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223 results on '"Si-Tahar, M."'

2. Pulmonary immune responses against SARS-CoV-2 infection: harmful or not?

Author

Guillon, A., Hiemstra, P. S., and Si-Tahar, M.

Subjects
Development and progression, Health aspects, Medical research -- Health aspects, Infection -- Development and progression, Lung diseases -- Development and progression, Immune response -- Health aspects, COVID-19 -- Development and progression, Medicine, Experimental -- Health aspects
Abstract

Author(s): A. Guillon [sup.1] [sup.2] [sup.3], P. S. Hiemstra [sup.4], M. Si-Tahar [sup.2] [sup.3] Author Affiliations: (1) grid.411167.4, 0000 0004 1765 1600, Intensive Care Unit, Tours University Hospital, , 2 [...]

Published
2020
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7. Retour triomphant des J2R 2023 à Tours : un tourbillon d’échanges scientifiques et d’émotion

Author

Annesi-Maesano, I., primary, Bonniaud, P., additional, Bouchaud, G., additional, Boyer, L., additional, Gazzeri, S., additional, Gosset, P., additional, Gras, D., additional, Guibert, C., additional, Guignabert, C., additional, Mari, B., additional, Matecki, S., additional, Morélot, C., additional, Pilette, C., additional, Planes, C., additional, Plantier, L., additional, Polette, M., additional, Si-Tahar, M., additional, Taillé, C., additional, and Vachier, I., additional

Published
2024
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13. RESPIRenT : RESeau de Pneumologie en Innovation et Recherche translaTionnelle, un nouveau souffle pour les J2R

Author

Annesi-Maesano, I., primary, Bonniaud, P., additional, Bouchaud, G., additional, Boyer, L., additional, Gazzeri, S., additional, Gosset, P., additional, Gras, D., additional, Guibert, C., additional, Guignabert, C., additional, Mari, B., additional, Matecki, S., additional, Morélot, C., additional, Pilette, C., additional, Planes, C., additional, Plantier, L., additional, Polette, M., additional, Si-Tahar, M., additional, Taillé, C., additional, and Vachier, I., additional

Published
2022
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19. Tonnerre de Brest ! Des Journées de Recherche Respiratoires 2020 pas comme les autres…

Author

Annesi-Maesano, I., primary, Bonniaud, P., additional, Bouchaud, G., additional, Boyer, L., additional, Frossard, N., additional, Gazzeri, S., additional, Gosset, P., additional, Gras, D., additional, Guibert, C., additional, Guignabert, C., additional, Mari, B., additional, Matecki, S., additional, Morelot, C., additional, Pilette, C., additional, Planes, C., additional, Plantier, L., additional, Polette, M., additional, Si-Tahar, M., additional, Taillé, C., additional, and Vachier, I., additional

Published
2021
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25. Les Auteurs

Author

Abroug, F., Abtan, J., Aguilar, C., Aissaoui, N., Ait Hssain, A., Ait-Oufella, H., Ajzenberg, N., Aloy, B., Ammirati, C., Amoura, Z., Amstutz, P., Anglicheau, D., Annane, D., Anxionnat, R., Arab, K., Argaud, L., Arnaout, M., Arrivé, L., Assouad, J., Aubron, C., Augis, V., Ayari, H., Azabou, E., Azoulay, E., Bakhos, D., Bailly, E., Bailly, P., Baldolli, A., Barbaud, A., Barbier, F., Barbut, F., Bardon, J., Barraud, D., Barreda, T., Barrot, L., Barry, B., Bartier, J.-C., Bastien, O., Baud, F.J., Baudel, J.-L., Beaussier, M., Bedos, J.-P., Bédry, R., Béduneau, G., Beloncle, F., Beltrami, A., Benghanem, S., Ben Ammar, M., Ben Hadj Salem, O., Benchetrit, D., Benyamina, M., Benzidi, Y., Bernardin, G., Bertholdt, C., Bertocchio, J.-P., Bertoletti, L., Bertrand, C., Besnier, E., Beuret, P., Beydon, L., Bialais, É., Bienaimé, F., Bigé, N., Bihan, K., Bilbault, P., Binoche, A., Biour, M., Birgand, G., Bitker, L., Blanc, J.-V., Blatteau, J.-E., Blivet, S., Blot, F., Bodenes, L., Boels, D., Bohé, J., Boissier, F., Boiteau, R., Boles, J.-M., Bollaert, P.-E., Bondeelle, L., Bonnet, N., Boudon, M., Bouglé, A., Boulain, T., Boulanger, D., Bounab, R., Bourcier, S., Bourigault, C., Bourenne, J., Bouteau, I., Boutonnet, M., Bouzgarrou, R., Boyer, A., Boyer, D., Boyer-Suavet, S., Bracard, S., Brault, C., Bretonnière, C., Bréchot, N., Bridoux, F., Brivet, F.-G., Brochard, L., Bruder, N., Bruneel, F., Brunet, J., Burgel, P.-R., Buscot, M., Cabrio, D., Cadranel, J., Calvet, L., Camus, C., Canaud, B., Canellas, A., Canet, E., Capaldo, L., Capellier, G., Carbonell, N., Cariou, A., Carli, P., Carpentier, D., Carrat, F., Carteaux, G., Casolla, B., Castanares-Zapatero, D., Castelain, V., Cavaillon, J.-M., Cecchini, J., Cha, O., Chamaraux-Tran, T.-N., Champigneulle, B., Chanard, J., Charles, P.-E., Charpentier, J., Chastre, J., Chaussard, M., Chemla, D., Cherifa, M., Chiche, J.-D., Cholley, B., Chopin, C., Chosidow, O., Choukroun, M.-L., Clair, B., Claude, F., Clavier, T., Clément, E., Clere-Jehl, R., Clouzeau, B., Cochereau, I., Cohen, Y., Collins, M., Combes, A., Commandeur, D., Contou, D., Coppo, P., Cordonnier, C., Coriat, P., Cornelis, F., Costedoat-Chalumeau, N., Cottin, V., Cour, M., Coutrot, M., Couturier, J., Couzigou, C., Cravoisy-Popovic, A., Crozier, S., Danel, V., Danin, P.-E., Dargaud, Y., Darmaun, D., Darmon, M., Daubin, C., David, S., De Backer, D., De Cagny, B., Decavèle, M., Decousus, H., Degos, V., De Groote, E., De Jong, A., Dekeyser, T., Delabranche, X., Delahaye, A., Delarue, J., Delclaux, C., Delemazure, J., Delile, E., Delisle, S., Dellamonica, J., Delluc, A., Delplancq, H., Deltour, S., De Martin, E., Demeret, S., Demiselle, J., De Montalembert, M., Demoule, A., Dépret, F., de Prost, N., Dequatre-Ponchelle, N., Dequin, P.-F., Deray, G., Derelle, A.-L., Deriaz, H., De Schryver, N., Deshayes, S., Desmettre, T., Desrousseaux, J., Dessevre, A., Dewitte, A., Deye, N., Dhainaut, J.-F., Didier, S., Diehl, J.-L., Di Martino, V., Djibré, M., Dolz, M., Dorandeu, F., Dorent, R., Do Vale, J., Dres, M., Dreyfuss, D., Dromer, C., Dubée, V., Duburcq, T., Duceau, B., Du Cheyron, D., Ducloy-Bouthors, A.-S., Dugernier, J., Durand, A., Durand, F., Duranteau, J., Durocher, A., Dussaule, J.-C., Eckert, C., Écotière, L., Ehrmann, S., El Gharbi, F., Elbaz, M., Embriaco, N., Étienne, H., Essig, M., Fagon, J.-Y., Fagot-Gandet, F., Fartoukh, M., Faugeras, F., Favory, R., Faisy, C., Ferrière, N., Ferry, T., Flamant, M., Folscheid, D., Fontaine, E., Forel, J.-M., Fourrier, F, Fraipont, V., Franchineau, G., Francoz, C., Frat, J.-P., Fresco, R., Friedlander, G., Friedman, D., Fromentin, M., Gainnier, M., Galanaud, D., Garcia, H., Garret, C., Garrouste-Orgeas, M., Gateau, C., Geeraerts, T., Gehanno, P., Gempp, E., Geri, G., Germain, A., Giacardi, C., Gibelin, A., Gibot, S., Girardot, T., Girault, C., Giura, G., Gkalea, V., Godard, A., Godeau, B., Goffinet, F., Gonzalez-Bermejo, J., Gory, B., Gouëllo, J.-P., Goulenok, C., Goursaud, S., Goury, A., Goutagny, S., Graftieaux, J.-P., Grangé, S., Grimaldi, D., Gros, A., Gruson, D., Gruson-Vescovali, D., Guérin, C., Guérot, E., Guettrot-Imbert, G., Guervilly, C., Guidet, B., Guillon, A., Guillot, M., Guitton, C., Gutton, Ch., Haidar, M., Halimi, C., Hamada, S., Hammoud, K., Hansmann, Y., Hariri, G., Harlay, M.-L., Harrois, A., Harry, P., Hauw-Berlemont, C., Hébuterne, X., Hejblum, G., Helms, J., Hékimian, G., Heming, N., Herbrecht, J.-E., Hertig, A., Heshmati, F., Hickmann, C., Hites, M., Hong Tuan Ha, V., Houfflin-Debarge, V., Houhou, N., Houillier, P., Hua, C., Hullin, T., Humbert, M., Hugon-Vallet, É., Hurel, D., Ichaï, P., Ioos, V., Isnard-Bagnis, C., Jaber, S., Jacobs, F., Jacquens, A., Jaffal, K., Jaïs, X., Janus, N., Jardel, B., Jars-Guincestre, M.-C., Jaubert, P., Jehl, F., Jirka, A., Joannès-Boyau, O., Joffre, J., Jolliet, P., Joly, F., Joly, L.-M., Joly-Guillou, M.-L., Jouffroy, R., Jonard, M., Jougon, J., Jourdain, M., Jozwiak, M., Jully, M., Jung, B., Juniat, A.-A., Kandji, M., Kanfer, A., Karoubi, P., Kentish-Barnes, N., Kerlan, V., Khalil, A., Kim, S., Kimmoun, A., Klouche, K., Koffel, J.-C., Kopferschmitt, J., Laaban, J.P., Labadie, M., Labbé, V., Lachâtre, M., Labrousse, J., Lacroix, D., Lancel, S., Lanceleur, A., Landais, M., Landelle, C., Landman, C., Lanternier, F., Larcher, R., Launay-Vacher, V., Langeron, O., Lapostolle, F., Larmignat, P., Laterre, P.-F., Laudenbach, V., Laurent, V., Lautrette, A., Lavillegrand, J.-R., Lavolé, A., Law-ye, B., Lebas, B., Lebranchu, Y., Lebreton, G., Lebrun-Vignes, B., Leclercq, D., Le Conte, P., Le Corre, B., Lefaucheur, J.-P., Lefevre, J., Leflon-Guibout, V., Léger, D., Legrand, M., Le Gouez, A., Leguay, T., Lejay, M., Lellouche, F., Lemaire, F., Lemaitre, C., Lemarié, J., Lemiale, V., Lemonnier, M.-P., Lepape, A., Leprince, P., Leray-Moraguès, H., Léon, A., Leone, M., Lerolle, N., Le Roux, M., Leroy, O., Leteurtre, S., Lescot, T., Le Tulzo, Y., Leverve, X., Levy, B., Lévy, P., L'Her, E., Liao, L., Lienhart, A., Llitjos, J.-F., Lofaso, F., Lothe, M.-N., Loubières, Y., Louge, P., Lucet, J.-C., Luyt, C.E., Lyazidi, A., Maamar, A., Mahieu, R., Maillet, J.-M., Mainardi, J.-L., Maître, B., Maizel, J., Mallaret, M.-R., Mancebo, J., Manzo-Silberman, S., Marchalot, A., Marit, G., Markowicz, P., Marqué, S., Martin, O., Martin-Lefèvre, L., Marx, T., Massanet, P.L., Mathian, A., Mathieu, C., Mathieu, D., Maury, E., Maxime, V., Mazeraud, A., Meffert, A., Mégarbane, B., Mehl, J., Mekontso Dessap, A., Melchior, C., Meng, P., Mentec, H., Mercier, F.-J., Mercat, A., Merdji, H., Méresse, Z., Mertes, P.-M., Mesland, J.-B., Meyer, G., Meynard, J.-L., Meziani, F., Miatello, J., Michard, B., Mira, J.-P., Mismetti, P., Misset, B., Miyara, M., Moga, L., Mohty, M., Monchi, M., Monéger, G., Monneret, G., Monnet, X., Monnier-Cholley, L., Montani, D., Mora, P., Morau, E., Moreau, AS., Morel, G., Morawiec, E., Mortaza, S., Mottier, D., Murgier, M., Naccache, L., Nace, L., Naeije, R., Naïm, G., Nave, S., Nitenberg, A., Nouette-Gaulain, K., Nouri-Neuville, M., Nousbaum, J.B., Novy, E., Nuss, P., Obadia, É., Offenstadt, G., Oger, E., Onimus, T., Orlikowski, D., Oro, S., Osman, O., Ouanes, I., Ouanes-Besbes, L., Ouedraogo, R., Outin, H., Oziel, J., Ozier, Y., Pajot, O., Papazian, L., Parmentier, E., Parquin, F., Parrilla, F.J., Parrot, A., Pasquet, A., Pateron, D., Paugam-Burtz, C., Peigné, M., Peineau, S., Pelaccia, T., Pène, F., Perrotin, D., Pessey, F., Pham, T., Philit, F., Pichené, C., Picod, A., Piette, J.-C., Pillet, O., Pilmis, B., Pineau, J., Pineton de Chambrun, M., Piquilloud, L., Pirracchio, R., Piton, G., Plantefève, G., Podglajen, I., Poidevin, A., Poissy, J., Pottecher, J., Poujol, A.-L., Poussardin, C., Prat, F., Préau, S., Preiser, J.-C., Prevel, R., Prot-Bertoye, C., Pruvo, J.-P., Pujol, S., Puntous, M., Quenot, J.-P., Quevrain, E., Quillerou, B., Rabaud, C., Raynard, B., Raynaud, L., Regard, L., Reignier, J., Reizine, F., Réminiac, F., Renault, A., Revest, M., Ricard, J.-D., Richalet, J-P., Richard, C., Richard, J-C.M., Ricôme, J.-L., Ridel, C., Rigollot, M., Rigaud, J.-P., Rigolet, A., Rimmelé, T., Rineau, E., Robert, R., Robert, T., Robineau, O., Roch, A., Roesler, J., Roger, I., Rohaut, B., Roullet, S., Rousset, D., Roux, D., Rozé, H., Rudler, M., Rugeri, L., Ruppé, E., Sab, J.-M., Sacleux, S.-C., Saliba, F., Samuel, D., Sauder, P., Saulnier, F., Sauvanet, A., Savale, L., Savoye, G., Schlemmer, B., Schlemmer, F., Schmidt, E., Schmidt, M., Schneider, F., Schneider, S.M., Schortgen, F., Schuby, M., Schwan, R., Schwebel, C., Seguin, A., Seksik, P., Senneville, É., Seronde, M.-F., Sharshar, T., Sigaut, S., Silva, S., Si-Tahar, M., Sitbon, O., Sivanandamoorthy, S., Slama, M., Sollet, J.-P., Somme, D., Sonneville, R., Souday, V., Soufir, L., Soussi, S., Souweine, B., Spaulding, C., Squara, P., Steg, P.-G., Sterlin, D., Stiel, L., Sublon, M., Sudre, E., Surgers, L., Szychowiak, P., Tacquard, C., Tadié, J.-M., Talvard, O., Tamburini, J., Tamion, F., Tarazona, V., Tardy, B., Taright, N., Tasseau, F., Tattevin, P., Tauzin-Fin, P., Tazarourte, K., Teboul, J.-L., Terzi, N., Thabut, D., Thaler, F., Thellier, D., Thervet, E., Thévenot, T., Thibault, M., Thibault, R., Thierry, A., Thille, A.W., Thomas, G., Thumerel, M., Thuong, M., Thy, M., Timsit, J.-F., Tissières, P., Tonnelet, R., Touchard, G., Tournoy, A., Tourtier, J.-P., Tourtier, Y., Tran Van Nhieu, J., Troché, G., Trouillet, J.L., Ubeaud-Séquier, G., Uhel, F., Urbina, T., Valeyrie-Allanore, L., Van de Louw, A., Van der Meersch, G., Vargas, F., Velly, L., Venet, F., Verdon, R., Veyradier, A., Vieillard-Baron, A., Vignon, Ph., Vigué, B., Villers, D., Vinsonneau, C., Voiriot, G., Weil-Verhoeven, D., Wiel, É., Wittebole, X., Woch, S., Woerther, P.-L., Woimant, F., Wolff, M., Wysocki, M., Xhaard, A., Yazdanpanah, Y., Zafrani, L., Zahar, J.-R., Zarrouk, V., Zéni, F., Zerbib, P., Zerbib, Y., Zieleskiewicz, L., Zlotnik, D., and Zuber, B.

Published
2020
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27. French Intensive Care Society, International congress - Réanimation 2016

Author

Jaillette, E, Girault, C, Brunin, G, Zerimech, F, Chiche, A, Broucqsault Dedrie, C, Fayolle, C, Minacori, F, Alves, I, Barrailler, S, Robriquet, L, Delaporte, E, Thellier, D, Delcourte, C, Duhamel, A, Nseir, S, Valette, X, Desmeulles, I, Savary, B, Masson, R, Seguin, A, Daubin, C, Sauneuf, B, Verrier, P, Pottier, V, Orabona, M, Samba, D, Viquesnel, G, Lermuzeaux, M, Hazera, P, Hanouz, J, Parienti, J, Du Cheyron, D, Demoule, A, Clavel, M, Rolland Debord, C, Perbet, S, Terzi, N, Kouatchet, A, Wallet, F, Roze, H, Vargas, F, Guérin, C, Dellamonica, J, Jaber, S, Similowski, T, Quenot, J, Binquet, C, Vinsonneau, C, Barbar, S, Vinault, S, Deckert, V, Lemaire, S, Hssain, A, Bruyère, R, Souweine, B, Lagrost, L, Adrie, C, Jung, B, Daurat, A, De Jong, A, Chanques, G, Mahul, M, Monnin, M, Molinari, N, Lheureux, O, Trepo, E, Hites, M, Cotton, F, Wolff, F, Surin, R, Créteur, J, Vincent, J, Gustot, T, Jacobs, F, Taccone, F, Neuville, M, Timsit, J, El Helali, N, Le Monnier, A, Magalhaes, E, Radjou, A, Smonig, R, Soubirou, J, Voiriot, G, Sonneville, R, Bouadma, L, Mourvillier, B, Gélisse, E, Brasseur, A, Roisin, S, De Backer, D, Van Ruychevelt, V, Carlier, E, Piagnerelli, M, Vanhaeverbeek, M, Danguy, C, Biston, P, Au, S, Begot, E, Dalmay, F, Repessé, X, Prat, G, Bouferrache, K, Slama, M, Vieillard Baron, A, Monnet, X, Marik, P, Teboul, J, Jozwiak, M, Richard, C, Chauvet, J, El Dash, S, Delastre, O, Bouffandeau, B, Jusserand, D, Michot, J, Bauer, F, Brazier, F, Mercado, P, Kontar, L, Titeca, D, De Cagny, B, Bacari Risal, G, Riviere, A, Maizel, J, Guillot, C, Le Reun, C, Lampin, M, Sadik, A, Botte, A, Leteurtre, S, Collins, A, Kempeneers, C, Cajgfinger, N, Ohlmann, C, Pouyau, R, Subtil, F, Baudin, F, Massenavette, B, Javouhey, E, Milesi, C, Essouri, S, Liet, J, Afanetti, M, Durand, S, Durand, P, Roze, J, Dupont, D, Cambonie, G, Soyer, B, Rusca, M, Lukaszewicz, A, Crassard, I, Guichard, J, Bresson, D, de la Garanderie, D, Cantier, M, Sabben, C, Louedec, L, Delbosc, S, Journé, C, Ou, P, Klein, I, Chau, F, Lefort, A, Desilles, J, Michel, J, Mazighi, M, Salem, O, Demeret, S, Bolgert, F, Sharshar, T, Grabli, D, Arib, S, Crippa, I, Soummer, A, Engrand, N, Guedin, P, Aldea, S, Cerf, C, Desailly, V, Pasquier, P, Brun, P, Roux, D, Latournerie, G, Kasprzyk, L, Grosjean, V, Latreche, A, Habert, P, Huot, S, Jobin, T, Tesnière, A, Dreyfuss, D, Ricard, J, Mignon, A, Gaudry, S, Laithier, F, Kimmoun, A, Chouihed, T, Albizzati, S, Camenzind, E, Vanhuyse, F, Levy, B, Cour, M, Venet, F, Hernu, R, Demaret, J, Monneret, G, Argaud, L, Dumas, F, Lamhaut, L, Rosencher, J, Pène, F, Varenne, O, Carli, P, Jouven, X, Spaulding, C, Cariou, A, Geri, G, Bonnetain, F, Marijon, E, Empana, J, Mirouse, A, Resche Rigon, M, Mayaux, J, Rabbat, A, Meert, A, Benoit, D, Bruneel, F, Azoulay, E, Dupuis, C, Schwebel, C, Ruckly, S, Goldgran Toledano, D, Marcotte, G, Lafarge, A, Pichereau, C, Theodose, I, Scotto, M, Kemlin, D, Ghrenassia, E, Schlemmer, B, Vimpere, D, Galicier, L, Contou, D, Guérot, E, Grimaldi, D, Ricome, S, Maury, E, Plantefève, G, Dessap, A, Brun Buisson, C, de Prost, N, Dubé, B, Delemazure, J, Dres, M, Rousseau, L, Drouot, X, Diaz, V, Rebollar, Y, Frat, J, Thille, A, Aissa, D, Coquet, P, Ruiz, J, Ferre, F, Hoarau, L, Riu Poulenc, B, Bataille, B, Silva, S, Baudel, J, Bigé, N, Tahiri, J, Dubée, V, Guidet, B, Ait Oufella, H, Jinglun, L, Shen, F, Bailly, S, Leroy, O, Montravers, P, Constantin, J, Dupont, H, Guillemot, D, Lortholary, O, Perrigault, P, Gangneux, J, Razazi, K, Mekontso Dessap, A, Jansen, C, Lecronier, M, Sandrine, V, Mira, J, Blein, S, Marin, N, Rousseau, C, Charpentier, J, Pachot, A, Hraiech, S, Bordes, J, De, L, Mège, J, Forel, J, Guervilly, C, Adda, M, Raoult, D, Papazian, L, Kentish Barnes, N, Cohen Solal, Z, Souppart, V, Kerhuel, L, Haubertin, C, Exbrayat, I, Rozières, E, Argain, A, Suc, A, Vignes, M, Cougot, P, Fourcade, O, Brunel, E, Messika, J, Tubach, F, Dubief, E, Pasquet, B, Guillo, S, Pierron, C, Grimaud, M, Farnoux, C, Maillard, A, Decavèle, M, Prodanovic, H, Idbaih, A, Alentorn, A, Delattre, J, De Montmollin, E, Brule, N, Conrad, M, Dailler, F, Navellou, J, Alves, M, Tonnelier, J, Picard, G, Rogemond, V, Honnorat, J, Marzorati, C, Lebert, C, Perez, P, Citerio, G, Legriel, S, Tripon, S, Mallet, M, Rudler, M, Imbert Bismut, F, Thabut, D, Canet, E, Faguer, S, Moreau, A, Barbier, F, Merceron, S, Guitton, C, Labadie, F, Lemiale, V, Faucher, E, Klouche, K, Chevret, S, Ragot, S, Coudroy, R, Boulain, T, Jamet, A, Mercat, A, Brochard, L, Roux, A, Franchineau, G, Brechot, N, Lebreton, G, Hekimian, G, Nieszkowska, A, Leprince, P, Trouillet, J, Combes, A, Schmidt, M, Barrot, L, Piton, G, Bailey, M, Panwar, R, Belin, N, Belon, F, Patry, C, Grandperrin, M, Chaignat, C, Labro, G, Vivet, B, Capellier, G, Daix, T, Guérin, E, Tavernier, E, Mercier, E, Gissot, V, Vallejo, C, François, B, Ravry, C, Pichon, N, Chapellas, C, Fedou, A, Galy, A, Ploy, M, Barraud, O, Vignon, P, Thooft, A, Conotte, R, Colet, J, Le Dorze, M, Tarazona, V, Brumpt, C, 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Elkhawand, C, Vermeesh, F, Vermeesh, F., and CITERIO, GIUSEPPE

Abstract

Determinants of outcome in critically ill patients with hematological malignancy and central neurological failure: data from the TRIAL OH study

Published
2016

29. Innate sensing of HIV-infected cells

Author

4.Lepelley A, Louis S, Sourisseau M, Law HK, Pothlichet J, Schilte C, Chaperot L, Plumas J, Randall RE, Si-Tahar M, Mammano F, Albert ML, and Schwartz O

Published
2011

30. Preliminary studies for the establishment of a model of CFTR-deficient piglets

Author

Guillon, A., primary, Barc, C., additional, Chevaleyre, C., additional, Riou, M., additional, Pezant, J., additional, Olivier, M., additional, Coigné, J., additional, Venturi, E., additional, Lardy, H., additional, Villemagne, T., additional, Moënne-Loccoz, J., additional, Brea, D., additional, Winter, N., additional, Mélo, S., additional, Gauthier, F., additional, Schwartz, B., additional, Bähr, A., additional, Wolf, E., additional, Meurens, F., additional, Berri, M., additional, Ramphal, R., additional, Attucci, S., additional, Buzoni-Gatel, D., additional, Si-Tahar, M., additional, and Sarradin, P., additional

Published
2014
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46. Constitutive and regulated secretion of secretory leukocyte proteinase inhibitor by human intestinal epithelial cells

Author

Si-Tahar, M., Merlin, D., Sitaraman, S., and Madara, J.L.

Abstract

Background & Aims: Epithelial cells participate in immune regulation and mucosal integrity by generating a range of biologically active mediators. In the intestine, little is known about the potential endogenous anti-inflammatory molecules. Secretory leukocyte proteinase inhibitor (SLPI) is a major serine proteinase inhibitor, a potent antibiotic, and thus a potential anti-inflammatory molecule, although it is not known if it is secreted by intestinal epithelial cells. Methods: We show, by reverse-transcription polymerase chain reaction, the presence of SLPI messenger RNA in human model intestinal epithelial cell lines (Caco2-BBE, T84, and HT29-Cl.19A) and human jejunum and colon biopsy specimens. The polymerase chain reaction product was cloned and sequenced and is identical to that of SLPI isolated previously from the human parotid gland. Results: As analyzed by enzyme-linked immunosorbent assay, the constitutive secretion of SLPI occurs in a markedly polarized manner toward the apical surface and is enhanced by inflammatory mediators including tumor necrosis factor @a and interleukin 1@b (~3.5-fold increase over control value). SLPI release is also stimulated by activation of protein kinase C isoenzymes, but not by activation of adenosine 3',5'-cyclic monophosphate- or Ca^2^+-regulated signaling molecules. SLPI protein is detectable in intestinal lavage fluids collected from normal adult humans. Recombinant SLPI attenuates digestive enzyme (trypsin)- or leukocyte proteinase (elastase)-induced permeability alteration of a model epithelia in a dose-dependent manner. Moreover, SLPI exhibits an antibacterial activity against at least one major intestinal pathogen, Salmonella typhimurium. In contrast, SLPI does not influence epithelial barrier integrity as assessed by transepithelial conductance measurements or electrogenic ion transport. Conclusions: These results establish that human intestinal epithelium expresses and apically secretes SLPI, a molecule that may significantly contribute to the protection against attack from inflammatory cells and digestive enzymes, as well as against microbial infection. GASTROENTEROLOGY 2000;118:1061-1071

Published
2000
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47. Adhesion molecules expressed on homing lymphocytes in model intestinal epithelia

Author

Shibahara, T., Si-Tahar, M., Shaw, S.K., and Madara, J.L.

Abstract

Background & Aims: The development of intestinal intraepithelial lymphocytes (IELs) requires the movement of lymphocytes into the epithelial compartment (i.e., IEL homing). The rules governing and the biologic consequences of IEL homing are poorly understood. The aims of this study were to examine the adhesion molecules involved in IEL homing and the phenotypic alteration of lymphocytes as a consequence of homing. Methods: We previously developed an in vitro IEL homing model consisting of human IEL cell lines and a polarized monolayer of human intestinal epithelial T84 cells. Homing capacity of lymphocytes was assessed by measuring their migration into epithelial monolayers, and phenotypic analysis was performed by flow cytometry. Results: In this model, ~30% of lymphocytes moved into the epithelial monolayer, regardless of the lymphocyte concentration. Flow cytometric screening of adhesion molecules revealed that homed lymphocytes expressed high levels of integrin @aX@b2 and @aE@b7 and low levels of @a4@b7 compared with nonhomed lymphocytes. In addition, subpopulations sorted as @aX@b2^h^i^g^h or @aE@b7^h^i^g^h independently showed greater homing capacities. After homing, @aE@b7 and intercellular adhesion molecule 1 (ICAM-1) on homed lymphocytes were significantly up-regulated, which was consistent with their high expression observed on freshly isolated human IELs. The up-regulation of @aE@b7 (but not ICAM-1) was completely dependent on epithelial-derived transforming growth factor @b1 (TGF-@b1). The expression of @aX@b2 was observed on a small population of freshly isolated human IELs, and was markedly induced by stimulation. Also, epithelial-derived TGF-@b1 down-regulated the @aX@b2 expression (an event likely to occur after homing). Conclusions: Our findings indicate a relationship between IEL @aX@b2 and @aE@b7 expression and homing into intestinal epithelia. We also show that phenotypic alteration of IELs is induced by close interaction with intestinal epithelia as a consequence of homing. GASTROENTEROLOGY 2000;118:289-298

Published
2000
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48. Human neutrophil elastase proteolytically activates the platelet integrin alphaIIbbeta3 through cleavage of the carboxyl terminus of the alphaIIb subunit heavy chain. Involvement in the potentiation of platelet aggregation.

Author

Si-Tahar, M, Pidard, D, Balloy, V, Moniatte, M, Kieffer, N, Van Dorsselaer, A, and Chignard, M

Abstract

Neutrophil elastase (NE) and cathepsin G are two serine proteinases released concomitantly by stimulated polymorphonuclear neutrophils. We previously demonstrated that while NE by itself does not activate human platelets, it strongly enhances the weak aggregation induced by a threshold concentration of cathepsin G (threshold of cathepsin G) (Renesto, P., and Chignard, M. (1993) Blood 82, 139-144). The aim of this study was to delineate the molecular mechanisms involved in this potentiation process. Two main pieces of data prompted us to focus on the activation of the platelet fibrinogen receptor, the alphaIIbbeta3 integrin. First, previous studies have shown this integrin to be particularly prone to proteolytic regulation of its function. Second, we found that the potentiating activity of NE on the threshold of cathepsin G-induced platelet aggregation was strictly dependent on the presence of exogenous fibrinogen. Using flow cytometry analysis, NE was shown to trigger a time-dependent binding of PAC-1 and AP-5, two monoclonal antibodies specific for the activated and ligand-occupied conformers of alphaIIbbeta3. Furthermore, the potentiated aggregation was shown to result from an increased capacity of platelets to bind fibrinogen. Indeed, the combination of NE and threshold of cathepsin G increased the binding of PAC-1 approximately 5.5-fold over basal values measured on nontreated platelets, whereas this binding raised only by approximately 3-fold in threshold of cathepsin G-stimulated platelets (p < 0.05). By contrast, phosphatidic acid accumulation, pleckstrin phosphorylation, and calcium mobilization produced by the combination of NE and threshold of cathepsin G were not significantly different from those measured with threshold of cathepsin G alone (p > 0.05), indicating that the phospholipase C/protein kinase C pathway is not involved in the potentiation of aggregation. The foregoing data, as well as the requirement of catalytically active NE to trigger alphaIIbbeta3 activation and potentiate threshold of cathepsin G-initiated platelet aggregation, led us to examine whether the structure of this integrin was affected by NE. Immunoblot and flow cytometry analysis revealed a limited proteolysis of the carboxyl terminus of the alphaIIb subunit heavy chain (alphaIIbH), as judged by the disappearance of the epitope for the monoclonal antibody PMI-1. Mass spectrometry studies performed on a synthetic peptide mapping over the cleavage domain of alphaIIbH predicted the site of proteolysis as located between Val837 and Asp838. Treatment by NE of ATP-depleted platelets or Chinese hamster ovary cells expressing human recombinant alphaIIbbeta3 clearly established that activation of the integrin was independent of signal transduction events and was concomitant with the proteolysis of alphaIIbH. In support of this latter observation, a close correlation was observed between the kinetics of proteolysis of alphaIIbH on platelets and that of expression of the ligand binding activity of alphaIIbbeta3 (r2 = 0.902, p

Published
1997

49. Inhibition of neutrophil serine proteinases by suramin.

Author

Cadène, M, Duranton, J, North, A, Si-Tahar, M, Chignard, M, and Bieth, J G

Abstract

Suramin, a hexasulfonated naphtylurea recently used as an anti-tumor drug, is a potent inhibitor of human neutrophil elastase, cathepsin G, and proteinase 3. The complexes it forms with these enzymes are partially active on synthetic substrates, but full inhibition takes place when elastase activity is measured with fibrous elastin or when cathepsin G activity is measured using platelet aggregation. One molecule of elastase binds four molecules of suramin with a Ki of 2 x 10(-7) M as determined by enzyme inhibition or intrinsic fluorescence enhancement of suramin. The binding curves show no sign of cooperativity or anticooperativity. The Ki for the complexes with cathepsin G and proteinase 3 are 8 x 10(-8) and 5 x 10(-7) M, respectively. Ionic strength increases the Ki of the elastase-suramin complex in a way that suggests that four of the six sulfonate groups of suramin form ionic interactions with basic residues of the enzyme and that at saturation almost all arginines of elastase form salt bridges with suramin. The neutrophil proteinase-inhibitory activity of suramin might be used to prevent tissue destruction and thrombus formation in diseases where massive infiltration and activation of neutrophils take place.

Published
1997

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