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3. 1465P Clinical impact of proton pump inhibitor on the therapeutic outcome of non-small cell lung cancer patients with PD-L1 TPS ≥50% receiving pembrolizumab monotherapy versus immune checkpoint inhibitor plus chemotherapy: A retrospective multicenter cohort study

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Kawachi, H., Yamada, T., Tamiya, M., Negi, Y., Goto, Y., Nakao, A., Shiotsu, S., Tanimura, K., Takeda, T., Okada, A., Harada, T., Date, K., Chihara, Y., Hasegawa, I., Tamiya, N., Iwasaku, M., Tokuda, S., Kijima, T., and Takayama, K.

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2023
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4. Epidemiology and patterns of tracheostomy practice in patients with acute respiratory distress syndrome in ICUs across 50 countries

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Abe T., Madotto F., Pham T., Nagata I., Uchida M., Tamiya N., Kurahashi K., Bellani G., Laffey J. G, Francois GM, Rabboni F, Madotto F, Conti S, Laffey JG, Bellani G, Pham T, Fan E, Pesenti A, Brochard L, Esteban A, Gattinoni L, van Haren F, Larsson A, McAuley DF, Ranieri M, Rubenfeld G, Thompson BT, Wrigge H, Slutsky AS, Rios F, Sottiaux T, Depuydt P, Lora FS, Azevedo LC, Bugedo G, Qiu H, Gonzalez M, Silesky J, Cerny V, Nielsen J, Jibaja M, Matamis D, Ranero JL, Amin P, Hashemian SM, Clarkson K, Kurahashi K, Villagomez A, Zeggwagh AA, Heunks LM, Laake JH, Palo JE, do Vale Fernandes A, Sandesc D, Arabi Y, Bumbasierevic V, Nin N, Lorente JA, Piquilloud L, Abroug F, McNamee L, Hurtado J, Bajwa E, Démpair G, Sula H, Nunci L, Cani A, Zazu A, Dellera C, Insaurralde CS, Alejandro RV, Daldin J, Vinzio M, Fernandez RO, Cardonnet LP, Bettini LR, Bisso MC, Osman EM, Setten MG, Lovazzano P, Alvarez J, Villar V, Milstein C, Pozo NC, Grubissich N, Plotnikow GA, Vasquez DN, Ilutovich S, Tiribelli N, Chena A, Pellegrini CA, Saenz MG, Estenssoro E, Brizuela M, Gianinetto H, Gomez PE, Cerrato VI, Bezzi MG, Borello SA, Loiacono FA, Fernandez AM, Knowles S, Reynolds C, Inskip DM, Miller JJ, Kong J, Whitehead C, Bihari S, Seven A, Krstevski A, Rodgers HJ, Millar RT, Mckenna TE, Bailey IM, Hanlon GC, Aneman A, Lynch JM, Azad R, Neal J, Woods PW, Roberts BL, Kol MR, Wong HS, Riss KC, Wittebole X, Berghe C, Bulpa PA, Dive AM, Verstraete R, Lebbinck H, Vermassen J, Meersseman P, Ceunen H, Rosa JI, Beraldo DO, Piras C, Rampinelli AM, Nassar AP Jr, Mataloun S, Moock M, Thompson MM, Gonçalves CH, Antônio ACP, Ascoli A, Biondi RS, Fontenele DC, Nobrega D, Sales VM, Shindhe S, Ismail DHMABPH, Laffey J, Beloncle F, Davies KG, Cirone R, Manoharan V, Ismail M, Goligher EC, Jassal M, Nishikawa E, Javeed A, Curley G, Rittayamai N, Parotto M, Ferguson ND, Mehta S, Knoll J, Pronovost A, Chile SC, Bruhn AR, Garcia PH, Aliaga FA, Farías PA, Yumha JS, Ortiz CA, Salas JE, Saez AA, Vega LD, Labarca EF, Martinez FT, Carreño NG, Lora P, Liu H, Liu L, Tang R, Luo X, An Y, Zhao H, Gao Y, Zhai Z, Ye ZL, Wang W, Li W, Li Q, Zheng R, Yu W, Shen J, Li X, Yu T, Lu W, Wu YQ, Huang XB, He Z, Lu Y, Han H, Zhang F, Sun R, Wang HX, Qin SH, Zhu BH, Zhao J, Liu J, Li B, Liu JL, Zhou FC, Li QJ, Zhang XY, Li-Xin Z, Xin-Hua Q, Jiang L, Gao YN, Zhao XY, Li YY, Li XL, Wang C, Yao Q, Yu R, Chen K, Shao H, Qin B, Huang QQ, Zhu WH, Hang AY, Hua MX, Li Y, Xu Y, Di YD, Ling LL, Qin TH, Wang SH, Qin J, Han Y, Vargas MP, Silesky Jimenez JI, González Rojas MA, Solis-Quesada JE, Ramirez-Alfaro CM, Máca J, Sklienka P, Gjedsted J, Villamagua BG, Llano M, Burtin P, Buzancais G, Beuret P, Pelletier N, Mortaza S, Mercat A, Chelly J, Jochmans S, Terzi N, Daubin C, Carteaux G, de Prost N, Chiche JD, Daviaud F, Fartoukh M, Barberet G, Biehler J, Dellamonica J, Doyen D, Arnal JM, Briquet A, Hraiech S, Papazian L, Roux D, Messika J, Kalaitzis E, Médicale R, Dangers L, Combes A, Au SM, Béduneau G, Carpentier D, Zogheib EH, Dupont H, Ricome S, Santoli FL, Besset SL, Michel P, Gelée B, Danin PE, Goubaux B, Crova PJ, Phan NT, Berkelmans F, Badie JC, Tapponnier R, Gally J, Khebbeb S, Herbrecht JE, Schneider F, Declercq PM, Rigaud JP, Duranteau J, Harrois A, Chabanne R, Marin J, Bigot C, Thibault S, Ghazi M, Boukhazna M, Zein SO, Richecoeur JR, Combaux DM, Grelon F, Le Moal C, Sauvadet EP, Robine A, Lemiale V, Reuter D, Dres M, Demoule A, Goldgran-Toledano D, Baboi L, Guérin C, Lohner R, Kraßler J, Schäfer S, Zacharowski KD, Meybohm P, Reske AW, Simon P, Hopf HF, Schuetz M, Baltus T, Papanikolaou MN, Papavasilopoulou TG, Zacharas GA, Ourailogloy V, Mouloudi EK, Massa EV, Nagy EO, Stamou EE, Kiourtzieva EV, Oikonomou MA, Avila LE, Cortez CA, Citalán JE, Jog SA, Sable SD, Shah B, Gurjar M, Baronia AK, Memon M, Muthuchellappan R, Ramesh VJ, Shenoy A, Unnikrishnan R, Dixit SB, Rhayakar RV, Ramakrishnan N, Bhardwaj VK, Mahto HL, Sagar SV, Palaniswamy V, Ganesan D, Jamaati H, Heidari F, Meaney EA, Nichol A, Knapman KM, O'Croinin D, Dunne ES, Breen DM, Clarkson KP, Jaafar RF, Dwyer R, Amir F, Ajetunmobi OO, O'Muircheartaigh AC, Black CS, Treanor N, Collins DV, Altaf W, Zani G, Fusari M, Spadaro S, Volta CA, Graziani R, Brunettini B, Palmese S, Formenti P, Umbrello M, Lombardo A, Pecci E, Botteri M, Savioli M, Protti A, Mattei A, Schiavoni L, Tinnirello A, Todeschini M, Giarratano A, Cortegiani A, Sher S, Rossi A, Antonelli MM, Montini LM, Casalena P, Scafetti S, Panarello G, Occhipinti G, Patroniti N, Pozzi M, Biscione RR, Poli MM, Raimondi F, Albiero D, Crapelli G, Beck E, Pota V, Schiavone V, Molin A, Tarantino F, Monti G, Frati E, Mirabella L, Cinnella G, Fossali T, Colombo R, Pattarino PTI, Mojoli F, Braschi A, Borotto EE, Cracchiolo AN, Palma DM, Raponi F, Foti G, Vascotto ER, Coppadoro A, Brazzi L, Floris L, Iotti GA, Venti A, Yamaguchi O, Takagi S, Maeyama HN, Watanabe E, Yamaji Y, Shimizu K, Shiozaki K, Futami S, Ryosuke S, Saito K, Kameyama Y, Ueno K, Izawa M, Okuda N, Suzuki H, Harasawa T, Nasu M, Takada T, Ito F, Nunomiya S, Koyama K, Abe T, Andoh K, Kusumoto K, Hirata A, Takaba A, Kimura H, Matsumoto S, Higashijima U, Honda H, Aoki N, Imai H, Ogino Y, Mizuguchi I, Ichikado K, Nitta K, Mochizuki K, Hashida T, Tanaka H, Nakamura T, Niimi D, Ueda T, Kashiwa Y, Uchiyama A, Sabelnikovs O, Lebanon PO, Haddad Y, Liew KY, Ñamendys-Silva SA, Jarquin-Badiola YD, Sanchez-Hurtado LA, Gomez-Flores SS, Marin MC, Villagomez AJ, General H, Lemus JS, Fierro JM, Cervantes MR, Mejia FJF, Dector D, Dector DM, Gonzalez DR, Estrella CR, Sanchez-Medina JR, Ramirez-Gutierrez A, George FG, Aguirre JS, Buensuseso JA, Poblano M, Dendane T, Balkhi H, Elkhayari M, Samkaoui N, Ezzouine H, Benslama A, Amor M, Maazouzi W, Cimic N, Beck O, Bruns MM, Schouten JA, Rinia M, Raaijmakers M, Van Wezel HM, Heines SJ, Strauch U, Buise MP, Simonis FD, Schultz MJ, Goodson JC, Browne TS, Navarra L, Hunt A, Hutchison RA, Bailey MB, Newby L, Mcarthur C, Kalkoff M, Mcleod A, Casement J, Hacking DJ, Andersen FH, Dolva MS, Barratt-Due A, Noremark KAL, Søreide E, Sjøbø BÅ, Guttormsen AB, Leon Yoshido HH, Aguilar RZ, Montes Oscanoa FA, Alisasis AU, Robles JB, Pasanting-Lim RAB, Tan Poland BC, Andruszkiewicz P, Jakubowska K, Coxo CM, Alvarez AM, Oliveira BS, Montanha GM, Barros NC, Pereira CS, Messias AM, Monteiro JM, Araujo AM, Catorze NT, Marum SM, Bouw MJ, Gomes RM, Brito VA, Castro S, Estilita JM, Barros FM, Serra IM, Romania A, Tomescu DR, Marcu A, Bedreag OH, Papurica M, Corneci DE, Negoita SI, Grigoriev E, Gritsan AI, Gazenkampf AA, Almekhlafi G, Albarrak MM, Mustafa GM, Maghrabi KA, Salahuddin N, Aisa TM, Al Jabbary AS, Tabhan E, Arabim YM, Arabi YM, Trinidad OA, Al Dorzi HM, Tabhan EE, Bolon S, Smith O, Mancebo J, Aguirre-Bermeo H, Lopez-Delgado JC, Esteve F, Rialp G, Forteza C, de Haro C, Artigas A, Albaiceta GM, de Cima-Iglesias S, Seoane-Quiroga L, Ceniceros-Barros A, Ruiz-Aguilar AL, Claraco-Vega LM, Soler JA, Del Carmen Lorente M, Hermosa C, Gordo F, Prieto-González M, López-Messa JB, Perez MP, Perez CP, Allue RM, Roche-Campo F, Ibañez-Santacruz M, Temprano S, Pintado MC, de Pablo R, Gómez PRA, Ruiz SR, Moles SI, Jurado MT, Arizmendi A, Piacentini EA, Franco N, Honrubia T, Cheng MP, Losada EP, Blanco J, Yuste LJ, Carbayo-Gorriz C, Cazorla-Barranquero FG, Alonso JG, Alda RS, Algaba Á, Navarro G, Cereijo E, Diaz-Rodriguez E, Marcos DP, Montero LA, Para LH, Sanchez RJ, Navalpotro MAB, Abad RD, González RM, Toribio DP, Castro AG, Artiga MJD, Penuelas O, Roser TP, Olga MF, Curto EG, Sánchez RM, Imma VP, Elisabet GM, Claverias L, Magret M, Pellicer AM, Rodriguez LL, Sánchez-Ballesteros J, González-Salamanca Á, Jimenez AG, Huerta FP, Sotillo Diaz JCJ, Lopez EB, Llinares Moya DD, Tallet Alfonso AA, Luis PSE, Cesar PS, Rafael SI, Virgilio CG, Recio NN, Adamsson RO, Rylander CC, Holzgraefe B, Broman LM, Wessbergh J, Persson L, Schiöler F, Kedelv H, Tibblin AO, Appelberg H, Hedlund L, Helleberg J, Eriksson KE, Glietsch R, Larsson N, Nygren I, Nunes SL, Morin AK, Kander T, Adolfsson A, Zender HO, Leemann-Refondini C, Elatrous S, Bouchoucha S, Chouchene I, Ouanes I, Souissi AB, Kamoun S, Demirkiran O, Aker M, Erbabacan E, Ceylan I, Girgin NK, Ozcelik M, Ünal N, Meco BC, Akyol OO, Derman SS, Kennedy B, Parhar K, Srinivasa L, McAuley D, Hopkins P, Mellis C, Kakar V, Hadfield D, Vercueil A, Bhowmick K, Humphreys SK, Ferguson A, Mckee R, Raj AS, Fawkes DA, Watt P, Twohey L, JhaMatthew Thomas RR, Morton A, Kadaba V, Smith MJ, Hormis AP, Kannan SG, Namih M, Reschreiter H, Camsooksai J, Kumar A, Rugonfalvi S, Nutt C, Oneill O, Seasman C, Dempsey G, Scott CJ, Ellis HE, Mckechnie S, Hutton PJ, Di Tomasso NN, Vitale MN, Griffin R, Dean MN, Cranshaw JH, Willett EL, Ioannou N, Gillis S, Csabi P, Macfadyen R, Dawson H, Preez PD, Williams AJ, Boyd O, de Gordoa LO, Bramall J, Symmonds S, Chau SK, Wenham T, Szakmany T, Toth-Tarsoly P, Mccalman KH, Alexander P, Stephenson L, Collyer T, Chapman R, Cooper R, Allan RM, Sim M, Wrathall DW, Irvine DA, Zantua KS, Adams JC, Burtenshaw AJ, Sellors GP, Welters ID, Williams KE, Hessell RJ, Oldroyd MG, Battle CE, Pillai S, Okane SC, Donnelly A, Frigyik AD, Careless JP, May MM, Stewart R, John Trinder T, Hagan SJ, Wise MP, Cole JM, MacFie CC, Dowling AT, Nuñez E, Pittini G, Rodriguez R, Imperio MC, Santos C, França AG, Ebeid A, Deicas A, Uppalapati A, Kamel G, Banner-Goodspeed VM, Beitler JR, Mukkera SR, Kulkarni S, Lee J, Mesar T, Shinn Iii JO, Gomaa D, Tainter C, Yeatts DJ, Warren J, Lanspa MJ, Miller RR, Grissom CK, Brown SM, Bauer PR, Gosselin RJ, Kitch BT, Cohen JE, Beegle SH, Gueret RM, Tulaimat A, Choudry S, Stigler W, Batra H, Huff NG, Lamb KD, Oetting TW, Mohr NM, Judy C, Saito S, Kheir FM, Kheir F, Schlichting AB, Delsing A, Crouch DR, Elmasri M, Ismail D, Dreyer KR, Blakeman TC, Baron RM, Grijalba CQ, Hou PC, Seethala R, Aisiku I, Henderson G, Frendl G, Hou SK, Owens RL, Schomer A, Bumbasirevic V, Jovanovic B, Surbatovic M, Veljovic M., UCL - SSS/IREC/MEDA - Pôle de médecine aiguë, UCL - (SLuc) Service de soins intensifs, UCL - (MGD) Services des soins intensifs, Department of Medicine and Surgery [Monza, Italy] (Research Center on Public Health), Università degli Studi di Milano-Bicocca [Milano] (UNIMIB), Sorbonne Université (SU), Physiopathologie Cardiovasculaire et Mitochondriale (MITOVASC), Université d'Angers (UA)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), ACS - Heart failure & arrhythmias, AII - Inflammatory diseases, Graduate School, Intensive Care Medicine, ACS - Diabetes & metabolism, ACS - Pulmonary hypertension & thrombosis, ACS - Microcirculation, Abe, T, Madotto, F, Pham, T, Nagata, I, Uchida, M, Tamiya, N, Kurahashi, K, Bellani, G, Laffey, J, Abe, T., Madotto, F., Pham, T., Nagata, I., Uchida, M., Tamiya, N., Kurahashi, K., Bellani, G., Laffey, J. G., Francois, G. M., Rabboni, F., Conti, S., Fan, E., Pesenti, A., Brochard, L., Esteban, A., Gattinoni, L., van Haren, F., Larsson, A., Mcauley, D. F., Ranieri, M., Rubenfeld, G., Thompson, B. T., Wrigge, H., Slutsky, A. S., Rios, F., Sottiaux, T., Depuydt, P., Lora, F. S., Azevedo, L. C., Bugedo, G., Qiu, H., Gonzalez, M., Silesky, J., Cerny, V., Nielsen, J., Jibaja, M., Matamis, D., Ranero, J. L., Amin, P., Hashemian, S. M., Clarkson, K., Villagomez, A., Zeggwagh, A. A., Heunks, L. M., Laake, J. H., Palo, J. E., do Vale Fernandes, A., Sandesc, D., Arabi, Y., Bumbasierevic, V., Nin, N., Lorente, J. A., Piquilloud, L., Abroug, F., Mcnamee, L., Hurtado, J., Bajwa, E., Dempair, G., Sula, H., Nunci, L., Cani, A., Zazu, A., Dellera, C., Insaurralde, C. S., Alejandro, R. V., Daldin, J., Vinzio, M., Fernandez, R. O., Cardonnet, L. P., Bettini, L. R., Bisso, M. C., Osman, E. M., Setten, M. G., Lovazzano, P., Alvarez, J., Villar, V., Milstein, C., Pozo, N. C., Grubissich, N., Plotnikow, G. A., Vasquez, D. N., Ilutovich, S., Tiribelli, N., Chena, A., Pellegrini, C. A., Saenz, M. G., Estenssoro, E., Brizuela, M., Gianinetto, H., Gomez, P. E., Cerrato, V. I., Bezzi, M. G., Borello, S. A., Loiacono, F. A., Fernandez, A. M., Knowles, S., Reynolds, C., Inskip, D. M., Miller, J. J., Kong, J., Whitehead, C., Bihari, S., Seven, A., Krstevski, A., Rodgers, H. J., Millar, R. T., Mckenna, T. E., Bailey, I. M., Hanlon, G. C., Aneman, A., Lynch, J. M., Azad, R., Neal, J., Woods, P. W., Roberts, B. L., Kol, M. R., Wong, H. S., Riss, K. C., Wittebole, X., Berghe, C., Bulpa, P. A., Dive, A. M., Verstraete, R., Lebbinck, H., Vermassen, J., Meersseman, P., Ceunen, H., Rosa, J. I., Beraldo, D. O., Piras, C., Rampinelli, A. M., Nassar, A. P., Mataloun, S., Moock, M., Thompson, M. M., Goncalves, C. H., Antonio, Acp., Ascoli, A., Biondi, R. S., Fontenele, D. C., Nobrega, D., Sales, V. M., Shindhe, S., Ismail, Dhmabph., Beloncle, F., Davies, K. G., Cirone, R., Manoharan, V., Ismail, M., Goligher, E. C., Jassal, M., Nishikawa, E., Javeed, A., Curley, G., Rittayamai, N., Parotto, M., Ferguson, N. D., Mehta, S., Knoll, J., Pronovost, A., Chile, S. C., Bruhn, A. R., Garcia, P. H., Aliaga, F. A., Farias, P. A., Yumha, J. S., Ortiz, C. A., Salas, J. E., Saez, A. A., Vega, L. D., Labarca, E. F., Martinez, F. T., Carreno, N. G., Lora, P., Liu, H., Liu, L., Tang, R., Luo, X., An, Y., Zhao, H., Gao, Y., Zhai, Z., Ye, Z. L., Wang, W., Li, W., Li, Q., Zheng, R., Yu, W., Shen, J., Li, X., Yu, T., Lu, W., Wu, Y. Q., Huang, X. B., He, Z., Lu, Y., Han, H., Zhang, F., Sun, R., Wang, H. X., Qin, S. H., Zhu, B. H., Zhao, J., Liu, J., Li, B., Liu, J. L., Zhou, F. C., Li, Q. J., Zhang, X. Y., Li-Xin, Z., Xin-Hua, Q., Jiang, L., Gao, Y. N., Zhao, X. Y., Li, Y. Y., Li, X. L., Wang, C., Yao, Q., Yu, R., Chen, K., Shao, H., Qin, B., Huang, Q. Q., Zhu, W. H., Hang, A. Y., Hua, M. X., Li, Y., Xu, Y., Di, Y. D., Ling, L. L., Qin, T. H., Wang, S. H., Qin, J., Han, Y., Vargas, M. P., Silesky Jimenez, J. I., Gonzalez Rojas, M. A., Solis-Quesada, J. E., Ramirez-Alfaro, C. M., Maca, J., Sklienka, P., Gjedsted, J., Villamagua, B. G., Llano, M., Burtin, P., Buzancais, G., Beuret, P., Pelletier, N., Mortaza, S., Mercat, A., Chelly, J., Jochmans, S., Terzi, N., Daubin, C., Carteaux, G., de Prost, N., Chiche, J. D., Daviaud, F., Fartoukh, M., Barberet, G., Biehler, J., Dellamonica, J., Doyen, D., Arnal, J. M., Briquet, A., Hraiech, S., Papazian, L., Roux, D., Messika, J., Kalaitzis, E., Medicale, R., Dangers, L., Combes, A., Au, S. M., Beduneau, G., Carpentier, D., Zogheib, E. H., Dupont, H., Ricome, S., Santoli, F. L., Besset, S. L., Michel, P., Gelee, B., Danin, P. E., Goubaux, B., Crova, P. J., Phan, N. T., Berkelmans, F., Badie, J. C., Tapponnier, R., Gally, J., Khebbeb, S., Herbrecht, J. E., Schneider, F., Declercq, P. M., Rigaud, J. P., Duranteau, J., Harrois, A., Chabanne, R., Marin, J., Bigot, C., Thibault, S., Ghazi, M., Boukhazna, M., Zein, S. O., Richecoeur, J. R., Combaux, D. M., Grelon, F., Le Moal, C., Sauvadet, E. P., Robine, A., Lemiale, V., Reuter, D., Dres, M., Demoule, A., Goldgran-Toledano, D., Baboi, L., Guerin, C., Lohner, R., Krassler, J., Schafer, S., Zacharowski, K. D., Meybohm, P., Reske, A. W., Simon, P., Hopf, H. F., Schuetz, M., Baltus, T., Papanikolaou, M. N., Papavasilopoulou, T. G., Zacharas, G. A., Ourailogloy, V., Mouloudi, E. K., Massa, E. V., Nagy, E. O., Stamou, E. E., Kiourtzieva, E. V., Oikonomou, M. A., Avila, L. E., Cortez, C. A., Citalan, J. E., Jog, S. A., Sable, S. D., Shah, B., Gurjar, M., Baronia, A. K., Memon, M., Muthuchellappan, R., Ramesh, V. J., Shenoy, A., Unnikrishnan, R., Dixit, S. B., Rhayakar, R. V., Ramakrishnan, N., Bhardwaj, V. K., Mahto, H. L., Sagar, S. V., Palaniswamy, V., Ganesan, D., Jamaati, H., Heidari, F., Meaney, E. A., Nichol, A., Knapman, K. M., O'Croinin, D., Dunne, E. S., Breen, D. M., Clarkson, K. P., Jaafar, R. F., Dwyer, R., Amir, F., Ajetunmobi, O. O., O'Muircheartaigh, A. C., Black, C. S., Treanor, N., Collins, D. V., Altaf, W., Zani, G., Fusari, M., Spadaro, S., Volta, C. A., Graziani, R., Brunettini, B., Palmese, S., Formenti, P., Umbrello, M., Lombardo, A., Pecci, E., Botteri, M., Savioli, M., Protti, A., Mattei, A., Schiavoni, L., Tinnirello, A., Todeschini, M., Giarratano, A., Cortegiani, A., Sher, S., Rossi, A., Antonelli, M. M., Montini, L. M., Casalena, P., Scafetti, S., Panarello, G., Occhipinti, G., Patroniti, N., Pozzi, M., Biscione, R. R., Poli, M. M., Raimondi, F., Albiero, D., Crapelli, G., Beck, E., Pota, V., Schiavone, V., Molin, A., Tarantino, F., Monti, G., Frati, E., Mirabella, L., Cinnella, G., Fossali, T., Colombo, R., Pattarino, Pti., Mojoli, F., Braschi, A., Borotto, E. E., Cracchiolo, A. N., Palma, D. M., Raponi, F., Foti, G., Vascotto, E. R., Coppadoro, A., Brazzi, L., Floris, L., Iotti, G. A., Venti, A., Yamaguchi, O., Takagi, S., Maeyama, H. N., Watanabe, E., Yamaji, Y., Shimizu, K., Shiozaki, K., Futami, S., Ryosuke, S., Saito, K., Kameyama, Y., Ueno, K., Izawa, M., Okuda, N., Suzuki, H., Harasawa, T., Nasu, M., Takada, T., Ito, F., Nunomiya, S., Koyama, K., Andoh, K., Kusumoto, K., Hirata, A., Takaba, A., Kimura, H., Matsumoto, S., Higashijima, U., Honda, H., Aoki, N., Imai, H., Ogino, Y., Mizuguchi, I., Ichikado, K., Nitta, K., Mochizuki, K., Hashida, T., Tanaka, H., Nakamura, T., Niimi, D., Ueda, T., Kashiwa, Y., Uchiyama, A., Sabelnikovs, O., Lebanon, P. O., Haddad, Y., Liew, K. Y., Namendys-Silva, S. A., Jarquin-Badiola, Y. D., Sanchez-Hurtado, L. A., Gomez-Flores, S. S., Marin, M. C., Villagomez, A. J., General, H., Lemus, J. S., Fierro, J. M., Cervantes, M. R., Mejia, Fjf., Dector, D., Dector, D. M., Gonzalez, D. R., Estrella, C. R., Sanchez-Medina, J. R., Ramirez-Gutierrez, A., George, F. G., Aguirre, J. S., Buensuseso, J. A., Poblano, M., Dendane, T., Balkhi, H., Elkhayari, M., Samkaoui, N., Ezzouine, H., Benslama, A., Amor, M., Maazouzi, W., Cimic, N., Beck, O., Bruns, M. M., Schouten, J. A., Rinia, M., Raaijmakers, M., Van Wezel, H. M., Heines, S. J., Strauch, U., Buise, M. P., Simonis, F. D., Schultz, M. J., Goodson, J. C., Browne, T. S., Navarra, L., Hunt, A., Hutchison, R. A., Bailey, M. B., Newby, L., Mcarthur, C., Kalkoff, M., Mcleod, A., Casement, J., Hacking, D. J., Andersen, F. H., Dolva, M. S., Barratt-Due, A., Noremark, Kal., Soreide, E., Sjobo, B. A., Guttormsen, A. B., Leon Yoshido, H. H., Aguilar, R. Z., Montes Oscanoa, F. A., Alisasis, A. U., Robles, J. B., Pasanting-Lim, Rab., Tan Poland, B. C., Andruszkiewicz, P., Jakubowska, K., Coxo, C. M., Alvarez, A. M., Oliveira, B. S., Montanha, G. M., Barros, N. C., Pereira, C. S., Messias, A. M., Monteiro, J. M., Araujo, A. M., Catorze, N. T., Marum, S. M., Bouw, M. J., Gomes, R. M., Brito, V. A., Castro, S., Estilita, J. M., Barros, F. M., Serra, I. M., Romania, A., Tomescu, D. R., Marcu, A., Bedreag, O. H., Papurica, M., Corneci, D. E., Negoita, S. I., Grigoriev, E., Gritsan, A. I., Gazenkampf, A. A., Almekhlafi, G., Albarrak, M. M., Mustafa, G. M., Maghrabi, K. A., Salahuddin, N., Aisa, T. M., Al Jabbary, A. S., Tabhan, E., Arabim, Y. M., Arabi, Y. M., Trinidad, O. A., Al Dorzi, H. M., Tabhan, E. E., Bolon, S., Smith, O., Mancebo, J., Aguirre-Bermeo, H., Lopez-Delgado, J. C., Esteve, F., Rialp, G., Forteza, C., de Haro, C., Artigas, A., Albaiceta, G. M., de Cima-Iglesias, S., Seoane-Quiroga, L., Ceniceros-Barros, A., Ruiz-Aguilar, A. L., Claraco-Vega, L. M., Soler, J. A., Del Carmen Lorente, M., Hermosa, C., Gordo, F., Prieto-Gonzalez, M., Lopez-Messa, J. B., Perez, M. P., Perez, C. P., Allue, R. M., Roche-Campo, F., Ibanez-Santacruz, M., Temprano, S., Pintado, M. C., de Pablo, R., Gomez, Pra., Ruiz, S. R., Moles, S. I., Jurado, M. T., Arizmendi, A., Piacentini, E. A., Franco, N., Honrubia, T., Cheng, M. P., Losada, E. P., Blanco, J., Yuste, L. J., Carbayo-Gorriz, C., Cazorla-Barranquero, F. G., Alonso, J. G., Alda, R. S., Algaba, A., Navarro, G., Cereijo, E., Diaz-Rodriguez, E., Marcos, D. P., Montero, L. A., Para, L. H., Sanchez, R. J., Navalpotro, Mab., Abad, R. D., Gonzalez, R. M., Toribio, D. P., Castro, A. G., Artiga, Mjd., Penuelas, O., Roser, T. P., Olga, M. F., Curto, E. G., Sanchez, R. M., Imma, V. P., Elisabet, G. M., Claverias, L., Magret, M., Pellicer, A. M., Rodriguez, L. L., Sanchez-Ballesteros, J., Gonzalez-Salamanca, A., Jimenez, A. G., Huerta, F. P., Sotillo Diaz, Jcj., Lopez, E. B., Llinares Moya, D. D., Tallet Alfonso, A. A., Luis, Pse., Cesar, P. S., Rafael, S. I., Virgilio, C. G., Recio, N. N., Adamsson, R. O., Rylander, C. C., Holzgraefe, B., Broman, L. M., Wessbergh, J., Persson, L., Schioler, F., Kedelv, H., Tibblin, A. O., Appelberg, H., Hedlund, L., Helleberg, J., Eriksson, K. E., Glietsch, R., Larsson, N., Nygren, I., Nunes, S. L., Morin, A. K., Kander, T., Adolfsson, A., Zender, H. O., Leemann-Refondini, C., Elatrous, S., Bouchoucha, S., Chouchene, I., Ouanes, I., Souissi, A. B., Kamoun, S., Demirkiran, O., Aker, M., Erbabacan, E., Ceylan, I., Girgin, N. K., Ozcelik, M., Unal, N., Meco, B. C., Akyol, O. O., Derman, S. S., Kennedy, B., Parhar, K., Srinivasa, L., Mcauley, D., Hopkins, P., Mellis, C., Kakar, V., Hadfield, D., Vercueil, A., Bhowmick, K., Humphreys, S. K., Ferguson, A., Mckee, R., Raj, A. S., Fawkes, D. A., Watt, P., Twohey, L., JhaMatthew Thomas, R. R., Morton, A., Kadaba, V., Smith, M. J., Hormis, A. P., Kannan, S. G., Namih, M., Reschreiter, H., Camsooksai, J., Kumar, A., Rugonfalvi, S., Nutt, C., Oneill, O., Seasman, C., Dempsey, G., Scott, C. J., Ellis, H. E., Mckechnie, S., Hutton, P. J., Di Tomasso, N. N., Vitale, M. N., Griffin, R., Dean, M. N., Cranshaw, J. H., Willett, E. L., Ioannou, N., Gillis, S., Csabi, P., Macfadyen, R., Dawson, H., Preez, P. D., Williams, A. J., Boyd, O., de Gordoa, L. 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M., Tulaimat, A., Choudry, S., Stigler, W., Batra, H., Huff, N. G., Lamb, K. D., Oetting, T. W., Mohr, N. M., Judy, C., Saito, S., Kheir, F. M., Kheir, F., Schlichting, A. B., Delsing, A., Crouch, D. R., Elmasri, M., Ismail, D., Dreyer, K. R., Blakeman, T. C., Baron, R. M., Grijalba, C. Q., Hou, P. C., Seethala, R., Aisiku, I., Henderson, G., Frendl, G., Hou, S. K., Owens, R. L., Schomer, A., Bumbasirevic, V., Jovanovic, B., Surbatovic, M., Veljovic, M., Abe T., Madotto F., Pham T., Nagata I., Uchida M., Tamiya N., Kurahashi K., Bellani G., Laffey J.G, and Francois GM, Rabboni F, Madotto F, Conti S, Laffey JG, Bellani G, Pham T, Fan E, Pesenti A, Brochard L, Esteban A, Gattinoni L, van Haren F, Larsson A, McAuley DF, Ranieri M, Rubenfeld G, Thompson BT, Wrigge H, Slutsky AS, Rios F, Sottiaux T, Depuydt P, Lora FS, Azevedo LC, Bugedo G, Qiu H, Gonzalez M, Silesky J, Cerny V, Nielsen J, Jibaja M, Pham T, Matamis D, Ranero JL, Amin P, Hashemian SM, Clarkson K, Kurahashi K, Villagomez A, Zeggwagh AA, Heunks LM, Laake JH, Palo JE, do Vale Fernandes A, Sandesc D, Arabi Y, Bumbasierevic V, Nin N, Lorente JA, Piquilloud L, Abroug F, McNamee L, Hurtado J, Bajwa E, Démpair G, Sula H, Nunci L, Cani A, Zazu A, Dellera C, Insaurralde CS, Alejandro RV, Daldin J, Vinzio M, Fernandez RO, Cardonnet LP, Bettini LR, Bisso MC, Osman EM, Setten MG, Lovazzano P, Alvarez J, 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Bruhn AR, Garcia PH, Aliaga FA, Farías PA, Yumha JS, Ortiz CA, Salas JE, Saez AA, Vega LD, Labarca EF, Martinez FT, Carreño NG, Lora P, Liu H, Liu L, Tang R, Luo X, An Y, Zhao H, Gao Y, Zhai Z, Ye ZL, Wang W, Li W, Li Q, Zheng R, Yu W, Shen J, Li X, Yu T, Lu W, Wu YQ, Huang XB, He Z, Lu Y, Han H, Zhang F, Sun R, Wang HX, Qin SH, Zhu BH, Zhao J, Liu J, Li B, Liu JL, Zhou FC, Li QJ, Zhang XY, Li-Xin Z, Xin-Hua Q, Jiang L, Gao YN, Zhao XY, Li YY, Li XL, Wang C, Yao Q, Yu R, Chen K, Shao H, Qin B, Huang QQ, Zhu WH, Hang AY, Hua MX, Li Y, Xu Y, Di YD, Ling LL, Qin TH, Wang SH, Qin J, Han Y, Vargas MP, Silesky Jimenez JI, González Rojas MA, Solis-Quesada JE, Ramirez-Alfaro CM, Máca J, Sklienka P, Gjedsted J, Villamagua BG, Llano M, Burtin P, Buzancais G, Beuret P, Pelletier N, Mortaza S, Mercat A, Chelly J, Jochmans S, Terzi N, Daubin C, Carteaux G, de Prost N, Chiche JD, Daviaud F, Fartoukh M, Barberet G, Biehler J, Dellamonica J, Doyen D, Arnal JM, Briquet A, Hraiech S, Papazian L, Roux D, Messika J, Kalaitzis E, Médicale R, Dangers L, Combes A, Au SM, Béduneau G, Carpentier D, Zogheib EH, Dupont H, Ricome S, Santoli FL, Besset SL, Michel P, Gelée B, Danin PE, Goubaux B, Crova PJ, Phan NT, Berkelmans F, Badie JC, Tapponnier R, Gally J, Khebbeb S, Herbrecht JE, Schneider F, Declercq PM, Rigaud JP, Duranteau J, Harrois A, Chabanne R, Marin J, Bigot C, Thibault S, Ghazi M, Boukhazna M, Zein SO, Richecoeur JR, Combaux DM, Grelon F, Le Moal C, Sauvadet EP, Robine A, Lemiale V, Reuter D, Dres M, Demoule A, Goldgran-Toledano D, Baboi L, Guérin C, Lohner R, Kraßler J, Schäfer S, Zacharowski KD, Meybohm P, Reske AW, Simon P, Hopf HF, Schuetz M, Baltus T, Papanikolaou MN, Papavasilopoulou TG, Zacharas GA, Ourailogloy V, Mouloudi EK, Massa EV, Nagy EO, Stamou EE, Kiourtzieva EV, Oikonomou MA, Avila LE, Cortez CA, Citalán JE, Jog SA, Sable SD, Shah B, Gurjar M, Baronia AK, Memon M, Muthuchellappan R, Ramesh VJ, Shenoy A, Unnikrishnan R, Dixit SB, Rhayakar RV, Ramakrishnan N, Bhardwaj VK, Mahto HL, Sagar SV, Palaniswamy V, Ganesan D, Hashemian SM, Jamaati H, Heidari F, Meaney EA, Nichol A, Knapman KM, O'Croinin D, Dunne ES, Breen DM, Clarkson KP, Jaafar RF, Dwyer R, Amir F, Ajetunmobi OO, O'Muircheartaigh AC, Black CS, Treanor N, Collins DV, Altaf W, Zani G, Fusari M, Spadaro S, Volta CA, Graziani R, Brunettini B, Palmese S, Formenti P, Umbrello M, Lombardo A, Pecci E, Botteri M, Savioli M, Protti A, Mattei A, Schiavoni L, Tinnirello A, Todeschini M, Giarratano A, Cortegiani A, Sher S, Rossi A, Antonelli MM, Montini LM, Casalena P, Scafetti S, Panarello G, Occhipinti G, Patroniti N, Pozzi M, Biscione RR, Poli MM, Raimondi F, Albiero D, Crapelli G, Beck E, Pota V, Schiavone V, Molin A, Tarantino F, Monti G, Frati E, Mirabella L, Cinnella G, Fossali T, Colombo R, Pattarino PTI, Mojoli F, Braschi A, Borotto EE, Cracchiolo AN, Palma DM, Raponi F, Foti G, Vascotto ER, Coppadoro A, Brazzi L, Floris L, Iotti GA, Venti A, Yamaguchi O, Takagi S, Maeyama HN, Watanabe E, Yamaji Y, Shimizu K, Shiozaki K, Futami S, Ryosuke S, Saito K, Kameyama Y, Ueno K, Izawa M, Okuda N, Suzuki H, Harasawa T, Nasu M, Takada T, Ito F, Nunomiya S, Koyama K, Abe T, Andoh K, Kusumoto K, Hirata A, Takaba A, Kimura H, Matsumoto S, Higashijima U, Honda H, Aoki N, Imai H, Ogino Y, Mizuguchi I, Ichikado K, Nitta K, Mochizuki K, Hashida T, Tanaka H, Nakamura T, Niimi D, Ueda T, Kashiwa Y, Uchiyama A, Sabelnikovs O, Lebanon PO, Haddad Y, Liew KY, Ñamendys-Silva SA, Jarquin-Badiola YD, Sanchez-Hurtado LA, Gomez-Flores SS, Marin MC, Villagomez AJ, General H, Lemus JS, Fierro JM, Cervantes MR, Mejia FJF, Dector D, Dector DM, Gonzalez DR, Estrella CR, Sanchez-Medina JR, Ramirez-Gutierrez A, George FG, Aguirre JS, Buensuseso JA, Poblano M, Dendane T, Balkhi H, Elkhayari M, Samkaoui N, Ezzouine H, Benslama A, Amor M, Maazouzi W, Cimic N, Beck O, Bruns MM, Schouten JA, Rinia M, Raaijmakers M, Van Wezel HM, Heines SJ, Strauch U, Buise MP, Simonis FD, Schultz MJ, Goodson JC, Browne TS, Navarra L, Hunt A, Hutchison RA, Bailey MB, Newby L, Mcarthur C, Kalkoff M, Mcleod A, Casement J, Hacking DJ, Andersen FH, Dolva MS, Laake JH, Barratt-Due A, Noremark KAL, Søreide E, Sjøbø BÅ, Guttormsen AB, Leon Yoshido HH, Aguilar RZ, Montes Oscanoa FA, Alisasis AU, Robles JB, Pasanting-Lim RAB, Tan Poland BC, Andruszkiewicz P, Jakubowska K, Coxo CM, Alvarez AM, Oliveira BS, Montanha GM, Barros NC, Pereira CS, Messias AM, Monteiro JM, Araujo AM, Catorze NT, Marum SM, Bouw MJ, Gomes RM, Brito VA, Castro S, Estilita JM, Barros FM, Serra IM, Romania A, Tomescu DR, Marcu A, Bedreag OH, Papurica M, Corneci DE, Negoita SI, Grigoriev E, Gritsan AI, Gazenkampf AA, Almekhlafi G, Albarrak MM, Mustafa GM, Maghrabi KA, Salahuddin N, Aisa TM, Al Jabbary AS, Tabhan E, Arabim YM, Arabi YM, Trinidad OA, Al Dorzi HM, Tabhan EE, Bolon S, Smith O, Mancebo J, Aguirre-Bermeo H, Lopez-Delgado JC, Esteve F, Rialp G, Forteza C, de Haro C, Artigas A, Albaiceta GM, de Cima-Iglesias S, Seoane-Quiroga L, Ceniceros-Barros A, Ruiz-Aguilar AL, Claraco-Vega LM, Soler JA, Del Carmen Lorente M, Hermosa C, Gordo F, Prieto-González M, López-Messa JB, Perez MP, Perez CP, Allue RM, Roche-Campo F, Ibañez-Santacruz M, Temprano S, Pintado MC, de Pablo R, Gómez PRA, Ruiz SR, Moles SI, Jurado MT, Arizmendi A, Piacentini EA, Franco N, Honrubia T, Cheng MP, Losada EP, Blanco J, Yuste LJ, Carbayo-Gorriz C, Cazorla-Barranquero FG, Alonso JG, Alda RS, Algaba Á, Navarro G, Cereijo E, Diaz-Rodriguez E, Marcos DP, Montero LA, Para LH, Sanchez RJ, Navalpotro MAB, Abad RD, González RM, Toribio DP, Castro AG, Artiga MJD, Penuelas O, Roser TP, Olga MF, Curto EG, Sánchez RM, Imma VP, Elisabet GM, Claverias L, Magret M, Pellicer AM, Rodriguez LL, Sánchez-Ballesteros J, González-Salamanca Á, Jimenez AG, Huerta FP, Sotillo Diaz JCJ, Lopez EB, Llinares Moya DD, Tallet Alfonso AA, Luis PSE, Cesar PS, Rafael SI, Virgilio CG, Recio NN, Adamsson RO, Rylander CC, Holzgraefe B, Broman LM, Wessbergh J, Persson L, Schiöler F, Kedelv H, Tibblin AO, Appelberg H, Hedlund L, Helleberg J, Eriksson KE, Glietsch R, Larsson N, Nygren I, Nunes SL, Morin AK, Kander T, Adolfsson A, Zender HO, Leemann-Refondini C, Elatrous S, Bouchoucha S, Chouchene I, Ouanes I, Souissi AB, Kamoun S, Demirkiran O, Aker M, Erbabacan E, Ceylan I, Girgin NK, Ozcelik M, Ünal N, Meco BC, Akyol OO, Derman SS, Kennedy B, Parhar K, Srinivasa L, McAuley D, Hopkins P, Mellis C, Kakar V, Hadfield D, Vercueil A, Bhowmick K, Humphreys SK, Ferguson A, Mckee R, Raj AS, Fawkes DA, Watt P, Twohey L, JhaMatthew Thomas RR, Morton A, Kadaba V, Smith MJ, Hormis AP, Kannan SG, Namih M, Reschreiter H, Camsooksai J, Kumar A, Rugonfalvi S, Nutt C, Oneill O, Seasman C, Dempsey G, Scott CJ, Ellis HE, Mckechnie S, Hutton PJ, Di Tomasso NN, Vitale MN, Griffin R, Dean MN, Cranshaw JH, Willett EL, Ioannou N, Gillis S, Csabi P, Macfadyen R, Dawson H, Preez PD, Williams AJ, Boyd O, de Gordoa LO, Bramall J, Symmonds S, Chau SK, Wenham T, Szakmany T, Toth-Tarsoly P, Mccalman KH, Alexander P, Stephenson L, Collyer T, Chapman R, Cooper R, Allan RM, Sim M, Wrathall DW, Irvine DA, Zantua KS, Adams JC, Burtenshaw AJ, Sellors GP, Welters ID, Williams KE, Hessell RJ, Oldroyd MG, Battle CE, Pillai S, Okane SC, Donnelly A, Frigyik AD, Careless JP, May MM, Stewart R, John Trinder T, Hagan SJ, Wise MP, Cole JM, MacFie CC, Dowling AT, Nin N, Nuñez E, Pittini G, Rodriguez R, Imperio MC, Santos C, França AG, Ebeid A, Deicas A, Uppalapati A, Kamel G, Banner-Goodspeed VM, Beitler JR, Mukkera SR, Kulkarni S, Lee J, Mesar T, Shinn Iii JO, Gomaa D, Tainter C, Yeatts DJ, Warren J, Lanspa MJ, Miller RR, Grissom CK, Brown SM, Bauer PR, Gosselin RJ, Kitch BT, Cohen JE, Beegle SH, Gueret RM, Tulaimat A, Choudry S, Stigler W, Batra H, Huff NG, Lamb KD, Oetting TW, Mohr NM, Judy C, Saito S, Kheir FM, Kheir F, Schlichting AB, Delsing A, Crouch DR, Elmasri M, Ismail D, Dreyer KR, Blakeman TC, Gomaa D, Baron RM, Grijalba CQ, Hou PC, Seethala R, Aisiku I, Henderson G, Frendl G, Hou SK, Owens RL, Schomer A, Bumbasirevic V, Jovanovic B, Surbatovic M, Veljovic M.

Subjects
Male, ARDS, Internationality, [SDV]Life Sciences [q-bio], humanos, lnfectious Diseases and Global Health Radboud Institute for Molecular Life Sciences [Radboudumc 4], traqueostomía, Critical Care and Intensive Care Medicine, Severity of Illness Index, Cohort Studies, Propensity-matched analysi, 0302 clinical medicine, Tracheostomy, estudios prospectivos, Epidemiology, Acute respiratory distress syndrome (ARDS), 030212 general & internal medicine, Prospective Studies, puntuación de propensión, 10. No inequality, Prospective cohort study, estudios de cohortes, mediana edad, anciano, Respiratory Distress Syndrome, respiración, Respiration, lcsh:Medical emergencies. Critical care. Intensive care. First aid, Middle Aged, 3. Good health, Intensive Care Units, Cohort, Artificial, Critical Illne, Female, ICU, Propensity-matched analysis, Ventilation, Aged, Critical Illness, Humans, Propensity Score, Respiration, Artificial, Respiratory Distress Syndrome, Adult, Cohort study, Human, Adult, medicine.medical_specialty, Intensive Care Unit, Socio-culturale, unidades de cuidados intensivos, enfermedad crítica, 03 medical and health sciences, Severity of illness, Settore MED/41 - ANESTESIOLOGIA, medicine, índice de gravedad de la enfermedad, business.industry, Research, internacionalidad, lcsh:RC86-88.9, medicine.disease, R1, Prospective Studie, 030228 respiratory system, Propensity score matching, Emergency medicine, Observational study, Cohort Studie, business
Abstract

Background: To better understand the epidemiology and patterns of tracheostomy practice for patients with acute respiratory distress syndrome (ARDS), we investigated the current usage of tracheostomy in patients with ARDS recruited into the Large Observational Study to Understand the Global Impact of Severe Acute Respiratory Failure (LUNG-SAFE) study. Methods: This is a secondary analysis of LUNG-SAFE, an international, multicenter, prospective cohort study of patients receiving invasive or noninvasive ventilation in 50 countries spanning 5 continents. The study was carried out over 4 weeks consecutively in the winter of 2014, and 459 ICUs participated. We evaluated the clinical characteristics, management and outcomes of patients that received tracheostomy, in the cohort of patients that developed ARDS on day 1-2 of acute hypoxemic respiratory failure, and in a subsequent propensity-matched cohort. Results: Of the 2377 patients with ARDS that fulfilled the inclusion criteria, 309 (13.0%) underwent tracheostomy during their ICU stay. Patients from high-income European countries (n = 198/1263) more frequently underwent tracheostomy compared to patients from non-European high-income countries (n = 63/649) or patients from middle-income countries (n = 48/465). Only 86/309 (27.8%) underwent tracheostomy on or before day 7, while the median timing of tracheostomy was 14 (Q1-Q3, 7-21) days after onset of ARDS. In the subsample matched by propensity score, ICU and hospital stay were longer in patients with tracheostomy. While patients with tracheostomy had the highest survival probability, there was no difference in 60-day or 90-day mortality in either the patient subgroup that survived for at least 5 days in ICU, or in the propensity-matched subsample. Conclusions: Most patients that receive tracheostomy do so after the first week of critical illness. Tracheostomy may prolong patient survival but does not reduce 60-day or 90-day mortality., This work was funded and supported by the European Society of Intensive Care Medicine (ESICM), Brussels, Belgium, by St Michael's Hospital, Toronto, Canada, and by the University of Milan-Bicocca, Monza, Italy. This work was supported by JSPS KAKENHI JP 16 K15388, Japan.

Published
2018

6. MULTILEVEL VIEW OF FACILITY CHARACTERISTICS AND CARE NEED LEVEL DETERIORATION IN PRIVATE RESIDENTIAL HOMES IN JAPAN

Author

Sandoval Garrido, F, Tamiya, N, Jin, X, and Watanabe, T

Subjects
Abstracts
Abstract

In this study we examined the relationship of facility characteristics and care need level deterioration of users in Japanese private residential homes, stratifying by manpower levels. Care need levels are the official measurement for long-term care certification in Japan. We used a longitudinal, multilevel logistic regression design. Data was shared by a private residential home provider. Two points of administrative data for November 2015 and November 2016 were used, with a total of 4,734 users from 112 facilities in both sets. Facilities were divided into those with (i) higher manpower, and those with (ii) lower manpower, as preliminary analyses showed the relevance of staffing levels. Higher and lower manpower levels were determined by using the median of cumulative total staff working hours per 100 users per facility at each observation point. We controlled for gender, baseline age, care-level, prefecture, grip strength, mental and physical independence and institutionalization time. Results showed that factors associated with care need level deterioration in homes with lower manpower were as follows: fewer number of users (Odds Ratio [OR]:1.05), larger capacity (OR: 1.05), newer homes (OR: 1.09), fewer number of floors (OR: 1.26), and a higher users-to-beds ratio (OR: 1.56). However, these detrimental effects were not observed in facilities with higher manpower; the associations between care need level deterioration and these factors were moderated by the level of manpower. We conclude that higher manpower while addressing other risks, may help prevent deterioration of private residential home users.

Published
2018

7. EARLY INTENSIVE REHABILITATION AFTER HIP FRACTURE SURGERY AND ACTIVITIES OF DAILY LIVING IN PATIENTS WITH DEMENTIA

Author

Uda, K, Yasunaga, H, and Tamiya, N

Subjects
Abstracts
Abstract

Using a nationwide inpatient database in Japan, this retrospective cohort study examined the effect of early intensive postoperative rehabilitation on activities of daily living (ADL) based on the Barthel Index (BI) after hip fracture surgery in patients with dementia. Patients aged ≥65 years with dementia at admission who underwent hip fracture surgery and received postoperative rehabilitation from 1 April 2014 to 31 March 2016 were included. The average early rehabilitation intensity per day was calculated as the total units of rehabilitation within 7 days after surgery divided by the 7 days and categorized into the following four groups

Published
2018

8. HEARING LOSS AND OUTDOOR ACTIVITY LIMITATION, PSYCHOLOGICAL DISTRESS, AND MEMORY LOSS AMONG ELDERLY PEOPLE IN JAPAN

Author

Iwagami, M, Kobayashi, Y, Tsukazaki, E, Watanabe, T, Sugiyama, T, Wada, T, Hara, A, and Tamiya, N

Subjects
Abstracts
Abstract

We aimed to investigate the associations between self-reported hearing loss and outdoor activity limitations, psychological distress, and memory loss among elderly people. We conducted a cross-sectional study using the data from a nationally-representative questionnaire survey (2016 Comprehensive Survey of Living Conditions in Japan). The study population included people aged ≥65 years living at home, without clinically diagnosed dementia. The exposure of interest was self-reported hearing loss (Yes/No), whereas outcomes included outdoor activity limitations (Yes/No), psychological distress (Kessler Psychological Distress Scale [K6] score of ≥5), and self-reported memory loss (Yes/No). We conducted logistic regression analyses, adjusted for age, sex, smoking, alcohol, educational status, number of household members, average household expenditure in a month, and chronic diseases (diabetes, hypertension, thyroid disease, Parkinson’s disease, stroke, coronary artery disease, and cancer). Among 137,723 elderly people (mean age 74.5 [standard deviation 7.4], 45.1% men), 12,389 (9.0%) reported hearing loss. People with hearing loss showed a higher prevalence of outdoor activity limitation (28.9% vs. 9.5%), psychological distress (39.7% vs. 19.3%), and memory loss (37.7% vs. 5.2%) than those without. The adjusted odds ratios (95% confidence interval) comparing people with and without hearing loss were 2.20 (2.09–2.31), 2.24 (2.15–2.34), and 7.53 (7.17–7.90) for outdoor activity limitations, psychological distress, and memory loss. In conclusion, this nationwide study suggested that elderly people with hearing loss were more likely to experience outdoor activity limitations, psychological distress, and memory loss than those without. Early identification of and intervention in hearing loss may potentially reduce the risk of these poor health outcomes.

Published
2018

9. THE ASSOCIATIONS OF SOCIAL ISOLATION WITH MEDICAL AND LONG-TERM CARE UTILIZATION AMONG OLDER ADULTS IN JAPAN

Author

Mitsutake, S, Koike, T, Ishizaki, T, Nishi, M, Kobayashi, E, Hasebe, M, Tamiya, N, and Fujiwara, Y

Subjects
Abstracts
Abstract

This study aimed to examine whether social isolation (isolation) defined as having less contact than once a week with anyone outside the household was associated with medical and long-term care utilization. We conducted a two-wave questionnaire survey among city residents aged over 65 years (Wave 1 in 2008 and Wave 2 in 2010) in Wako city, Japan. From health insurance claim data and long-term care data from 2008 to 2011, the present cohort study extracted data receiving medical and long-term care and the related expenses in the three-year period. Using a two-part model to identify the association of isolation with receiving medical and long-term care and the related expenses, we analyzed 1,520 older adults. Approximately 29.6% of the participants were isolated. Using logistic regression-adjusted covariates (sex, age, educational level, resident status, household income, instrumental activities of daily living, depression symptoms, and the prevalence of cardiovascular disease, liver disease or other diseases), isolation was negatively associated with receiving medical outpatient care (adjusted odds ratio: 0.407, 95% confidence interval[95%CI]: 0.235 to 0.703). Moreover, in the generalized linear model for data with a gamma distribution with a log-link function, isolation was negatively associated with outpatient care expenses (adjusted risk ratio: 0.833, 95%CI: 0.747 to 0.928). There were no significant associations of isolation with inpatient care and long-term care and the related expenses. The negative associations of isolation with receiving outpatient care and the related expenses among older adults may demonstrate that those with isolation do not receive the medical outpatient care they required.

Published
2018

27. Predictors of continuity in home care for the elderly under public long-term care insurance in Japan.

Author

Ohwaki K, Hashimoto H, Sato M, Tamiya N, and Yano E

Abstract

Background and aims: With the rapid increase in the elderly population, the number of people requiring care is also increasing and the capacity of the family to provide care is decreasing. Because institutionalization costs are high, more research is needed to investigate predictors of preventing institutionalization. The aim of this study was to examine the impact of social engagement and other predictive factors, including disability, household composition, and formal services, on continuity in home care of the elderly. Methods: The study was retrospective longitudinal in design. Data were collected from elderly people living in the community who were certified as eligible for care level 2-5 under Japanese long-term care insurance. Continuity in home care was defined as a participant living at home 1 year after the beginning of the study. Results: Of 244 participants, 200 continued to receive home care (82%). Based on a logistic regression analysis predicting continuity in home care, after controlling for gender, age, initial care level, household composition, and daycare service use, having friends was significantly associated with continuity in home care (odds ratio [OR] 2.42; 95% confidence interval [Cl] 1.04-5.65). Participants who lived alone or with a spouse were less likely to continue to receive home care compared with those who lived with others (OR 0.27; 95% Cl 0.08-0.87 and OR 0.18; 95% ClO.06-0.53, respectively). Conclusions: Having friends was a significant predictor of continuity in home care. The promotion of social engagement may be important in preventing institutionalization. [ABSTRACT FROM AUTHOR]

Published
2009
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28. Gender and somatosensory amplification in relation to perceived work stress and social support in Japanese workers.

Author

Nakao M, Tamiya N, and Yano E

Abstract

To examine gender-related differences in somatization among workers, 490 Japanese municipal office employees (248 women) completed the Medical Symptom Checklist, Somatosensory Amplification Scale (SSAS), and Profile of Mood States (POMS), along with questionnaires on their working environment. In women, SSAS scores were positively associated with perceived work stress, and negatively with social support levels (both p < 0.01). Female sex was significantly associated with SSAS scores (p < 0.01), controlling for the effects of total somatic symptom count, POMS tension-anxiety and depression scores, perceived working stress, and social support. The phenomenon of somatosensory amplification might be essential in estimating gender-specific symptoms in a working population. [ABSTRACT FROM AUTHOR]

Published
2005
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34. Chemical taxonomy of the hinge-ligament proteins of bivalves according to their amino acid compositions

Author

Kikuchi, Y and Tamiya, N

Abstract

The proteins in the hinge ligaments of molluscan bivalves were subjected to chemotaxonomic studies according to their amino acid compositions. The hinge-ligament protein is a new class of structure proteins, and this is the first attempt to introduce chemical taxonomy into the systematics of bivalves. The hinge-ligament proteins from morphologically close species, namely mactra (superfamily Mactracea) or scallop (family Pectinidae) species, showed high intraspecific homology in their compositions. On the other hand, inconsistent results were obtained with two types of ligament proteins in pearl oyster species (genus Pinctada). The results of our chemotaxonomic analyses were sometimes in good agreement with the morphological classifications and sometimes inconsistent, implying a complicated phylogenetic relationship among the species.

Published
1987
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36. Isolation and amino acid sequence of a short-chain neurotoxin from an Australian elapid snake, Pseudechis australis

Author

Takasaki, C and Tamiya, N

Abstract

A short-chain neurotoxin Pseudechis australis a (toxin Pa a) was isolated from the venom of an Australian elapid snake Pseudechis australis (king brown snake) by sequential chromatography on CM-cellulose, Sephadex G-50 and CM-cellulose columns. Toxin Pa a has an LD50 (intravenous) value of 76 micrograms/kg body wt. in mice and consists of 62 amino acid residues. The amino acid sequence of Pa a shows considerable homology with those of short-chain neurotoxins of elapid snakes, especially of true sea snakes.

Published
1985
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37. The source of oxygen in the reaction catalysed by collagen lysyl hydroxylase

Author

Kikuchi, Y, Suzuki, Y, and Tamiya, N

Abstract

The synthetic peptides (Pro-Pro-Gly)5 and (Ile-Lys-Gly)5-Phe were hydroxylated with collagen prolyl hydroxylase and lysyl hydroxylase in an 18O2 atmosphere. The oxygen atoms in the hydroxy groups of hydroxyproline and hydroxylysine were 87% and 6.5% respectively derived from the atmospheric 18O2. The results are consistent with those reported previously for proline hydroxylation in vivo [Fujimoto & Tamiya (1962) Biochem. J. 84, 333-335; Prockop, Kaplan & Udenfriend (1962) Biochem. Biophys. Res. Commun. 9, 192-196; Fujimoto & Tamiya (1963) Biochem. Biophys. Res. Commun. 10, 498-501; Prockop, Kaplan & Udenfriend (1963) Arch. Biochem. Biophys. 101, 499-503] and in vitro [Cardinale, Rhoads & Udenfriend (1971) Biochem. Biophys. Res. Commun. 43, 537-543] and for lysine hydroxylation in vivo [Fujimoto & Tamiya (1963) Biochem. Biophys. Res. Commun. 10, 498-501]. In view of the similarities of these two oxygenase-type hydroxylation reactions the participation of intermediates is proposed, the oxygen atoms of which are exchangeable with those of water. The atmospheric oxygen atoms incorporated into the intermediate must be equilibrated with water oxygen atoms in the slower lysyl hydroxylase reaction.

Published
1983
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38. Neurotoxins from the venoms of the sea snakes Hydrophis ornatus and Hydrophis lapemoides

Author

Tamiya, N, Maeda, N, and Cogger, H G

Abstract

The main neurotoxic components, toxins Hydrophis ornatus a and Hydrophis lapemoides a, were isolated from the venoms of the sea snakes Hydrophis ornatus and Hydrophis lapemoides respectively. The amino acid sequence of toxin Hydrophis ornatus a was deduced to be identical with that of toxin Astrotia stokesii a [Maeda & Tamiya (1978) Biochem. J. 175, 507-517] on the basis of identity of the tryptic peptide ‘map’ and the amino acid composition of each peptide. The amino acid sequence of toxin Hydrophis lapemoides a was determined mainly on the basis of identity of the amino acid compositions, mobilities on paper electrophoresis and migration positions on paper chromatography of the tryptic peptides with those of other sea-snake toxins whose sequences are known. Both toxins Hydrophis ornatus a and Hydrophis lapemoides a consisted of 60 amino acid residues and there were six amino acid replacements between them. The taxonomy of sea snakes in the Hydrophis ornatus complex has long been confused, and the above snakes were originally assigned to taxa that proved to be inconsistent with the relationships indicated by the neurotoxin amino acid sequences obtained. A subsequent re-examination of the specimens revealed an error in the original identifications and demonstrated the value of the protein amino acid sequences in systematic and phylogenetic studies. The isolation procedure and results of amino acid analysis of the tryptic peptides have been deposited as Supplementary Publication SUP 50121 (8 pages) with the British Library Lending Division, Boston Spa, Wetherby, West Yorkshire LS23 7BQ, U.K., from whom copies may be obtained as indicated in Biochem. J. (1983) 209, 5.

Published
1983
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39. Amino acid sequences of three phospholipases A I, III and IV from the venom of the sea snake Laticauda semifasciata

Author

Nishida, S, Kim, H S, and Tamiya, N

Abstract

Amino acid sequences of three phospholipases A, I, III and IV, from the venom of the sea snake Laticauda semifasciata were elucidated. Each protein consisted of a single chain of 118 amino acid residues, including 14 half-cystine residues. They showed high homology among themselves, and with the other snake-venom phospholipases A and with the enzymes from mammalian pancreas. Phospholipases A III and IV were especially similar to each other, with only four differences out of their 118 amino acid residues. Phospholipase A I contained one tryptophan residue at position 64, which was important for enzymic activity, whereas III and IV did not contain tryptophan residues and their corresponding positions were occupied by leucine residues. The substitution by leucine resulted in a decreased, but definite, phospholipase A activity. The substituted enzymes have a more potent neuromuscular blocking activity. Full experimental details and evidence for the amino acid sequences of the proteins have been deposited as Supplementary Publication SUP 50118 (39 pages) at the British Library Lending Division, Boston Spa, Wetherby, West Yorkshire LS23 7BQ, U.K., from whom copies can be obtained on the terms indicated in Biochem. J.(1981)193,5.

Published
1982
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40. Amino acid sequences of two novel long-chain neurotoxins from the venom of the sea snake Laticauda colubrina

Author

Kim, H S and Tamiya, N

Abstract

From the venom of a population of the sea snake Laticauda colubrina from the Solomon Islands, a neurotoxic component, Laticauda colubrina a (toxin Lc a), was isolated in 16.6% (A280) yield. Similarly, from the venom of a population of L. colubrina from the Philippines, a neurotoxic component, Laticauda colubrina b (toxin Lc b), was obtained in 10.0% (A280) yield. The LD50 values of these toxins were 0.12 microgram/g body wt. on intramuscular injection in mice. Toxins Lc a and Lc b were each composed of molecules containing 69 amino acid residues with eight half-cystine residues. The complete amino acid sequences of these two toxins were elucidated. Toxins Lc a and Lc b are different from each other at five positions of their sequences, namely at positions 31 (Phe/Ser), 32 (Leu/Ile), 33 (Lys/Arg), 50 (Pro/Arg) and 53 (Asp/His) (residues in parentheses give the residues in toxins Lc a and Lc b respectively). Toxins Lc a and Lc b have a novel structure in that they have only four disulphide bridges, although the whole amino acid sequences are homologous to those of other known long-chain neurotoxins. It is remarkable that toxins Lc a and Lc b are not coexistent at the detection error of 6% of the other toxin. Populations of Laticauda colubrina from the Solomon Islands and from the Philippines have either toxin Lc a or toxin Lc b and not both of them.

Published
1982
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41. Isoelectric points of erabutoxins and monoacyl derivatives of erabutoxin b. Estimation of the pK values of amino groups in erabutoxins by using isoelectric-focusing data

Author

UI, N, Takasaki, C, and Tamiya, N

Abstract

The isoelectric points of erabutoxins a, b and c, neurotoxic proteins of a sea snake, Laticauda semifasciata, were determined by density-gradient isoelectric focusing. The same measurement was also made with monoacyl derivatives of erabutoxin b, in which each one of all amino groups had been either acetylated or propionylated. Erabutoxins a and b showed the same isoelectric point at pH 9.68. The values for [1-N alpha-acetyl-arginine]-, [15-N6-acetyl-lysine]-, [27-N6-acetyl-lysine]-, [47-N6-propionyl-lysine]- and [51-N6-acetyl-lysine]-erabutoxin b were at pH 9.52, 9.31, 9.45, 9.22 and 9.09 respectively, being definitely different from each other and lower than the value for the unmodified molecule. The isoelectric point of erabutoxin c, which is [51-asparagine]-erabutoxin b, was the same as that of [51-N6-acetyl-lysine]erabutoxin b. Assuming that no change in pK occurs on monoacylation, the pK values of amino groups in erabutoxin b were calculated from the isoelectric-point data. It is indicated that the pK values of zeta-amino groups differ markedly from each other and that the value of alpha-amino group is anomalously high.

Published
1982
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42. Isolation, properties and amino acid sequences of a phospholipase A2 and its homologue without activity from the venom of a sea snake, Laticauda colubrina, from the Solomon Islands

Author

Takasaki, C, Kimura, S, Kokubun, Y, and Tamiya, N

Abstract

A phospholipase A2, Laticauda colubrina phospholipase A2 II (LcPLA-II), and a phospholipase A2 homologue, Laticauda colubrina phospholipase A2 homologue I (LcPLH-I), were isolated from the venom of the yellow-lipped sea snake, Laticauda colubrina, from the Solomon Islands. LcPLA-II showed phospholipase A2 activity towards egg-yolk phosphatidylcholine (24 mumol/min per mg at optimal conditions at 37 degrees C) and lethal potency (LD50 45 micrograms/kg body wt. intravenously in mice). Both of the activities were lost by treatment with p-bromophenacyl bromide. LcPLH-I showed neither phospholipase A2 activity nor lethal potency at a dose of 4.5 mg/kg body wt. in mice. It was not modified by the treatment with p-bromophenacyl bromide. LcPLA-II and LcPLH-I bound Ca2+ at a 1:1 molar ratio with KCa values of 105 microM and 44 microM at pH 8.0 respectively. Elucidation of the amino acid sequences of these two proteins showed that each protein consisted of a single chain of 118 amino acid residues, including 14 half-cystine residues. The two sequences are different from each other at 22 residues and highly homologous to those from other sources. The essential histidine residue for the phospholipase A2 activity at position 48 is replaced by an asparagine residue in the homologue LcPLH-I. Details of the separation of the peptides obtained by proteinase digestions of LcPLA-II and LcPLA-I and the determination of their amino acid sequences are given in Supplementary Publication SUP 50145 (14 pages), which has been deposited at the British Library Lending Division, Boston Spa, Wetherby, West Yorkshire LS23 7BQ, U.K., from whom copies can be obtained on the terms indicated in Biochem. J. (1988) 249, 5.

Published
1988
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43. Isolation and properties of lysophospholipases from the venom of an Australian elapid snake, Pseudechis australis

Author

Takasaki, C and Tamiya, N

Abstract

Two lysophospholipases were isolated from the venom of an Australian elapid snake (subfamily Acanthophiinae), Pseudechis australis, by sequential chromatography on CM-52 cellulose, Sephadex G-75 and DE-52 cellulose columns. They were very similar to each other. One of them, lysophospholipase I, was obtained as a homodimer, the monomer of which consisted of 123 amino acid residues with seven disulphide bridges. The amino acid composition and the N-terminal amino acid sequence of the enzyme were similar to those of phospholipase A2, Ca2+ was required for its activity and the maximum activity was attained at 2 mM-CaCl2 in the presence of 1 mM-EDTA. The optimum pH was 7.5. Lysophospholipase I hydrolysed lysophosphatidylcholine more rapidly than lysophosphatidylethanolamine. It did not hydrolyse, however, phosphatidylcholine, 1-palmitoylglycerol, tripalmitoylglycerol or p-nitrophenyl acetate. Modification of the enzyme with p-bromophenacyl bromide or 2-nitrophenylsulphenyl chloride suppressed the activity. A strong direct haemolytic activity was exhibited when the lysophospholipase was present together with phospholipase A2.

Published
1982
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44. The amino acid sequence and position of the free thiol group of a short-chain neurotoxin from common-death-adder (Acanthophis antarcticus) venom

Author

Kim, H S and Tamiya, N

Abstract

The amino acid sequence of a short-chain neurotoxin Acanthophis antarcticus c (toxin Aa c) from the venom of an Australian elapid snake, the common death adder (Acanthophis antarcticus, subfamily Acanthophiinae) was elucidated. Toxin Aa c is composed of 62 amino acid residues, including eight half-cystine residues and a cysteine residue. The amino acid sequence of toxin Aa c is homologous with those of other short-chain neurotoxins found in snakes of the family Elapidae, especially with those from snakes of the subfamily Hydrophiinae. The single cysteine residue was located in position 4. Toxin Aa c has a lethal dose (LD50) of 0.08 micrograms/g body weight of mouse on intramuscular injection.

Published
1981
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45. Isolation, properties and amino acid sequence of a long-chain neurotoxin, Acanthophis antarcticus b, from the venom of an Australian snake (the common death adder, Acanthophis antarcticus)

Author

Kim, H S and Tamiya, N

Abstract

The venom of an Australian elapid snake, the common death adder (Acanthophis antarcticus), was chromatographed on a CM-cellulose CM52 column. One of the neurotoxic components, Acanthophis antarcticus b (toxin Aa b) was isolated in about 9.4% (A280) yield. The complete amino acid sequence of toxin Aa b was elucidated. Toxin Aa b is composed of 73 amino acid residues, with ten half-cystine residues, and has a formula weight of 8135. Toxin Aa b has no histidine or methionine residue in its sequence. The amino acid sequence of toxin Aa b is homologous with those of other neurotoxins with known sequences, although it is novel in having a valine residue at its N-terminus and an arginine residue at position-23, where a lysine residue is found in almost all the so-far-known neurotoxins. Irrespective of the latter replacement, the toxin Aa b is fully active, with an LD50 value (in mice) of 0.13 microgram/g body weight on intramuscular injection.

Published
1981
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46. Three neurotoxins from the venom of a sea snake Astrotia stokesii, including two long-chain neurotoxic proteins with amidated C-termini

Author

Maeda, N and Tamiya, N

Abstract

From the venom of a sea snake Astrotia stokesii three neurotoxic components, toxins Astrotia stokesii a, b and c were isolated in 40, 15 and 5% yield by weight respectively of the whole venom. Their LD50 values for 20g mice were 0.13, 0.096 and 0.098 microgram/g body wt. respectively and accounted for almost all the lethal activity of the venom. Their amino acid sequences were determined. Astrotia stokesii a was composed of 60 amino acid residues with nine half-cystine residues and was quite homologous to other sea-snake short-chain neurotoxins in its amino acid sequence. Toxins Astrotia stokesii b and c were composed of 70 and 72 amino acid residues respectively with 10 half-cystine residues. They are the first long-chain neurotoxins with high activity isolated from sea-snake venoms. The C-terminal carboxy groups of toxins b and c were found to be amidated; the amidation is known for some polypeptides, but is novel for a protein. The amide group may make a hydrogen-bond with glutamic acid-39, which replaces a lysine that has so far been found invariably in long-chain neutrotoxins. Astrotia stokesii b and c are also novel in having phenylalanine-25 and isoleucine- or valine-42. The ordinary Tyr-Glu pair, which is observed in X-ray structure [Low, Preston, Sato, Rosen, Searl, Rudko & Richardson (1976) Proc. Natl. Acad. Sci. U.S.A. 73, 2991-2994] and n.m.r.study [Inagaki, Tatsumi, Miyazawa, Hori & Tamiya (1977) Abstr. Int. Congr. Pure Appl. Chem. 26th, p. 336] on erabutoxins may be replaced by a hydrophobic pair. Detailed evidence for the amino acid sequences of the proteins has been deposited as Supplementary Publication SUP 5009o (30 pages) at the British Library Lending Division, Boston Spa, Wetherby, West Yorkshire LS23 7B1, U.K., from whom copies can be obtained on the terms indicated in Biochem. J. (1978) 169, 5.

Published
1978
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47. Preparation and activity of guanidinated or acetylated erabutoxins

Author

Hori, H and Tamiya, N

Abstract

1. Erabutoxins, a, b and c, neurotoxic proteins of a sea snake Lacticauda semifasciata, were guanidinated with O-methylisourea. The amino groups of all the lysine residues and those at the N-termini of the toxins were modified. The lethal activity of the toxins decreased to 50% (erabutoxins a and b) or 17% (erabutoxin c) of the original value on the modification. The c.d. (circular dichroism) maximum at 227 nm of the modified toxins became lower, whereas the whole profile of the c.d. curve remained unchanged. 2. The amino groups of erabutoxin b were acetylated with acetic anhydride. All the five monoacetyl derivatives were isolated from the reaction products by CM-cellulose and Bio-Rex 70 column chromatography. [1-Nalpha-acetylarginine]-, [15-N6-acetyl-lysine]- and [51-N6-acetyl-lysine]-erabutoxin b retained the toxicity of the native toxin, whereas [27-N6-acetyl-lysine] and [47-N6-acetyl-lysine]-erabutoxin b were 17 and 8% active respectively. The overall profile of c.d. spectrum of erabutoxin b remained unchanged on the monoacetylation.

Published
1976
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48. Isolation, properties and amino acid sequences of three neurotoxins from the venom of a sea snake, Aipysurus laevis

Author

Maeda, N and Tamiya, N

Abstract

Aipysurus laevis venom was chromatographed on CM-cellulose and Bio-Rex 70 columns. Three neurotoxic components, toxins Aipysurus laevis a, b and c, were isolated. The toxins a, b and c corresponded to 22, 33 and 21% respectively of the proteins in the original venom, and accounted for almost all the lethal activity of the venom. The three toxins a, b and c were monodisperse on disc electrophoresis at pH4; toxins a and b moved at the same velocity and c a little faster. They were monodisperse also on sodium dodecyl sulphate-polyacrylamide-disc-gel electrophoresis, giving a molecular weight of 7600. The molecular weight of toxin b estimated by gel filtration was 7000. The amino acid sequence analyses of these toxins revealed that they consisted of 60 amino acid residues and that Aipysurus laevis b was [25-methionine, 28-arginine] Aipysurus laevis a. Aipysurus laevis c was [28-lysine] Aipysurus laevis a, the tryptic peptide sequence relying on homology. The LD50 values of these toxins for 20g mice were 0.076 μg/g body wt. They inhibited the acetylcholine-induced contracture but did not affect the CKl-induced contracture of the isolated muscle.

Published
1976
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49. The isolation, properties and amino acid sequence of erabutoxin c, a minor neurotoxic component of the venom of a sea snake Laticauda semifasciata

Author

Tamiya, N. and Abe, H.

Abstract

Erabutoxin c, a minor neurotoxic component of the venom of a sea snake Laticauda semifasciata, was isolated in pure form by repeated column chromatography on CM-cellulose columns. The toxin was crystallizable and monodisperse in rechromatography, disc electrophoresis and isoelectric focusing (isoelectric point, pH9.23–9.25). The molecular weight of the toxin, as estimated by gel filtration, was 7000. The toxin showed the same lethal activity to mice (0.13μg/g body wt., intramuscular injection) and the same effect on isolated frog muscle as erabutoxins a and b, the main toxic components of the venom. The toxin inhibited the acetylcholine contracture but not the potassium chloride contracture of muscle. Erabutoxin c consisted of 62 amino acid residues, containing one fewer lysine and one more histidine than erabutoxin a and one fewer lysine and one more aspartic acid (or asparagine) than erabutoxin b. Erabutoxin c was reduced, S-carboxymethylated and hydrolysed with trypsin. The only fragment different from the corresponding fragments from erabutoxin b was hydrolysed further with pepsin. One of the peptic fragments, which was assumed to have the aspartic acid (or asparagine) residue in question at the C-terminal end, was treated with carboxypeptidase A. The C-terminal residue was found to be an asparagine. It was therefore concluded that erabutoxin c was [51-asparagine]-erabutoxin b.

Published
1972
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50. Synthesis and enzymic hydroxylation of protocollagen model peptide containing a hydroxyproline residue

Author

Kikuchi, Y., Fujimoto, D., and Tamiya, N.

Abstract

1. Two protocollagen model peptides, Z-Gly-Pro-Hyp-Gly-(Pro-Pro-Gly)5 (Z, benzyloxycarbonyl) and AOC-(Pro-Pro-Gly)6 (AOC, tert.-pentyloxycarbonyl), were synthesized and hydroxylated with protocollagen proline hydroxylase. 2. The two model peptides were hydroxylated equally. The results suggest that the hydroxyl group of hydroxyproline contained in the N-terminal region of the peptide has no effect on the enzymic hydroxylation of the model peptide.

Published
1971
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