-Etienne (CHU de Saint-Etienne), Laboratoire Maladies Rares: Génétique et Métabolisme (Bordeaux) (U1211 INSERM/MRGM), Université de Bordeaux (UB)-Groupe hospitalier Pellegrin-Institut National de la Santé et de la Recherche Médicale (INSERM), German Centre for Lung Research, Max Planck Institute of Neurobiology, Charité - UniversitätsMedizin = Charité - University Hospital [Berlin], Ministère de l'Enseignement Supérieur et de la Recherche, the 'Région Centre-Val de Loire' (Project BPCO-Lyse), European Project: 668036,H2020,H2020-PHC-2015-two-stage,RELENT(2015), ProdInra, Migration, RELapses prevENTion in chronic autoimmune disease: common mechanisms and co-morbidities - RELENT - - H20202015-11-01 - 2020-04-30 - 668036 - VALID, Université de Tours-Institut National de la Santé et de la Recherche Médicale (INSERM), Centre Hospitalier Régional Universitaire de Tours (CHRU TOURS), Institut National de la Recherche Agronomique (INRA)-Université de Tours, Centre Hospitalier Universitaire de Saint-Etienne [CHU Saint-Etienne] (CHU ST-E), and Centre Hospitalier Régional Universitaire de Tours (CHRU Tours)

Subjects
Adult, Male, neutrophile, Adolescent, Neutrophils, cathepsin C, Myeloblastin, Papillon-Lefèvre syndrome, Médecine humaine et pathologie, cathepsine, autoimmune disease, Cysteine Proteinase Inhibitors, activation cellulaire, protease inhibitor, Young Adult, antigen, genetic disease, cellule souche, Humans, cardiovascular diseases, Child, hématopoïèse, aminopeptidase, granulomatosis with polyangiitis, neutrophil, protease, proteinase 3, maladie autoimmune, [SDV.MHEP] Life Sciences [q-bio]/Human health and pathology, Cell Membrane, inhibiteur pharmacologique, Case-Control Studies, Child, Preschool, Proteolysis, Enzymology, Female, Human health and pathology, [SDV.MHEP]Life Sciences [q-bio]/Human health and pathology
Abstract

International audience; Membrane-bound proteinase 3 (PR3m) is the main target antigen of anti-neutrophil cytoplasmic autoantibodies (ANCA) in granulomatosis with polyangiitis, a systemic small-vessel vasculitis. Binding of ANCA to PR3m triggers neutrophil activation with the secretion of enzymatically active PR3 and related neutrophil serine proteases, thereby contributing to vascular damage. PR3 and related proteases are activated from pro-forms by the lysosomal cysteine protease cathepsin C (CatC) during neutrophil maturation. We hypothesized that pharmacological inhibition of CatC provides an effective measure to reduce PR3m and therefore has implications as a novel therapeutic approach in granulomatosis with polyangiitis. We first studied neutrophilic PR3 from 24 patients with Papillon-Lefèvre syndrome (PLS), a genetic form of CatC deficiency. PLS neutrophil lysates showed a largely reduced but still detectable (0.5-4%) PR3 activity when compared with healthy control cells. Despite extremely low levels of cellular PR3, the amount of constitutive PR3m expressed on the surface of quiescent neutrophils and the typical bimodal membrane distribution pattern were similar to what was observed in healthy neutrophils. However, following cell activation, there was no significant increase in the total amount of PR3m on PLS neutrophils, whereas the total amount of PR3m on healthy neutrophils was significantly increased. We then explored the effect of pharmacological CatC inhibition on PR3 stability in normal neutrophils using a potent cell-permeable CatC inhibitor and a CD34+ hematopoietic stem cell model. Human CD34+ hematopoietic stem cells were treated with the inhibitor during neutrophil differentiation over 10 days. We observed strong reductions in PR3m, cellular PR3 protein, and proteolytic PR3 activity, whereas neutrophil differentiation was not compromised.

Published
2018

10. Prolonged pharmacological inhibition of cathepsin C results in elimination of neutrophil serine proteases

Author

Guarino, Carla, primary, Hamon, Yveline, additional, Croix, Cécile, additional, Lamort, Anne-Sophie, additional, Dallet-Choisy, Sandrine, additional, Marchand-Adam, Sylvain, additional, Lesner, Adam, additional, Baranek, Thomas, additional, Viaud-Massuard, Marie-Claude, additional, Lauritzen, Conni, additional, Pedersen, John, additional, Heuzé-Vourc'h, Nathalie, additional, Si-Tahar, Mustapha, additional, Fıratlı, Erhan, additional, Jenne, Dieter E., additional, Gauthier, Francis, additional, Horwitz, Marshall S., additional, Borregaard, Niels, additional, and Korkmaz, Brice, additional

Published
2017
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19. Development of an ion-pairing reversed-phase liquid chromatography method using a double detection analysis (UV and evaporative light scattering detection) to monitor the stability of Alimta®-pemetrexed preparations: Identification and quantification of l-glutamic acid as a potential degradation product

Author

Respaud, Renaud, Tournamille, Jean-François, Croix, Cécile, Laborie, Hélène, Elfakir, Claire, and Viaud-Massuard, Marie-Claude

Subjects
*HIGH performance liquid chromatography, *GLUTAMIC acid, *LIGHT scattering, *ACETONITRILE, *EXPERIMENTAL design, *DRUG therapy
Abstract

Abstract: A new method based on high-performance liquid chromatography coupled to ultraviolet and evaporative light scattering detection (HPLC-UV-ELSD) was developed for the determination of l-glutamic acid, a potential degradation product of pemetrexed, and for the quantification of pemetrexed itself. This is an ion-pairing, reversed-phase method. The column was a Synergi MAX-RP C12 4μm (150mm×4.6mm). The mobile phase was 1mM tridecafluoroheptanoic acid in aqueous solution and acetonitrile under gradient elution mode. l-Glutamic acid was detected by ELSD, and pemetrexed by UV at 254nm. Good resolution was achieved between pemetrexed and l-glutamic acid. The HPLC method was validated according to SFSTP and ICH guidelines, and applied the accuracy profile procedure with a five-level validation experimental design. For pemetrexed, the decision criteria selected consisted of the acceptability limits (±3%) and the proportion of results within the calculated tolerance intervals (95%). In conclusion, the proposed analytical procedures were validated over the selected validation domains for l-glutamic acid (0.005–0.025mg/mL) and pemetrexed (0.4–0.6mg/mL) and shown to provide a very effective method. [ABSTRACT FROM AUTHOR]

Published
2011
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20. Consequences of cathepsin C inactivation for membrane exposure of proteinase 3, the target antigen in autoimmune vasculitis.

Author

Seren S, Rashed Abouzaid M, Eulenberg-Gustavus C, Hirschfeld J, Nasr Soliman H, Jerke U, N'Guessan K, Dallet-Choisy S, Lesner A, Lauritzen C, Schacher B, Eickholz P, Nagy N, Szell M, Croix C, Viaud-Massuard MC, Al Farraj Aldosari A, Ragunatha S, Ibrahim Mostafa M, Giampieri F, Battino M, Cornillier H, Lorette G, Stephan JL, Goizet C, Pedersen J, Gauthier F, Jenne DE, Marchand-Adam S, Chapple IL, Kettritz R, and Korkmaz B

Subjects
Adolescent, Adult, Case-Control Studies, Child, Child, Preschool, Female, Granulomatosis with Polyangiitis drug therapy, Granulomatosis with Polyangiitis genetics, Granulomatosis with Polyangiitis metabolism, Humans, Male, Myeloblastin genetics, Neutrophils enzymology, Proteolysis, Young Adult, Cathepsin C antagonists & inhibitors, Cell Membrane metabolism, Cysteine Proteinase Inhibitors pharmacology, Granulomatosis with Polyangiitis pathology, Myeloblastin metabolism
Abstract

Membrane-bound proteinase 3 (PR3 m ) is the main target antigen of anti-neutrophil cytoplasmic autoantibodies (ANCA) in granulomatosis with polyangiitis, a systemic small-vessel vasculitis. Binding of ANCA to PR3 m triggers neutrophil activation with the secretion of enzymatically active PR3 and related neutrophil serine proteases, thereby contributing to vascular damage. PR3 and related proteases are activated from pro-forms by the lysosomal cysteine protease cathepsin C (CatC) during neutrophil maturation. We hypothesized that pharmacological inhibition of CatC provides an effective measure to reduce PR3 m and therefore has implications as a novel therapeutic approach in granulomatosis with polyangiitis. We first studied neutrophilic PR3 from 24 patients with Papillon-Lefèvre syndrome (PLS), a genetic form of CatC deficiency. PLS neutrophil lysates showed a largely reduced but still detectable (0.5-4%) PR3 activity when compared with healthy control cells. Despite extremely low levels of cellular PR3, the amount of constitutive PR3 m expressed on the surface of quiescent neutrophils and the typical bimodal membrane distribution pattern were similar to what was observed in healthy neutrophils. However, following cell activation, there was no significant increase in the total amount of PR3 m on PLS neutrophils, whereas the total amount of PR3 m on healthy neutrophils was significantly increased. We then explored the effect of pharmacological CatC inhibition on PR3 stability in normal neutrophils using a potent cell-permeable CatC inhibitor and a CD34 + hematopoietic stem cell model. Human CD34 + hematopoietic stem cells were treated with the inhibitor during neutrophil differentiation over 10 days. We observed strong reductions in PR3 m , cellular PR3 protein, and proteolytic PR3 activity, whereas neutrophil differentiation was not compromised., (© 2018 Seren et al.)

Published
2018
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