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6. Safety and efficacy of self-administered inhaled loxapine (ADASUVE) in agitated patients outside the hospital setting: protocol for a phase IV, single-arm, open-label trial

Author

Gil E, Garcia-Alonso F, Boldeanu A, Teixeira T, Tordera V, Palmer Viciedo R, Salgado P, Domingo Ribas J, Corripio Collado I, Manuel Montes J, Correas Lauffer J, Ruiz Murugarrem S, Ovejero Garcia S, Mora F, Lopez A, Fontalba Navas A, Gonzalez Pinto A, Martinez R, Garcia Castrillo C, Toledo F, Vieta E, Gonzalez E, Franco M, Virgil Drasovean N, Havard Dahl N, Skagen B, Zilles D, Zwanzger P, Juckel G, Kahl K, Messer T, Kasper S, and Loxapine Inhaled Home Use Study In

Abstract

Introduction There is a need for fast-acting, non-injection antiagitation treatments that are well tolerated and can be used outside of healthcare facilities. In phase II/III trials, an inhaled formulation of loxapine (ADASUVE (R)), a well-established, first-generation antipsychotic agent, provided rapid control of mild to moderate agitation in the hospital setting. The present study was designed to investigate the safety and efficacy of inhaled loxapine when self-administered outside the hospital setting. Methods and analysis This phase IV, multicentre, single-arm, open-label clinical trial is being conducted in five countries in Europe: Spain, Germany, Norway, Romania and Austria. The aim is to include approximately 500 patients with schizophrenia or bipolar disorder who previously received and responded well to inhaled loxapine in the hospital setting. Eligible patients will be followed up for 6 months from baseline. They will be given a 10 mg dose of inhaled loxapine to self-administer outside the hospital setting to treat an agitation episode, should one occur. Patients will also be given a short-acting beta-agonist bronchodilator for treatment of possible severe respiratory side effects. The primary endpoint is incidence of serious adverse events (AEs) and respiratory AEs of special interest related to use of inhaled loxapine outside the hospital setting. Secondary endpoints include incidence of other AEs, Clinical Global Impression-Improvement scores up to 2 hours after self-administration of inhaled loxapine, time to improvement of agitation, patient satisfaction with treatment, treatment outcomes according to agitation severity and concordance between the patient (or a family member/caregiver) and the physician in scoring of agitation severity and the decision to self-administer inhaled loxapine. Ethics and dissemination The protocol received ethics committee approval in the participating countries between January and August 2016. The results of this study will be disseminated through one or more scientific papers.

Published
2018

7. dsDNA, ssDNA, G-quadruplex DNA, and nucleosomal DNA electrochemical screening using canthin-6-one alkaloid-modified electrodes

Author

Domenech-Carbo, A, Cebrian-Torrejon, G, de Miguel, L, Tordera, V, Rodrigues-Furtado, D, Assad-Kahn, S, Fournet, A, Figadere, B, Vazquez-Manrique, RP, and Poupon, E

Subjects
G-quadruplex-DNA, Natural products, Voltammetry of microparticles, DNA screening, Canthin-6-one
Abstract

Microparticulate films of a canthin-6-one alkaloid (L), a natural beta-carboline alkaloid presenting a characteristic naphtyridone motif, on glassy carbon electrodes yield different, separate voltammetric signals for dsDNA, ssDNA, G-quadruplex DNA, different degrees of DNA methylation and the biomimetic nucleosomal DNA with detection limit of 10(-5) M. This multiple-signal electrochemical behavior is in contrast with conventional use of DNA intercalators, only discriminating between different DNA forms by variations in the intensity of a unique signal. Complementary photochemical and scanning electrochemical microscopy (SECM) data suggest that the differences in the voltammetric response of the different DNA forms derive from the intercalating properties of the canthin-6-one. (C) 2013 Elsevier Ltd. All rights reserved.

Published
2014

10. Abstracts

Author

Barthelemy, O., primary, Silvain, J., additional, Brieger, D., additional, Bellemain-Appaix, A., additional, Cayla, G., additional, Beygui, F., additional, Lancar, R., additional, Collet, J. P., additional, Mercadier, A., additional, Montalescot, G., additional, Cha, K. S., additional, Nam, Y. H., additional, Kim, J. H., additional, Park, S. Y., additional, Park, T. H., additional, Kim, M. H., additional, Kim, Y. D., additional, Lee, H. C., additional, Ahn, M. S., additional, Hong, T. J., additional, Blanco, R., additional, Blanco, F., additional, Szarfer, J., additional, Garcia Escudero, A., additional, Gigena, G., additional, Gagliardi, J., additional, Rodriguez, A., additional, Sarmiento, R., additional, Affatatto, S., additional, Riccitelli, M., additional, Petris, A., additional, Datcu, M. D., additional, Pop, C., additional, Radoi, M., additional, Arsenescu-Georgescu, C., additional, Petrescu, I., additional, Petrescu, L., additional, Serban, L., additional, Nechita, E., additional, Tatu-Chitoiu, G., additional, Dorobantu, M., additional, Benedek, I., additional, Craiu, E., additional, Sinescu, C., additional, Ionescu, D. D., additional, Ginghina, C., additional, Minescu, B., additional, Izzo, A., additional, Mantovani, P., additional, Tomasi, L., additional, Dall'oglio, L., additional, Bonatti, S., additional, Rosiello, R., additional, Romano, M., additional, Agostini, F., additional, Zanini, R., additional, Zhao, Z. Y., additional, Wu, Y. J., additional, Li, J. J., additional, Yany, Y. J., additional, Qian, H. Y., additional, Tang, Y. D., additional, Timoteo, A. T., additional, Toste, A., additional, Lousinha, A., additional, Ramos, R., additional, Oliveira, J. A., additional, Ferreira, M. L., additional, Ferreira, R. C., additional, Cabades, C., additional, Diez Gil, J. L., additional, Aguar, P., additional, Sanmiguel, D., additional, Lopez-March, A., additional, Marmol, R., additional, Guerra, L., additional, Girbes, V., additional, Ferrando, J., additional, Rincon De Arellano, A., additional, Patricio, L., additional, Blondal, M., additional, Ainla, T., additional, Marandi, T., additional, Eha, J., additional, Oliveira, M. M., additional, Silva, M. N., additional, Cunha, P. S., additional, Feliciano, J., additional, Silva, S., additional, Kanovsky, J., additional, Kala, P., additional, Parenica, J., additional, Poloczek, M., additional, Prymusova, K., additional, Kubkova, L., additional, Spinar, J., additional, Olinic, D., additional, Homorodean, C., additional, Ober, M., additional, Olinic, M., additional, Andrioaia, C., additional, Condac, A., additional, Masmoudi, M., additional, Berdaoui, B., additional, Labidi, S., additional, Tapia Ballesteros, C., additional, Hernandez Luis, C., additional, Sandin, M. G., additional, Vegas, J. M., additional, Andion, R., additional, Martinez, N., additional, Gonzalez, I. A., additional, Alvarado, M., additional, Amat, I. J., additional, San Roman, J. A., additional, Garcia Gonzalez, M. J., additional, Arroyo Ucar, E., additional, Hernandez Garcia, C., additional, Dorta Martin, M., additional, Marrero Rodriguez, F., additional, Dragu, R., additional, Kapeliovich, M., additional, Hammerman, H., additional, Silva, D., additional, Cortez-Dias, N., additional, Jorge, C., additional, Silva Marques, J., additional, Carilho Ferreira, P., additional, Robalo Martins, S., additional, Almeida Ribeiro, M., additional, Calisto, C., additional, Fiuza, M., additional, Lopes, M. G., additional, Milicevic, P., additional, Panic, M., additional, Stankovic, I., additional, Milicevic, D., additional, Kalezic, T., additional, Kafedzic, S., additional, Ilic, I., additional, Cerovic, M., additional, Putnikovic, B., additional, Neskovic, A., additional, Rott, D., additional, Leibowitz, D., additional, Monhart, Z., additional, Reissigova, J., additional, Grunfeldova, H., additional, Jansky, P., additional, Valente, B., additional, Villanueva Benito, I., additional, Solla, I., additional, Paredes, E., additional, Diaz Castro, O., additional, Calvo, F., additional, Baz, J. A., additional, Iniguez, A., additional, Aleksova, A., additional, Gerloni, R., additional, Belfiore, R., additional, Carriere, C., additional, Barbati, G., additional, Fabris, E., additional, Possa, F., additional, Nait, D., additional, Milo, M., additional, Sinagra, G., additional, Marques, N., additional, Mimoso, J., additional, Gomes, V., additional, Agra Bermejo, R. M., additional, Emad Abu Assi, E. A. A., additional, Sergio Raposeiras Roubin, S. R. R., additional, Pilar Cabanas Grandio, P. C. G., additional, Carlos Pena Gil, C. P. G., additional, Jose Maria Garcia Acuna, J. M. G. A., additional, Jose Ramon Gonzalez Juanatey, J. R. G. J., additional, Daly, M. J., additional, Scott, P., additional, Owens, C. G., additional, Tomlin, A., additional, Smith, B., additional, Adgey, A. A. J., additional, Alvarez-Contreras, L. R., additional, Juarez, U., additional, Altamirano, A., additional, Arias, A., additional, Alvarez-San Gabriel, A., additional, Gonzalez-Pacheco, H., additional, Martinez-Sanchez, C., additional, Rahnavardi, M., additional, Keshtkar-Jahromi, M., additional, Vakili, H., additional, Gholamin, S., additional, Razavi, S. M., additional, Gilis-Januszewski, T., additional, Mellwig, K.- P., additional, Wiemer, M., additional, Gilis-Januszewski, J., additional, Peterschroeder, A., additional, Koerfer, J., additional, Horstkotte, D., additional, Vrsalovic, M., additional, Getaldic, B., additional, Vrkic, N., additional, Pintaric, H., additional, Khan, S., additional, Wasan, B., additional, Moretti, L., additional, Grossi, P., additional, Silenzi, S., additional, Testa, M., additional, Candelori, L., additional, Clementi, L. N., additional, Forlini, M., additional, Lando, L., additional, Pezzuoli, M. L., additional, Corradetti, P., additional, Leurent, G., additional, Pennec, P. Y., additional, Filippi, E., additional, Moquet, B., additional, Hacot, J. P., additional, Druelles, P., additional, Rialan, A., additional, Rouault, G., additional, Coudert, I., additional, Le Breton, H., additional, Gevaert, S., additional, Tromp, F., additional, Vandecasteele, E., additional, De Somer, F., additional, Van Belleghem, Y., additional, Bouchez, S., additional, Martens, F., additional, Herck, I., additional, De Pauw, M., additional, Ludka, O., additional, Sepsi, M., additional, Miklik, R., additional, Dusek, L., additional, Tomcikova, D., additional, Garcia-Acuna, J. M., additional, Aguiar-Souto, P., additional, Raposeiras Roubin, S., additional, Agra-Bermejo, R., additional, Jacquet, M., additional, Abu-Assi, E., additional, Gonzalez-Juanatey, J. R., additional, Ibatov, A., additional, Labrova, R., additional, Karlik, R., additional, Lokaj, P., additional, She, Q., additional, Deng, S. B., additional, Huang, S. H., additional, Gu, L. J., additional, Rong, J. I. A. N., additional, Wu, Z. K., additional, Li, Y., additional, Zhang, J., additional, Parascan, L., additional, Campanile, A., additional, Spinelli, L., additional, Santulli, G., additional, Ciccarelli, M., additional, De Gennaro, S., additional, Assante Di Panzillo, E., additional, Trimarco, B., additional, Iaccarino, G., additional, Bobescu, E., additional, Datcu, G., additional, Dobreanu, D., additional, Doka, B., additional, Charniot, J.- C., additional, Cosson, C., additional, Albertini, J. P., additional, Bittar, R., additional, Giral, P., additional, Cherfils, C., additional, Guillerm, E., additional, Bonnefont-Rousselot, D., additional, Rusali, A., additional, Cojocaru, L., additional, Parepa, I., additional, Koizumi, T., additional, Iida, S., additional, Sato, J., additional, Kikutani, T., additional, Muramatsu, T., additional, Nishimura, S., additional, Komiyama, N., additional, Lee, W. P., additional, Ong, B. B., additional, Haralambos, K., additional, Townsend, D., additional, Rees, J. A. E., additional, Williams, E. J., additional, Halcox, J. P., additional, Mcdowell, I., additional, Damjanovic, M., additional, Koracevic, G., additional, Djordjevic-Radojkovic, D., additional, Pavlovic, M., additional, Krstic, N., additional, Ciric-Zdravkovic, S., additional, Stojkovic, A., additional, Perisic, Z., additional, Apostolovic, S., additional, Faustino, A., additional, Seca, L., additional, Barra, S., additional, Caetano, F., additional, Providencia, R., additional, Silva, J., additional, Gomes, P., additional, Costa, G., additional, Costa, M., additional, Leitao-Marques, A., additional, Volkova, A. L., additional, Arutyunov, G. P., additional, Bylova, N. A., additional, Dayter, I. I., additional, Jao, Y. T. F. N., additional, Fang, C. C., additional, Chen, Y., additional, Yu, C. L., additional, Wang, S. P., additional, Valencia, J., additional, Perez-Berbel, P., additional, Ruiz-Nodar, J. M., additional, Pineda, J., additional, Bordes, P., additional, Quintanilla, M., additional, Mainar, V., additional, Sogorb, F., additional, Santos, N., additional, Serrao, M., additional, Cafe, H., additional, Silva, B., additional, Oliveira, R., additional, Caires, G., additional, Drumond, A., additional, Araujo, J., additional, Providencia, R. A., additional, Gomes, P. L., additional, Pais, J. R., additional, Mota, P., additional, Leitao-Marques, A. M., additional, Farhan, S., additional, Jarai, R., additional, Tentzeris, I., additional, Vogel, B., additional, Freynhofer, M. K., additional, Wojta, J., additional, Huber, K., additional, Poli, M., additional, Trambaiolo, P., additional, Corsi, F., additional, De Luca, M., additional, Mustilli, M., additional, Lukic, V., additional, Simonetti, M., additional, Ferraiuolo, G., additional, Lettino, M., additional, Casella, G., additional, Conte, M. R., additional, De Luca, L., additional, Geraci, G., additional, Ceravolo, R., additional, Pani, A., additional, Fradella, G., additional, Schratter, A., additional, Thiele, H., additional, Klemm, T., additional, Demmin, K., additional, Lehmann, D., additional, Mende, M., additional, Schuler, G., additional, Pittl, U., additional, Chernova, A., additional, Nikulina, S. U., additional, Naruke, T., additional, Inomata, T., additional, Yanagisawa, T., additional, Maekawa, E., additional, Mizutani, T., additional, Shinagawa, H., additional, Nishii, M., additional, Takeuchi, I., additional, Takehana, H., additional, Izumi, T., additional, Paulo, C., additional, Mascarenhas, J., additional, Patacho, M., additional, Pimenta, J., additional, Bettencourt, P., additional, Nardai, S., additional, Szabo, G. Y., additional, Berta, B., additional, Edes, I., additional, Merkely, B., additional, Delgado Silva, J., additional, Baptista, R., additional, Faria, R., additional, Trigo, J., additional, Gago, P., additional, Gheorghe, G., additional, Nanea, I. T., additional, Cristea, A., additional, Almarichi, S., additional, Martins, H., additional, Saraiva, F., additional, Jorge, E., additional, Mendes, P. L., additional, Monteiro, P., additional, Costa, S., additional, Franco, F., additional, Providencia, L. A., additional, Nanea, T., additional, Gheorghe, G. S., additional, Visan, S., additional, Paun, N., additional, Gaber, R., additional, Delewi, R., additional, Nijveldt, R., additional, De Bruin, H. A., additional, Hirsch, A., additional, Van Der Laan, A., additional, Bouma, B. J., additional, Tijssen, J. P. G., additional, Van Rossum, A. C., additional, Zijlstra, F., additional, Piek, J. J., additional, Rus, H., additional, Donea, M., additional, Ciurea, C., additional, Ifteni, G., additional, Casolo, G., additional, Chioccioli, M., additional, Magnacca, M., additional, Del Meglio, J., additional, Comella, A., additional, Baratto, M., additional, Lera, J., additional, Salvadori, L., additional, Tessa, C., additional, Vignali, C., additional, Keca, Z., additional, Momcilov Popin, T., additional, Panic, G., additional, White, R., additional, Mateen, F., additional, Weaver, A., additional, Agmon, Y., additional, Okisheva, E., additional, Tsaregorodtsev, D., additional, Sulimov, V., additional, Amat Santos, I. J., additional, Hernandez, C., additional, Tapia, C., additional, Campo, A., additional, Fredman, D., additional, Svensson, L., additional, Rosenqvist, M., additional, Tadel-Kocjancic, S., additional, Radsel, P., additional, Knafelj, R., additional, Gorjup, V., additional, Noc, M., additional, Zima, E., additional, Jenei, Z. S., additional, Kovacs, E., additional, Osztheimer, I., additional, Molnar, L., additional, Horvath, A., additional, Becker, D., additional, Geller, L., additional, Maggi, R., additional, Furukawa, T., additional, Viscardi, V., additional, Brignole, M., additional, Leal, S. R. N., additional, Dores, H., additional, Rosario, I., additional, Monge, J., additional, Carvalho, M. J., additional, Arroja, I., additional, Leitao, A., additional, Fonseca, C., additional, Aleixo, A., additional, Silva, A., additional, Keuleers, S., additional, Herijgers, P., additional, Herregods, M. C., additional, Budts, W., additional, Dubois, C., additional, Meuris, B., additional, Verhamme, P., additional, Flameng, W., additional, Van De Werf, F., additional, Adriaenssens, T., additional, Badran, H., additional, Elnoamany, M., additional, Lolah, T., additional, Olariu, C., additional, Macarie, C., additional, Mollik, M. A. H., additional, Hassan, A. I., additional, Paul, T. K., additional, Haque, M. Z., additional, Jahan, R., additional, Rahmatullah, M., additional, Khatun, M. A., additional, Rahman, M. T., additional, Chowdhury, M. H., additional, Bustamante Munguira, J., additional, Tamayo, E., additional, Garcia-Cuenca, I., additional, Bustamante, E., additional, Gualis, J., additional, Gomez-Martinez, M. L., additional, Florez, S., additional, Gomez-Herreras, J. I., additional, Ramirez Rodriguez, R., additional, Ramirez Rodriguez, A. M., additional, Garcia-Bello, M. A., additional, Hernadez Ortega, E., additional, Caballero Dorta, E., additional, Garcia Quintana, A., additional, Piro Mastraccio, V., additional, Medina Fernandez Aceytuno, A., additional, Assanelli, E., additional, De Metrio, M., additional, Rubino, M., additional, Lauri, G., additional, Cabiati, A., additional, Campodonico, J., additional, Grazi, M., additional, Moltrasio, M., additional, Marana, I., additional, Marenzi, G., additional, Lovlien, M., additional, Schei, B., additional, Picon-Heras, R., additional, Acebal, C., additional, Garcia Rubira, J. C., additional, Vivas Balcones, D., additional, Nunez-Gil, I., additional, Ruiz-Mateos, B., additional, Ibanez, B., additional, Fernandez-Ortiz, A., additional, Vintila, V. D., additional, Enescu, O. A., additional, Stoicescu, C. I., additional, Udroiu, C., additional, Cinteza, M., additional, Tatu - Chitoiu, G., additional, Vinereanu, D., additional, Fresco, C., additional, De Biasio, M., additional, Muser, D., additional, Sappa, R., additional, Morocutti, G., additional, Bernardi, G., additional, Proclemer, A., additional, Fontanella, B., additional, Affatato, A., additional, Ciccarese, C., additional, Sacchini, M., additional, Volpini, M., additional, Bianchetti, F., additional, Verzura, G., additional, Dei Cas, L., additional, Pudil, R., additional, Blaha, V., additional, Vojacek, J., additional, Paraskevaidis, I., additional, Ikonomidis, I., additional, Parissis, J., additional, Papadopoulos, C., additional, Stasinos, V., additional, Bistola, V., additional, Anastasiou-Nana, M., additional, Shochat, M., additional, Shotan, A., additional, Kazatsker, M., additional, Gurovich, V., additional, Asif, A., additional, Noiman, E., additional, Levy, Y., additional, Blondhaim, D., additional, Rabinovich, P., additional, Meisel, S., additional, Petrovic, S., additional, Glasnovic, J., additional, Tomasevic, M., additional, Sakac, D., additional, Obradovic, S., additional, Londono Sanchez, O., additional, Pacreu, S., additional, Torres, L., additional, Mihaylov, G., additional, Shaban, G. M., additional, Trendafilova, E., additional, Krasteva, V., additional, Mudrov, T. S., additional, Didon, J. P., additional, Panageas, V., additional, Vlachos, N., additional, Pernat, A., additional, Radan, I., additional, Mozina, H., additional, Pepi, P., additional, Cionini, F., additional, Baccaglioni, N., additional, Viertel, A., additional, Havers, J., additional, Ballard, G., additional, Groenefeld, G., additional, Branco, L. M., additional, Ferreira, L., additional, Fiarresga, A., additional, Lettieri, L., additional, Reggiani, A., additional, Juarez Prera, R., additional, Blanco Palacios, G., additional, Martin, A.- C., additional, Manzo Silberman, S., additional, Chaib, A., additional, Varenne, O., additional, Allouch, P., additional, Salengro, E., additional, Jegou, A., additional, Margot, O., additional, Spaulding, C., additional, Diego, A., additional, De Miguel, A., additional, Cuellas, C., additional, Fraile, E., additional, Martin, J., additional, Vega, B., additional, Bangueses, R., additional, Fernandez-Vazquez, F., additional, Perez De Prado, A., additional, Leal, S., additional, Correia, M. J., additional, Monge, J. C., additional, Abecasis, J., additional, Garcia-Garcia, C., additional, Subirana, I., additional, Sala, J., additional, Bruguera, J., additional, Valle, V., additional, Sanz, G., additional, Fiol, M., additional, Aros, F., additional, Marrugat, J., additional, Elosua, R., additional, Barra, S. N. C., additional, Leitao Marques, A., additional, Yang, Y. J., additional, Xu, B., additional, Song, G. Y., additional, G, R. L., additional, Aleksic, A., additional, Serpytis, P., additional, Rucinskas, K., additional, Kalinauskas, A., additional, Karvelyte, N., additional, Santos De Sousa, C. I., additional, Ferreira, S., additional, Calaca, J., additional, Lousada, N., additional, Palma Reis, R., additional, Gualandro, D. M., additional, Seguro, L. F. B. C., additional, Braga, F. G. M., additional, Silvestre, O. M., additional, Lage, R. L., additional, Fabri, J., additional, Oliveira, M. T., additional, Urbano Moral, J. A., additional, Torres Llergo, J., additional, Solanilla Rodriguez, R., additional, Sanchez Gonzalez, A., additional, Martinez Martinez, A., additional, Den Uil, C. A., additional, Lagrand, W. K., additional, Van Der Ent, M., additional, Jewbali, L. S. D., additional, Cheng, J. M., additional, Spronk, P. E., additional, Simoons, M. L., additional, Mornos, C., additional, Dragulescu, D., additional, Ionac, A., additional, Guardado, J., additional, Azevedo, O., additional, Fernandes, M., additional, Canario-Almeida, F., additional, Sanfins, V., additional, Pereira, A., additional, Almeida, J., additional, Kaplunova, V. U., additional, Belenkov, Y. N., additional, Privalova, E. V., additional, Fomin, A. A., additional, Suvorov, A. Y., additional, Goodkova, A., additional, Rubakova, M. G., additional, Kuznetsova, I. A., additional, Semernin, E. N., additional, Keshavarzi, F., additional, Kojuri, J., additional, Mikhailov, V. M., additional, Vezhenkova, I. V., additional, Goodkova, A. Y. A., additional, Pavlovic, I., additional, Schwarz, M., additional, Jakl, G., additional, Smetana, P., additional, Perkmann, T., additional, Mayr, A., additional, Mair, J., additional, Klug, G., additional, Schocke, M., additional, Trieb, T., additional, Jaschke, W., additional, Pachinger, O., additional, Metzler, B., additional, Bronze Carvalho, L., additional, Azevedo, J., additional, Andrade, M. L., additional, Relvas, M. J., additional, Coucello, J., additional, Morais, G., additional, Seabra, M., additional, Afamefule, F., additional, Luaces Mendez, M., additional, Teijeiro-Mestre, R., additional, Nunez-Gil, I. J., additional, Leco-Gil, N., additional, Madronal-Cerezo, E., additional, Zannin, I., additional, Ruiz, J., additional, Orynchak, M. A., additional, Vakalyuk, I. I., additional, Vakalyuk, I. P., additional, Berezin, A., additional, Panasenko, T., additional, Cavusoglu, Y., additional, Cavusoglu, A., additional, Unluoglu, I., additional, Tek, M., additional, Demirustu, C., additional, Gorenek, B., additional, Unalacak, M., additional, Birdane, A., additional, Yuksel, F., additional, Ata, N., additional, Halcox, J. P. J., additional, Beyaztas, A., additional, Entok, E., additional, Uslu, I., additional, Schaefer, A., additional, Flierl, U., additional, Seydelmann, N., additional, Bauersachs, J., additional, Calmac, L., additional, Marinescu, S., additional, Tatu Chitoiu, G., additional, Fruntelata, A. G., additional, Hamdi, S., additional, Maazoun, Y., additional, Neji, A., additional, Farhat, O., additional, Majdoub, M., additional, Ben Hamda, K., additional, Maatouk, F., additional, Balanescu, S. M., additional, Nedelciuc, I., additional, Deleanu, D., additional, Ortan, F., additional, Mot, S., additional, Sinnaeve, P. R., additional, Moreels, S., additional, Coosemans, M., additional, Vydt, T., additional, Desmet, W., additional, Tobing, D., additional, Rifnaldi, R., additional, Juzar, D., additional, Firdaus, I., additional, Dharma, S., additional, Irmalita, I., additional, Kalim, H., additional, Bejiqi, R., additional, Retkoceri, R., additional, Bejiqi, H., additional, Kryeziu, L., additional, Kelmendi, M., additional, Borovci, S. H., additional, Victor, S. M., additional, Gnanaraj, A., additional, Deshmukh, R., additional, Mullasari, A. S., additional, Yahalom, M., additional, Kaiyal, R. S., additional, Roguin, N., additional, Bornstein, J., additional, Atar, S., additional, Farah, R., additional, Seca, L. F., additional, Leitao Marques, A. M., additional, Margato, R., additional, Sousa, P., additional, Ribeiro, H., additional, Rocha, L., additional, Correia, A., additional, Moreira, J. I., additional, Carvalho, H. 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A., additional, Adgey, J. A. A., additional, Caeiro Pereira, D., additional, Braga, P., additional, Fontes Carvalho, R., additional, Rodrigues, A., additional, Goncalves, M., additional, Simoes, L., additional, and Borisov, K. V., additional

Published
2010
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11. X-ray structure of the N-terminus RRM domain of Set1

Author

Tresaugues, L., primary, Dehe, P.M., additional, Guerois, R., additional, Rodriguez-Gil, A., additional, Varlet, I., additional, Salah, P., additional, Pamblanco, M., additional, Luciano, P., additional, Quevillon-Cheruel, S., additional, Sollier, J., additional, Leulliot, N., additional, Couprie, J., additional, Tordera, V., additional, Zinn-Justin, S., additional, Chavez, S., additional, Van Tilbeurgh, H., additional, and Geli, V., additional

Published
2007
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15. HAT1 and HAT2 proteins are components of a yeast nuclear histone acetyltransferase enzyme specific for free histone H4.

Author

Ruiz-García, A B, Sendra, R, Galiana, M, Pamblanco, M, Pérez-Ortín, J E, and Tordera, V

Abstract

We have analyzed the histone acetyltransferase enzymes obtained from a series of yeast hat1, hat2, and gcn5 single mutants and hat1,hat2 and hat1,gcn5 double mutants. Extracts prepared from both hat1 and hat2 mutant strains specifically lack the following two histone acetyltransferase activities: the well known cytoplasmic type B enzyme and a free histone H4-specific histone acetyltransferase located in the nucleus. The catalytic subunits of both cytoplasmic and nuclear enzymes have identical molecular masses (42 kDa), the same as that of HAT1. However, the cytoplasmic complex has a molecular mass (150 kDa) greater than that of the nuclear complex (110 kDa). The possible functions of HAT1 and HAT2 in the yeast nucleus are discussed. In addition, we have detected a yeast histone acetyltransferase not previously described, designated HAT-A4. This enzyme is located in the nucleus and is able to acetylate free and nucleosome-bound histones H3 and H4. Finally, we show that the hat1, gcn5 double mutant is viable and does not exhibit a new phenotype, thus suggesting the existence of several histone acetyltransferases with overlapping functions.

Published
1998

16. Yeast contains multiple forms of histone acetyltransferase

Author

López-Rodas, G, Tordera, V, Sánchez del Pino, M M, and Franco, L

Abstract

We have assayed several methods to quantitatively recover yeast histone acetyltransferases in an attempt to study the multiplicity of enzymatic activities. Two methods, namely (NH4)2SO4 precipitation and salt dissociation of chromatin in 0.5 M NaCl, yielded convenient preparations of total histone acetyltransferases. DEAE-Sepharose chromatography of the crude extracts resulted in the separation of three peaks of activity when total yeast histones were used as substrate. However, the scanning of the enzymatic activity toward individual histones along the chromatography, achieved by determining the specific activity of the individual histones after incubating whole histones and [14C]acetyl-CoA with the chromatographic fractions, yielded four peaks. The first two peaks showed specificity toward H2B and H3, respectively. Although they partially overlapped, rechromatography on cation exchangers allowed us to resolve the two activities, and several criteria were used to prove that they correspond to different enzyme molecules. The last two peaks were H4-specific, but the present data suggest that one of the activities is chromatin-bound, whereas the other surely corresponds to the cytoplasmic B-form of the enzyme. The enzyme specific for yeast H2B acetylates chicken erythrocyte H2A, rather than H2B. The detected multiplicity of yeast histone acetyltransferases may correspond to the multiplicity of roles proposed for histone acetylation.

Published
1989
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22. Favourable mid-term clinical and echocardiographical follow-up of patients with transient left ventricular apical ballooning

Author

Tatjer Hernanz, I., Gonzalez Costello, J., Torrens Oses, A., Maristany Daunert, J., Ariza Sole, A., Lorente Tordera, V., and Esplugas Oliveras, E.

Subjects
ECHOCARDIOGRAPHY, TAKOTSUBO cardiomyopathy
Abstract

An abstract of the article "Favourable mid-term clinical and echocardiographical follow-up of patients with transient left ventricular apical ballooning," by I. Tatjer Hernanz and collagues is presented.

Published
2008
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23. Compassionate use of esketamine intranasal in patients with severe major depressive disorder resistant to the treatment.

Author

Gutiérrez-Rojas L, Vendrell-Serres J, Ramos-Quiroga JA, Etxeandia-Pradera JI, Aguilar E, De Santiago-Díaz AI, Hernández-Huerta D, Tordera V, Vázquez-Ventoso C, Bolívar M, Abril A, Catalán-Barragán R, and García-Jiménez J

Subjects
Humans, Male, Female, Retrospective Studies, Middle Aged, Adult, Treatment Outcome, Psychiatric Status Rating Scales, Severity of Illness Index, Ketamine administration & dosage, Ketamine adverse effects, Administration, Intranasal, Depressive Disorder, Treatment-Resistant drug therapy, Depressive Disorder, Major drug therapy, Antidepressive Agents administration & dosage, Antidepressive Agents adverse effects, Compassionate Use Trials
Abstract

Background: Treatment-resistant depression (TRD) is defined as the failure of at least two antidepressants in adequate doses and timing during a major depressive episode. Esketamine intranasal (ESK-IN) has been approved by the Food and Drug Administration and the European Medicines Agency for the treatment of TRD in combination with other antidepressants., Aims: To assess the effectiveness and tolerability of a sample of TRD patients who received treatment with ESK-IN as part of the compassionate use program., Methods: A retrospective, observational study was carried out on patients with a diagnosis of TRD enrolled in the early access program of ESK-IN in nine centers. Effectiveness was assessed with the Montgomery-Asberg depression rating scale (MADRS) at four time points: baseline, 28, 90, and 180 days of treatment., Results: The sample included 71 patients (70% women) with a mean baseline MADRS score of 38.27 ± 5.9 and total or partial work disability rates of 85%. ESK-IN treatment was associated with a statistically and clinically significant reduction in the severity of depressive symptoms at all time points assessed. The presence of side effects was common but the majority were mild in severity and resolved after the observation period. Those patients who received psychotherapy in combination with ESK-IN showed a significantly lower MADRS score at 90 and 180 days than those patients who did not undergo psychotherapy., Conclusion: ESK-IN has proven to be effective and safe in a clinical sample of patients with severe TRD. To optimize clinical outcomes, the pharmacological treatment for TRD should always be integrated into a comprehensive therapeutic plan that encompasses strategies such as psychotherapy, social support, and family interventions., Competing Interests: Declaration of conflicting interestsThe author(s) declared the following potential conflicts of interest with respect to the research, authorship, and/or publication of this article: LG-S has received consultancy and/or lecture honoraria from Lundbeck, Pfizer, Novartis, Janssen, Neuraxpharm, and Otsuka in the last 3 years, none of them with direct relation to this work. JIE-P has received consultancy and/or lecture honoraria from Janssen and Lundbeck. EA has received consultancy and/or lecture honoraria from Janssen, Lundbeck, Angelini, and Rovi. JV-S has received travel awards (air tickets + hotel) for taking part in annual psychiatric meetings from Lundbeck and Janssen-Cilag and was on the speakers’ bureau and acted as a consultant for Janssen Cilag. JARQ was on the speakers’ bureau and/or acted as a consultant for Janssen-Cilag, Novartis, Shire, Takeda, Bial, Shionogi, Sincrolab, Novartis, BMS, Medicine, Rubió, Uriach, Technofarma, and Raffo in the last 3 years. He also received travel awards (air tickets + hotel) for taking part in psychiatric meetings from Janssen-Cilag, Rubió, Shire, Takeda, Shionogi, Bial, and Medice. The Department of Psychiatry chaired by him received unrestricted educational and research support from the following companies in the last 3 years: Janssen-Cilag, Shire, Oryzon, Roche, Psious, and Rubió. AIDS-D has received consultancy and/or lecture honoraria from Janssen. DH-H has received consultancy and/or lecture honoraria from Janssen. VT has received consultancy and/or lecture honoraria from Janssen, Lundbeck, Angelini, Lilly, and Bial. CV-V has received consultancy and/or lecture honoraria from Janssen, Otsuka, Casen Recordati, Angelini, and Adamed. MB has received consultancy and/or lecture honoraria from Janssen, Lundbeck, Casen Recordati, Angelini, and Rovi. RC-B has received consultancy and/or lecture honoraria from Janssen, Lundbeck, and Otsuka. The rest of the authors declare they have no conflicts of interest.

Published
2025
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24. Nut1/Hos1 and Sas2/Rpd3 control the H3 acetylation of two different sets of osmotic stress-induced genes.

Author

Pérez-Martínez ME, Benet M, Alepuz P, and Tordera V

Subjects
Acetylation, DNA-Binding Proteins genetics, DNA-Binding Proteins metabolism, Epigenesis, Genetic, Histone Acetyltransferases genetics, Histone Code, Mediator Complex genetics, Mitogen-Activated Protein Kinases genetics, Mitogen-Activated Protein Kinases metabolism, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins genetics, Transcription Factors genetics, Transcription Factors metabolism, Gene Expression Regulation, Fungal, Histone Acetyltransferases metabolism, Histones metabolism, Mediator Complex metabolism, Osmotic Pressure, Protein Processing, Post-Translational, Saccharomyces cerevisiae Proteins metabolism
Abstract

Epigenetic information is able to interact with the cellular environment and could be especially useful for reprograming gene expression in response to a physiological perturbation. In fact the genes induced or repressed by osmotic stress undergo significant changes in terms of the levels of various histone modifications, especially in the acetylation levels of histone H3. Exposing yeast to high osmolarity results in the activation of stress-activated protein kinase Hog1, which plays a central role in gene expression control. We evaluated the connection between the presence of Hog1 and changes in histone H3 acetylation in stress-regulated genes. We found a parallel increase in the acetylation of lysines 9 and 14 of H3 in induced genes during stress, which was largely dependent on Hog1 at the genome-wide level. Conversely, we observed that acetylation decreased in repressed genes and was not dependent on Hog1. However, lack of Hog1 sometimes produced different, and even opposite, effects on the induction and acetylation of H3 of each gene. We also found that the acetylation state of lysine 9 of H3 was altered in the strains deficient in Nut1 HAT and Hos1 HDAC in the genes up-regulated during osmotic stress in an Msn2/Msn4-independent manner, while lysine 9 acetylation of H3 varied in the strains deficient in Sas2 HAT and Rpd3 HDAC for the Msn2/Msn4-dependent induced genes. The results presented here show new, unexpected participants in gene regulation processes in response to environmental perturbations.

Published
2020
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25. Homeostasis in the Central Dogma of molecular biology: the importance of mRNA instability.

Author

Pérez-Ortín JE, Tordera V, and Chávez S

Subjects
DNA metabolism, Escherichia coli genetics, Escherichia coli metabolism, Evolution, Molecular, Gene Expression Regulation, HeLa Cells, Humans, Proteins metabolism, Proteostasis genetics, RNA, Messenger metabolism, Saccharomyces cerevisiae genetics, Saccharomyces cerevisiae metabolism, Schizosaccharomyces genetics, Schizosaccharomyces metabolism, DNA genetics, Homeostasis genetics, Proteins genetics, RNA Stability, RNA, Messenger genetics, Transcription, Genetic
Abstract

Cell survival requires the control of biomolecule concentration, i.e. biomolecules should approach homeostasis. With information-carrying macromolecules, the particular concentration variation ranges depend on each type: DNA is not buffered, but mRNA and protein concentrations are homeostatically controlled, which leads to the ribostasis and proteostasis concepts. In recent years, we have studied the particular features of mRNA ribostasis and proteostasis in the model organism S. cerevisiae . Here we extend this study by comparing published data from three other model organisms: E. coli, S. pombe and cultured human cells. We describe how mRNA ribostasis is less strict than proteostasis. A constant ratio appears between the average decay and dilution rates during cell growth for mRNA, but not for proteins. We postulate that this is due to a trade-off between the cost of synthesis and the response capacity. This compromise takes place at the transcription level, but is not possible at the translation level as the high stability of proteins, versus that of mRNAs, precludes it. We hypothesize that the middle-place role of mRNA in the Central Dogma of Molecular Biology and its chemical instability make it more suitable than proteins for the fast changes needed for gene regulation.

Published
2019
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27. Modulation of protein synthesis and degradation maintains proteostasis during yeast growth at different temperatures.

Author

Benet M, Miguel A, Carrasco F, Li T, Planells J, Alepuz P, Tordera V, and Pérez-Ortín JE

Subjects
Homeostasis genetics, RNA, Messenger genetics, Ribosomes genetics, Saccharomyces cerevisiae Proteins genetics, Temperature, Transcription, Genetic genetics, Gene Expression Regulation, Fungal genetics, Protein Biosynthesis genetics, RNA Stability genetics, Saccharomyces cerevisiae genetics
Abstract

To understand how cells regulate each step in the flow of gene expression is one of the most fundamental goals in molecular biology. In this work, we have investigated several protein turnover-related steps in the context of gene expression regulation in response to changes in external temperature in model yeast Saccharomyces cerevisiae. We have found that the regulation of protein homeostasis is stricter than mRNA homeostasis. Although global translation and protein degradation rates are found to increase with temperature, the increase of the catalytic activity of ribosomes is higher than the global translation rate suggesting that yeast cells adapt the amount of translational machinery to the constraints imposed by kinetics in order to minimize energy costs. Even though the transcriptional machinery is subjected to the same constraints, we observed interesting differences between transcription and translation, which may be related to the different energy costs of the two processes as well as the differential functions of mRNAs and proteins., (Copyright © 2017 Elsevier B.V. All rights reserved.)

Published
2017
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28. Early prognostic evaluation after mild therapeutic hypothermia in sudden cardiac arrest survivors.

Author

Sánchez-Salado JC, Ariza-Solé A, Lorente-Tordera V, Sánchez-Prieto R, Muntané-Carol G, and Cequier-Fillat À

Subjects
Female, Humans, Male, Middle Aged, Out-of-Hospital Cardiac Arrest mortality, Prognosis, Retrospective Studies, Spain epidemiology, Survival Rate trends, Time Factors, Hypothermia, Induced methods, Out-of-Hospital Cardiac Arrest therapy, Survivors
Published
2015
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29. Comprehensive analysis of interacting proteins and genome-wide location studies of the Sas3-dependent NuA3 histone acetyltransferase complex.

Author

Vicente-Muñoz S, Romero P, Magraner-Pardo L, Martinez-Jimenez CP, Tordera V, and Pamblanco M

Abstract

Histone acetylation affects several aspects of gene regulation, from chromatin remodelling to gene expression, by modulating the interplay between chromatin and key transcriptional regulators. The exact molecular mechanism underlying acetylation patterns and crosstalk with other epigenetic modifications requires further investigation. In budding yeast, these epigenetic markers are produced partly by histone acetyltransferase enzymes, which act as multi-protein complexes. The Sas3-dependent NuA3 complex has received less attention than other histone acetyltransferases (HAT), such as Gcn5-dependent complexes. Here, we report our analysis of Sas3p-interacting proteins using tandem affinity purification (TAP), coupled with mass spectrometry. This analysis revealed Pdp3p, a recently described component of NuA3, to be one of the most abundant Sas3p-interacting proteins. The PDP3 gene, was TAP-tagged and protein complex purification confirmed that Pdp3p co-purified with the NuA3 protein complex, histones, and several transcription-related and chromatin remodelling proteins. Our results also revealed that the protein complexes associated with Sas3p presented HAT activity even in the absence of Gcn5p and vice versa. We also provide evidence that Sas3p cannot substitute Gcn5p in acetylation of lysine 9 in histone H3 in vivo. Genome-wide occupancy of Sas3p using ChIP-on-chip tiled microarrays showed that Sas3p was located preferentially within the 5'-half of the coding regions of target genes, indicating its probable involvement in the transcriptional elongation process. Hence, this work further characterises the function and regulation of the NuA3 complex by identifying novel post-translational modifications in Pdp3p, additional Pdp3p-co-purifying chromatin regulatory proteins involved in chromatin-modifying complex dynamics and gene regulation, and a subset of genes whose transcriptional elongation is controlled by this complex.

Published
2014
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30. Dynamic remodeling of histone modifications in response to osmotic stress in Saccharomyces cerevisiae.

Author

Magraner-Pardo L, Pelechano V, Coloma MD, and Tordera V

Subjects
Acetylation, Gene Expression Regulation, Fungal, Genome, Fungal, Methylation, Multigene Family, RNA Polymerase II metabolism, RNA, Messenger genetics, Transcription, Genetic, Transcriptional Activation, Chromatin Assembly and Disassembly, Histones metabolism, Osmotic Pressure, Saccharomyces cerevisiae genetics, Saccharomyces cerevisiae metabolism, Stress, Physiological genetics
Abstract

Background: Specific histone modifications play important roles in chromatin functions; i.e., activation or repression of gene transcription. This participation must occur as a dynamic process. Nevertheless, most of the histone modification maps reported to date provide only static pictures that link certain modifications with active or silenced states. This study, however, focuses on the global histone modification variation that occurs in response to the transcriptional reprogramming produced by a physiological perturbation in yeast., Results: We did a genome-wide chromatin immunoprecipitation analysis for eight specific histone modifications before and after saline stress. The most striking change was rapid acetylation loss in lysines 9 and 14 of H3 and in lysine 8 of H4, associated with gene repression. The genes activated by saline stress increased the acetylation levels at these same sites, but this acetylation process was quantitatively minor if compared to that of the deacetylation of repressed genes. The changes in the tri-methylation of lysines 4, 36 and 79 of H3 and the di-methylation of lysine 79 of H3 were slighter than those of acetylation. Furthermore, we produced new genome-wide maps for seven histone modifications, and we analyzed, for the first time in S. cerevisiae, the genome-wide profile of acetylation of lysine 8 of H4., Conclusions: This research reveals that the short-term changes observed in the post-stress methylation of histones are much more moderate than those of acetylation, and that the dynamics of the acetylation state of histones during activation or repression of transcription is a much quicker process than methylation.

Published
2014
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32. Invasive mechanical ventilation in acute coronary syndromes in the era of percutaneous coronary intervention.

Author

Ariza Solé A, Salazar-Mendiguchía J, Lorente-Tordera V, Sánchez-Salado JC, González-Costello J, Moliner-Borja P, Gómez-Hospital JA, Manito-Lorite N, and Cequier-Fillat A

Subjects
Acute Coronary Syndrome mortality, Female, Heart Arrest therapy, Hospitalization, Humans, Male, Middle Aged, Myocardial Infarction mortality, Prospective Studies, Pulmonary Edema therapy, Respiration, Artificial mortality, Shock therapy, Treatment Outcome, Acute Coronary Syndrome therapy, Myocardial Infarction therapy, Percutaneous Coronary Intervention methods, Respiration, Artificial methods
Abstract

Background: Percutaneous coronary intervention (PCI) improves prognosis in patients with acute coronary syndromes (ACS) reducing ischaemic complications and the development of heart failure, thus potentially changing invasive mechanical ventilation (IMV) requirements. Little information exists about patients with ACS requiring IMV in the current era. We aimed to analyze IMV requirements and characteristics of ACS patients treated under current recommendations (including a high rate of PCI)., Methods: Baseline characteristics, indications for IMV, management and in-hospital and mid-term clinical course were analyzed prospectively in a consecutive series of patients with ACS admitted to a tertiary care hospital., Results: We included 1821 patients, of which 106 (5.8%) required IMV. Mean follow-up was 347 days. PCI was performed in 84% of cases. Patients with IMV had more comorbidities, worse left ventricular function and more unstable hemodynamic parameters on admission. In-hospital mortality in patients requiring IMV was 29%. These patients also had higher mid-term mortality (hazard ratio (HR) 6.58; 95% confidence interval (CI) 4.49-9.64; p 0.001). The most common indication for IMV was cardiopulmonary arrest (CA) (65; 61%), followed by pulmonary oedema (27; 26%) and shock (14; 13.2%). Patients with CA were younger, with better hemodynamic parameters at admission, more favourable coronary anatomy and higher rates of PCI. There were no significant differences in overall mortality between the three groups. The main cause of death in CA patients was persistent vegetative state., Conclusions: Mortality in patients with ACS requiring IMV remained high despite a high rate of PCI. Baseline characteristics, management and clinical course were different according to the reason for IMV. The most common cause for IMV requirement was CA.

Published
2013
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33. CRUSADE bleeding risk score validation for ST-segment-elevation myocardial infarction undergoing primary percutaneous coronary intervention.

Author

Ariza-Solé A, Sánchez-Elvira G, Sánchez-Salado JC, Lorente-Tordera V, Salazar-Mendiguchía J, Sánchez-Prieto R, Romaguera-Torres R, Ferreiro-Gutiérrez JL, Gómez-Hospital JA, and Cequier-Fillat A

Subjects
Anticoagulants administration & dosage, Blood Coagulation drug effects, Female, Humans, Logistic Models, Male, Middle Aged, Myocardial Infarction physiopathology, Percutaneous Coronary Intervention adverse effects, Prognosis, Prospective Studies, Risk Assessment, Risk Factors, Treatment Outcome, Venous Thromboembolism prevention & control, Venous Thrombosis prevention & control, Hemorrhage etiology, Myocardial Infarction blood, Percutaneous Coronary Intervention methods
Abstract

Introduction: The CRUSADE bleeding risk score (CBRS) accurately predicts major bleeding in non-ST segment elevation myocardial infarction NSTEMI patients. However, little information exists about its application in ST segment elevation myocardial infarction STEMI. We aimed to assess the ability of CBRS to predict in-hospital major bleeding in STEMI patients undergoing primary percutaneous coronary intervention (PPCI)., Materials and Methods: We prospectively analyzed consecutive STEMI patients undergoing PPCI. Baseline characteristics, in-hospital complications and mid term mortality were recorded. Major bleeding was defined by the CRUSADE definition. Predictive ability of the CBRS was assessed by logistic regression method and the area under the ROC curve (AUC)., Results: We included 1064 patients (mean age 63years). Mean CBRS value was 24. Most of patients (740/1064 (69.6%)) were in the two lowest risk quintiles of CBRS. Incidence of in-hospital major bleeding was 33/1064 (3.1%). The rates of in-hospital bleeding across the quintiles of risk groups were 0.4% (very low risk), 2.6% (low), 4.6% (moderate), 7.2% (high), and 13.4% (very high) (p 0.001). AUC was 0.80 (95% CI 0.73-0.87 p 0.001). In patients with radial access angiography (n=621) AUC was 0.81 (95% CI: 0.65-0.97). Mean follow up was 344days. Patients with bleeding events had higher mortality during follow up (HR 6.91; 95% CI 3.72-12.82; p 0.001)., Conclusions: Our patients had a significantly lower bleeding risk as compared to CRUSADE NSTEMI population. CBRS accurately predicted major in-hospital bleeding in this different clinical scenario, including patients with radial artery approach., (© 2013.)

Published
2013
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34. The Sas3p and Gcn5p histone acetyltransferases are recruited to similar genes.

Author

Rosaleny LE, Ruiz-García AB, García-Martínez J, Pérez-Ortín JE, and Tordera V

Subjects
Acetylation, Chromatin Immunoprecipitation, Gene Expression Regulation, Fungal, Histones metabolism, Histone Acetyltransferases metabolism, Saccharomyces cerevisiae genetics, Saccharomyces cerevisiae metabolism, Saccharomyces cerevisiae Proteins metabolism
Abstract

Background: Specific histone modifications can perform several cellular functions, for example, as signals to recruit trans-acting factors and as modulators of chromatin structure. Acetylation of Lys14 of histone H3 is the main target of many histone acetyltransferases in vitro and may play a central role in the stability of the nucleosome. This study is focused on the genome-wide binding of Saccharomyces cerevisiae histone acetyltransferases that are specific for Lys14 of histone H3., Results: We have used a variation of the genome-wide location analysis method, based on a macroarray platform, to identify binding sites of yeast histone acetyltransferase catalytic subunits and to correlate their positions with acetylation of Lys14 of histone H3. Our results revealed that the histone acetyltransferases Sas3p and Gcn5p are recruited to a pool of intensely transcribed genes and that there is considerable overlap between the two cohorts of Sas3p and Gcn5p bound gene pools. We also demonstrate a positive correlation between binding sites of both proteins and the acetylation state of Lys14 of histone H3. Finally, a positive correlation between the decrease of H3 Lys14 acetylation in a GCN5 deleted strain and the Gcn5p genome occupancy is shown., Conclusion: Our data support a model in which both Gcn5p and Sas3p act as general activators of an overlapping pool of intensely transcribed genes. Since both proteins preferentially acetylate Lys14 of histone H3, our data support the hypothesis that acetylation of this specific residue facilitates the action of the transcriptional apparatus.

Published
2007
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35. Protein interactions within the Set1 complex and their roles in the regulation of histone 3 lysine 4 methylation.

Author

Dehé PM, Dichtl B, Schaft D, Roguev A, Pamblanco M, Lebrun R, Rodríguez-Gil A, Mkandawire M, Landsberg K, Shevchenko A, Shevchenko A, Rosaleny LE, Tordera V, Chávez S, Stewart AF, and Géli V

Subjects
Gene Expression Regulation, Fungal, Histone-Lysine N-Methyltransferase, Histones chemistry, Methylation, Protein Binding, Protein Subunits, DNA-Binding Proteins metabolism, Histones metabolism, Lysine metabolism, Saccharomyces cerevisiae metabolism, Saccharomyces cerevisiae Proteins metabolism, Transcription Factors metabolism
Abstract

Set1 is the catalytic subunit and the central component of the evolutionarily conserved Set1 complex (Set1C) that methylates histone 3 lysine 4 (H3K4). Here we have determined protein/protein interactions within the complex and related the substructure to function. The loss of individual Set1C subunits differentially affects Set1 stability, complex integrity, global H3K4 methylation, and distribution of H3K4 methylation along active genes. The complex requires Set1, Swd1, and Swd3 for integrity, and Set1 amount is greatly reduced in the absence of the Swd1-Swd3 heterodimer. Bre2 and Sdc1 also form a heteromeric subunit, which requires the SET domain for interaction with the complex, and Sdc1 strongly interacts with itself. Inactivation of either Bre2 or Sdc1 has very similar effects. Neither is required for complex integrity, and their removal results in an increase of H3K4 mono- and dimethylation and a severe decrease of trimethylation at the 5' end of active coding regions but a decrease of H3K4 dimethylation at the 3' end of coding regions. Cells lacking Spp1 have a reduced amount of Set1 and retain a fraction of trimethylated H3K4, whereas cells lacking Shg1 show slightly elevated levels of both di- and trimethylation. Set1C associates with both serine 5- and serine 2-phosphorylated forms of polymerase II, indicating that the association persists to the 3' end of transcribed genes. Taken together, our results suggest that Set1C subunits stimulate Set1 catalytic activity all along active genes.

Published
2006
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36. Structural characterization of Set1 RNA recognition motifs and their role in histone H3 lysine 4 methylation.

Author

Trésaugues L, Dehé PM, Guérois R, Rodriguez-Gil A, Varlet I, Salah P, Pamblanco M, Luciano P, Quevillon-Cheruel S, Sollier J, Leulliot N, Couprie J, Tordera V, Zinn-Justin S, Chàvez S, van Tilbeurgh H, and Géli V

Subjects
Amino Acid Sequence, Conserved Sequence genetics, Histone-Lysine N-Methyltransferase, Methylation, Models, Molecular, Molecular Sequence Data, Protein Binding, Protein Structure, Quaternary, Protein Subunits metabolism, RNA, Fungal metabolism, Saccharomyces cerevisiae enzymology, Sequence Alignment, Structure-Activity Relationship, Surface Properties, DNA-Binding Proteins chemistry, DNA-Binding Proteins metabolism, Histones chemistry, Histones metabolism, Lysine metabolism, Saccharomyces cerevisiae Proteins chemistry, Saccharomyces cerevisiae Proteins metabolism, Transcription Factors chemistry, Transcription Factors metabolism
Abstract

The yeast Set1 histone H3 lysine 4 (H3K4) methyltransferase contains, in addition to its catalytic SET domain, a conserved RNA recognition motif (RRM1). We present here the crystal structure and the secondary structure assignment in solution of the Set1 RRM1. Although RRM1 has the expected betaalphabetabetaalphabeta RRM-fold, it lacks the typical RNA-binding features of these modules. RRM1 is not able to bind RNA by itself in vitro, but a construct combining RRM1 with a newly identified downstream RRM2 specifically binds RNA. In vivo, H3K4 methylation is not affected by a point mutation in RRM2 that preserves Set1 stability but affects RNA binding in vitro. In contrast mutating RRM1 destabilizes Set1 and leads to an increase of dimethylation of H3K4 at the 5'-coding region of active genes at the expense of trimethylation, whereas both, dimethylation decreases at the 3'-coding region. Taken together, our results suggest that Set1 RRMs bind RNA, but Set1 RNA-binding activity is not linked to H3K4 methylation.

Published
2006
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37. Histone H3 lysine 4 mono-methylation does not require ubiquitination of histone H2B.

Author

Dehé PM, Pamblanco M, Luciano P, Lebrun R, Moinier D, Sendra R, Verreault A, Tordera V, and Géli V

Subjects
Histones chemistry, Methylation, Saccharomyces cerevisiae metabolism, Histones metabolism, Lysine metabolism, Ubiquitin metabolism
Abstract

The yeast Set1-complex catalyzes histone H3 lysine 4 (H3K4) methylation. Using N-terminal Edman sequencing, we determined that 50% of H3K4 is methylated and consists of roughly equal amounts of mono, di and tri-methylated H3K4. We further show that loss of either Paf1 of the Paf1 elongation complex, or ubiquitination of histone H2B, has only a modest effect on bulk histone mono-methylation at H3K4. Despite the fact that Set1 recruitment decreases in paf1delta cells, loss of Paf1 results in an increase of H3K4 mono-methylation at the 5' coding region of active genes, suggesting a Paf1-independent targeting of Set1. In contrast to Paf1 inactivation, deleting RTF1 affects H3K4 mono-methylation at the 3' coding region of active genes and results in a decrease of global H3K4 mono-methylation. Our results indicate that the requirements for mono-methylation are distinct from those for H3K4 di and tri-methylation, and point to differences among members of the Paf1 complex in the regulation of H3K4 methylation.

Published
2005
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38. Yeast HAT1 and HAT2 deletions have different life-span and transcriptome phenotypes.

Author

Rosaleny LE, Antúnez O, Ruiz-García AB, Pérez-Ortín JE, and Tordera V

Subjects
Histone Acetyltransferases, Immunoprecipitation, Phenotype, Sirtuins metabolism, Telomere, Acetyltransferases genetics, Gene Deletion, Saccharomyces cerevisiae genetics, Saccharomyces cerevisiae Proteins genetics, Transcription, Genetic
Abstract

HAT-B is a yeast histone acetyltransferase composed of Hat1, Hat2 and Hif1 proteins. We demonstrate that a hat2 mutant or a hat1hat2 double mutant, but not a hat1 mutant, have an extended life-span. Transcriptome analysis shows that the single hat mutants are not very different from wild type. However, the comparison of the hat1 and hat2 transcriptomes shows that they are different. The hat1hat2 double mutant shows a transcriptional phenotype similar to that of the hat1 mutant but strongly enhanced. These results indicate that Hat2p could have additional functions in the cell to those of Hat1p.

Published
2005
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39. Hif1 is a component of yeast histone acetyltransferase B, a complex mainly localized in the nucleus.

Author

Poveda A, Pamblanco M, Tafrov S, Tordera V, Sternglanz R, and Sendra R

Subjects
Acetylation, Histone Acetyltransferases, Histones metabolism, Hypoxia-Inducible Factor 1, Saccharomyces cerevisiae metabolism, Telomere metabolism, Acetyltransferases metabolism, DNA-Binding Proteins metabolism, Nuclear Proteins metabolism, Saccharomyces cerevisiae Proteins metabolism, Transcription Factors
Abstract

Hat1 is the catalytic subunit of the only type B histone acetyltransferase known (HAT-B). The enzyme specifically acetylates lysine 12, and to a lesser extent lysine 5, of free, non-chromatin-bound histone H4. The complex is usually isolated with cytosolic fractions and is thought to be involved in chromatin assembly. The Saccharomyces cerevisiae HAT-B complex also contains Hat2, a protein stimulating Hat1 catalytic activity. We have now identified by two-hybrid experiments Hif1 as both a Hat1- and a histone H4-interacting protein. These interactions were dependent on HAT2, indicating a mediating role for Hat2. Biochemical fractionation and co-immunoprecipitation assays demonstrated that Hif1 is a component of a yeast heterotrimeric HAT-B complex, in which Hat2 bridges Hat1 and Hif1 proteins. In contrast to Hat2, this novel subunit does not appear to regulate Hat1 enzymatic activity. Nevertheless, similarly to Hat1, Hif1 influences telomeric silencing. In a localization analysis by immunofluorescence microscopy on yeast strains expressing tagged versions of Hat1, Hat2, and Hif1, we have found that all three HAT-B proteins are mainly localized in the nucleus. Thus, we propose that the distinction between A- and B-type enzymes should henceforth be based on their capacity to acetylate histones bound to nucleosomes and not on their location within the cell. Finally, by Western blotting assays, we have not detected differences in the in vivo acetylation of H4 lysine 12 (acK12H4) between wild-type and hat1Delta, hat2Delta, or hif1Delta mutant strains, suggesting that the level of HAT-B-dependent acK12H4 may be very low under normal growth conditions.

Published
2004
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40. Bromodomain factor 1 (Bdf1) protein interacts with histones.

Author

Pamblanco M, Poveda A, Sendra R, Rodríguez-Navarro S, Pérez-Ortín JE, and Tordera V

Subjects
Acetyltransferases, Fungal Proteins genetics, Fungal Proteins metabolism, Genes, Reporter, Histone Acetyltransferases, Peptide Fragments genetics, Peptide Fragments metabolism, Protein Binding physiology, Recombinant Fusion Proteins genetics, Recombinant Fusion Proteins metabolism, Saccharomyces, Transcription Factors genetics, Two-Hybrid System Techniques, Histones metabolism, Saccharomyces cerevisiae Proteins, Transcription Factors metabolism
Abstract

Using a yeast two-hybrid assay we detected an interaction between the N-terminal region of histone H4 (amino acids 1--59) and a fragment of the bromodomain factor 1 protein (Bdf1p) (amino acids 304--571) that includes one of the two bromodomains of this protein. No interaction was observed using fragments of histone H4 sequence smaller than the first 59 amino acids. Recombinant Bdf1p (rBdf1p) demonstrates binding affinity for histones H4 and H3 but not H2A and H2B in vitro. Moreover, rBdf1p is able to bind histones H3 and H4 having different degrees of acetylation. Finally, we have not detected histone acetyltransferase activity associated with Bdf1p.

Published
2001
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41. Gcn5p is involved in the acetylation of histone H3 in nucleosomes.

Author

Ruiz-García AB, Sendra R, Pamblanco M, and Tordera V

Subjects
Acetylation, Animals, Chickens, Erythrocytes metabolism, Histone Acetyltransferases, Molecular Weight, Saccharomyces cerevisiae metabolism, DNA-Binding Proteins, Fungal Proteins metabolism, Histones metabolism, Nucleosomes metabolism, Protein Kinases metabolism, Saccharomyces cerevisiae Proteins
Abstract

Enzymatic extracts from a gcn5 mutant and wild-type strains of Saccharomyces cerevisiae were chromatographically fractionated and the histone acetyltransferase activities compared. When free histones were used as substrate, extracts from wild-type cells showed two peaks of activity on histone H3 but extracts from gcn5 mutant cells showed only one. With nucleosomes as substrate, the histone acetyltransferase activities present in extracts from the gcn5 mutant strain were not able to modify H3 whereas wild-type cell extracts acetylated intensely this histone. The activity that acetylated nucleosome-bound H3 behaved as a 170-kDa complex. We suggest that Gcn5p represents a catalytic subunit within a multiprotein complex containing proteins that confer on it the ability to acetylate H3 in nucleosomes.

Published
1997
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42. Subcellular localization and nucleosome specificity of yeast histone acetyltransferases.

Author

López-Rodas G, Tordera V, Sánchez del Pino MM, and Franco L

Subjects
Amidohydrolases metabolism, Cell Nucleus enzymology, Chromatography, Ion Exchange, Histone Acetyltransferases, Histones metabolism, Substrate Specificity, Acetyltransferases metabolism, Nucleosomes enzymology, Saccharomyces cerevisiae enzymology, Saccharomyces cerevisiae Proteins
Abstract

We have previously reported [López-Rodas et al. (1989) J. Biol. Chem. 264, 19028-19033] that the yeast Saccharomyces cerevisiae contains four histone acetyltransferases, which can be resolved by ion-exchange chromatography, and their specificity toward yeast free histones was studied. In the present contribution we show that three of the enzymes are nuclear, type A histone acetyltransferases and they are able to acetylate nucleosome-bound histones. They differ in their histone specificity. Enzyme A1 acetylates H2A in chicken nucleosomes, although it is specific for yeast free H2B; histone acetyltransferase A2 is highly specific for H3, and histone acetyltransferase A3 preparations acetylate both H3 and H4 in nucleosomes. The fourth enzyme, which is located in the cytoplasm, does not accept nucleosomes as substrate, and it represents a canonical type B, H4-specific histone acetyltransferase. Finally, histone deacetylase activity is preferentially found in the nucleus.

Published
1991
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43. Isolation and Characterization of an Fe(III)-Chelating Compound Produced by Pseudomonas syringae.

Author

Torres L, Pérez-Ortín JE, Tordera V, and Beltrán JP

Abstract

The phytopathogenic bacterium Pseudomonas syringae produces a fluorescent pigment when it is grown in iron-deficient media. This pigment forms a very stable Fe(III) complex that was purified in this form by using a novel procedure based on ultrafiltration and column chromatography. The Fe(III) complex has a molecular weight of 1,100 and contains 1 mol of Fe(III). The pigment is composed of an amino acid moiety with three threonines, three serines, one lysine, delta-N-hydroxyornithine, and a quinoline-type fluorescent chromophore. These features and its stability constant (in the range of 10) suggest that the fluorescent pigment of P. syringae is related to the siderophores produced by another Pseudomonas species.

Published
1986
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44. Comparative study of the iron-binding properties of transferrins. Differences in the involvement of histidine residues as revealed by carbethoxylation.

Author

Mazurier J, Leger D, Tordera V, Montreuil J, and Spik G

Subjects
Animals, Binding Sites, Cattle, Chemical Phenomena, Chemistry, Chickens, Diethyl Pyrocarbonate, Humans, Kinetics, Protein Binding, Rabbits, Species Specificity, Histidine isolation & purification, Iron metabolism, Transferrin metabolism
Published
1981
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