44 results on '"Mangieri, M"'
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2. An atypical case of sporadic fatal insomnia
- Author
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Priano, L., Giaccone, G., Mangieri, M., Albani, G., Limido, L., Brioschi, A., Pradotto, L., Orsi, L., Mortara, P., Fociani, P., Mauro, A., and Tagliavini, F.
- Subjects
Insomnia -- Research ,Insomnia -- Physiological aspects ,Prion diseases -- Research ,Prion diseases -- Physiological aspects ,Health ,Psychology and mental health - Published
- 2009
3. Poster abstracts
- Author
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Ferrie, J., Shipley, M., Cappuccio, F., Brunner, E., Miller, M., Kumari, M., Marmot, M., Coenen, A., Castillo, J. L., Araya, F., Bustamante, G., Montecino, L., Torres, C., Oporto, S., Gronli, J., Fiske, E., Murison, R., Bjorvatn, B., Sorensen, E., Ursin, R., Portas, C. M., Rajaraman, S., Gribok, A., Wesensten, N., Balkin, T., Reifman, J., Dursunoglu, N., Ozkurt, S., Baser, S., Delen, O., Sarikaya, S., Sadler, P., Mitchell, P., Françon, D., Decobert, M., Herve, B., Richard, A., Griebel, G., Avenet, P., Scatton, B., Fur, G. L., Eckert, D., Jordan, A., Wellman, A., Smith, S., Malhotra, A., White, D., Bruck, D., Thomas, I., Kritikos, A., Oertel, W., Stiasny-Kolster, K., Garcia-Borreguero, D., Poewe, W., Hoegl, B., Kohnen, R., Schollmayer, E., Keffel, J., Trenkwalder, C., Valle, A., Roizenblatt, S., Fregni, F., Boggio, P., Tufik, S., Ward, K., Robertson, L., Palmer, L., Eastwood, P., Hillman, D., Lee, J., Mukherjee, S., de Padova, V., Barbato, G., Ficca, G., Zilli, I., Salzarulo, P., Veldi, M., Hion, T., Vasar, V., Kull, M., Nowak, L., Davis, J., Latzer, Y., Tzischinsky, O., Crowley, S., Carskadon, M., Anca-Herschkovitsch, M., Frey, D., Ortega, J., Wiseman, C., Farley, C., Wright, K., Campbell, A., Neill, A., Spiegel, K., Leproult, R., Tasali, E., Scherberg, N., van Cauter, E., Noradina, A. T., Karim, N. A., Norlinah, I., Raymond, A. A., Sahathevan, R., Hamidon, B., Werth, E., Poryazova, R., Khatami, R., Bassetti, C., Beran, R. G., Ainley, L., Holand, G., Duncan, J., Kinney, H., Davis, B., Hood, B., Frey, S., Schmidt, C., Hofstetter, M., Peigneux, P., Cajochen, C., Hu, W.-P., Li, J.-D., Zhang, C., Boehmer, L., Siegel, J., Zhou, Q.-Y., Sagawa, Y., Kondo, H., Takemura, T., Kanayama, H., Kaneko, Y., Sato, M., Kanbayashi, T., Hishikawa, Y., Shimizu, T., Viola, A., James, L., Schlangen, L., Dijk, D.-J., Andretic, R., Kim, Y.-C., Han, K.-A., Jones, F., Greenspan, R., Sanford, L., Yang, L., Tang, X., Dieter, K., Uta, E., Sven, H., Richard, M., Oyane, N., Pallesen, S., Holsten, F., Inoue, Y., Fujita, M., Emura, N., Kuroda, K., Uchimura, N., Johnston, A., Astbury, J., Kennedy, G., Hoedlmoser, K., Schabus, M., Pecherstorfer, T., Moser, S., Gruber, G., Anderer, P., Klimesch, W., Naidoo, N., Ferber, M., Pack, A., Neu, D., Mairesse, O., Hoffmann, G., Dris, A., Lambrecht, L., Linkowski, P., Verbanck, P., Le Bon, O., Matsuura, N., Yamao, M., Adachi, N., Aritomi, R., Komada, Y., Tanaka, H., Shirakawa, S., Kondoh, H., Takemura, F., Ohnuma, S., Suzuki, M., Uemura, S., Iskra-Golec, I., Smith, L., Thanh, D.-V., Boly, M., Phillips, C., Steven, L., Luxen, A., Maquet, M., Jay, S., Dawson, D., Lamond, N., Basner, M., Fomberstein, K., Dinges, D., Ogawa, K., Nittono, H., Yamazaki, K., Hori, T., Glamann, C., Hornung, O., Hansen, M.-L, Danker-Hopfe, H., Jung, C., Kecklund, G., Anund, A., Peters, B., Åkerstedt, T., Verster, J., Roehrs, T., Mets, M., de Senerpont Domis, L., Olivier, B., Volkerts, E., Knutson, K., Lauderdale, D., Rathouz, P., Christie, M., Chen, L., Bolortuya, Y., Lee, E., Mckenna, J., Mccarley, R., Strecker, R., Tamaki, M., Matsuoka, T., Aritake, S., Suzuki, H., Kuriyama, K., Ozaki, A., Abe, Y., Enomoto, M., Tagaya, H., Mishima, K., Matsuura, M., Uchiyama, M., Lima-Pacheco, E., Davis, K., Sabourin, C., Lortie-Lussier, M., de Koninck, J., van Der Werf, Y., van Der Helm, E., Schoonheim, M., van Someren, E., Tokley, M., Ball, M., Sato, T., Ghilardi, M. F., Moisello, C., Bove, M., Busi, M., Pelosin, E., Tononi, G., Eguchi, N., Sakata, M., Urade, Y., Doe, N., Yoshihara, K., Abe, K., Manabe, Y., Iwatsuki, K., Hayashi, T., Shoji, M., Kamiya, T., Gooley, J., Brainard, G., Rajaratnam, S., Kronauer, R., Czeisler, C., Lockley, S., Phillips, A., Robinson, P., Burgess, H., Revell, V., Eastman, C., Bihari, S., Ramakrishnan, N., Camerino, D., Conway, P. M., Costa, G., Vandewalle, G., Albouy, G., Sterpenich, V., Darsaud, A., Rauchs, G., Berken, P.-Y, Balteau, E., Maquet, P., Tendero, J. A., Domenech, M. P., Isern, F. S., Martínez, C., Roure, N., Sancho, E. E., Moreno, C. R., Silva, M., Marqueze, E. C., Waage, S., Bobko, N., Chernyuk, V., Yavorskiy, Y., Saxvig, I., Sørensen, E., de Mello, M. T., Esteves, A., Teixeira, C., Bittencourt, L. R., Silva, R., Pires, M. L., Mottram, V., Middelton, B., Arendt, J., Amaral, O., Rodrigues, M., Pereira, C., Tavares, I., Baba, K., Honma, S., Honma, K.-I., Yamanaka, Y., Hashimoto, S., Tanahashi, Y., Nishide, S.-Y, Honma, K.-I, Sletten, T., Middleton, B., Lederle, K., Skene, D., Roth, T., Walsh, J., Hogben, A., Ellis, J., Archer, S., von Schantz, M., Chen, N.-H., Wang, P.-C., Chen, C.-W., Lin, Y., Shih, T.-S., Armstrong, S., Redman, J., Stephan, E., David, M., Delanaud, S., Chardon, K., Libert, J.-P., Bach, V., Telliez, F., Reid, K., Jaksa, A., Eisengart, J., Kane, P., Naylor, E., Zee, P., Viola, A. U., de Valck, E., Hofmans, J., Theuns, P., Cluydts, R., Alexander, G., Karel, M., Christina, R., Sohn, I.-K., Cho, I. H., Kim, S. J., Yu, S.-H., Kim, H., Yoo, S. Y., Koh, S.-H., Cho, S.-J., Rotenberg, L., Silva-Costa, A., Griep, R. H., Amely, T., Kennedy, G. A., Pavlis, A., Thompson, B., Pierce, R., Howard, M., Briellmann, R., Venkateswaran, S., Blunden, S., Krawczyk, E., Blake, J., Gururajan, R., Kerr, D., Matuisi, T., Iwasaki, M., Yamasita, N., Iemura, A., Ohya, T., Yanagawa, T., Misa, R., Coleman, G., Conduit, R., Duce, B., Hukins, C., Nyandaiti, Y. W., Bamaki, S., Mohammed, A., Kwajarfa, S., Veeramachaneni, S. P., Murthy, A., Wilson, A., Maul, J., Hall, G., Stick, S., Moseley, L., Gradisar, M., Kurihara, T., Yamamoto, M., Yamamoto, S., Kuranari, M., Sparks, C. B., Bartle, A., Beckert, L., Latham-Smith, F. B., Hilton, J., Whitehead, B., Gulliver, T., Salvini, A., Grahame, S., Swift, M., Laybutt, N., Sharon, D., Mack, C., Hymell, B., Perrine, B., Ideshita, K., Taira, M., Matuo, A., Furutani, M., van Dongen, H., Mott, C., Huang, J.-K., Mollicone, D. J., Mckenzie, F., Dinges, David, Barnes, M., Rochford, P., Churchward, T., O’Donoghue, F., Penzel, T., Fietze, I., Canisius, S., Bekiaris, E., Terrill, P. I., Wilson, S., Suresh, S., Cooper, D., Suzuki, T., Ouchi, K., Moriya, A., Kameyama, K., Takahashi, M., Büttner, A., Rühle, K.-H., Wang, D., Wong, K., Dungan, II, G., Grunstein, R., Davidson, P., Jones, R., Gergely, V., Mashima, K., Miyazaki, S., Tanaka, T., Okawa, M., Yamada, N., Wyner, A., Raizen, D., Galante, R., Ng, A. K., Koh, T. S., Lim, L. L., Puvanendran, K., Peiris, M., Bones, P., Roebuck, T., Ho, S., Szollosi, I., Naughton, M., Williams, G., Parsley, C., Harris, M.-A., Thornton, A., Ruehland, W., Banks, S., Arroyo, S., Carroll, K., Pilmore, J., Stewart, C., Hamilton, G., van Acker, F., Cvetkovic, D., Holland, G., Cosic, I., Tolson, J., Worsnop, C., Cresswell, P., Hart, I., Bouarab, M., Delechelle, E., Drouot, X., Acebo, C., Singh, P., Lakey, T., Schachter, L., Rand, J., Collin, H., Snyder, E., Ma, J., Svetnick, V., Deacon, S., Dana, B., Konstanze, D., Uwe, M., Ingo, F., Thomas, P., Ivar, R., Mackiewicz, M., Shockley, K., Romer, M., Zimmerman, J., Baldwin, D., Jensen, S., Churchill, G., Paigen, B., Imeri, L., Ferrari, L., Bianchi, S., Dossena, S., Garofoli, A., Mangieri, M., Tagliavini, F., Forloni, G., Chiesa, R., Pedrazzoli, M., Pereira, D., Veauny, M., Bodenmann, S., Hohoff, C., Freitag, C., Deckert, J., Rétey, J., Landolt, H.-P., Strohl, K., Price, E., Yamauchi, M., Dostal, J., Feng, P., Han, F., Havekes, R., Novati, A., Hagewoud, R., Barf, P., van Der Borght, K., van Der Zee, E., Meerlo, P., Ruby, P., Caclin, A., Boulet, S., Delpuech, C., Morlet, D., Veasey, S., Aton, S., Jha, S., Coleman, T., Seibt, J., Frank, M., Lack, L., Churches, O., Feng, S. Y. S., Cassaglia, P., Yu, V. Y. H., Walker, A. M., Kohler, M., Kennedy, D., Martin, J., van Den Heuvel, C., Lushington, K., Herron, K., Khurana, C., Sterr, A., Olivadoti, M., Toth, L., Opp, M., Dang-Vu, T., Degueldre, C., Gais, S., Dang-Vu, T. T., Desseilles, M., Philips, C., Chijavadze, E., Babilodze, M., Chkhartishvili, E., Nachkebia, N., Mchedlidze, O., Dzadzamia, S., Griffiths, R., Walker, A., Horovitz, S., Fukunaga, M., Carr, W., Picchioni, D., de Zwart, J., van Gelderen, P., Braun, A., Duyn, J., Hanlon, E. H., Faraguna, U., Vyazovskiy, V., Cirelli, C., Ocampo-Garcés, A., Ibáñez, F., López, S., Vivaldi, E., Torrealba, F., Romanowski, C. P. 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W., Basheer, R., Aizawa, R., Sunahara, H., Abe, S.-I., Iwaki, S., Houjyou, M., Satoh, M., Suda, H., Kheirandish-Gozal, L., Gozal, D., Walker, P., Noa, A., O’Driscoll, D., Ng, M., Yang, J., Davey, M., Anderson, V., Trinder, J., Horne, R., Sands, S., Kelly, V., Sia, K., Edwards, B., Skuza, E., Davidson, M., Berger, P. H. I. L. I. P., Wilkinson, M., Sánchez-Narváez, F., Gutiérrez, R., Camacho, L., Anaya, E., García-Campos, E., Labra, A., Domínguez, G., García-Polo, L., Haro, R., Verginis, N., Nixon, G., Baumert, M., Pamula, Y., Mihai, R., Wawurszak, M., Smith, N., Yiallourou, S., Andrew Ramsden, C., Williamson, B., Blecher, G., Teng, A., Dakin, C. Y. N., Yuil, M., Harris, M., Sadasivam, S., Bennison, J., Galland, B., Dawes, P., Taylor, B., Norman, M., Edwards, N., Harrison, H., Kol, C., Sullivan, C., Valladares, E., Macey, P., Kumar, R., Woo, M., Harper, R., Alger, J., Mcnamara, D., Tang, J., Goh, A., Teoh, O. H., Chiang, W. C., Chay, O. M., Marie Salvini, A., Riben, C., Blanck, A.-S., Marklund, M., Tourneux, P., Cardot, V., Leke, A., Iqbal, S. M., (Gus) Cooper, D., Witmans, M., Rodger, K., Thevasagayam, R., El-Hakim, H., Hill, C. M., Baya, A., Bucks, R., Kirkham, F., Virues-Ortega, J., Baldeweg, T., Paul, A., Hogan, A., Goodwin, J., Silva, G., Kaemingk, K., Sherrill, D., Morgan, W., Fregosi, R., Quan, S., Evans, C., Maclean, J., Waters, K., Fitzsimmons, D., Hayward, P., Fitzgerald, D., Terrill, G., O’Connell, A., Vannan, K., Richardson, H., Poluektov, M., Levin, I., Snegodskaya, M., Kolosova, N., Geppe, N., Nixon, G. 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T., Collins, A., Jerums, G., Hare, D., Panagiotopoulos, S., Weatherhead, B., Bailey, M., Neil, C., Goldsworthy, U., Hill, C., Valencia-Flores, M., Resendiz, M., Juarez, S., Castano, A., Santiago, V., Aguilar, C., Ostrosky, F., Krum, H., Kaye, D., Neves, C., Decio, M., Monteiro, M., Cintra, F., Poyares, D., Viegas, C., Silva, C., Oliveira, H., Peixoto, T., Mikami, A., Watanabe, T., Kumano-Go, T., Adachi, H., Sugita, Y., Takeda, M., Oktay, B., Firat, H., Akbal, E., Ardic, S., Paim, S., Santos, R., Barrreto, A., Whitmore, H., Imperial, J., Temple, K., Rue, A., Hoffman, L., Liljenquist, D., Kazsa, K., Pavasovic, M., Copland, J., Ho, M., Jayamaha, J., Peverill, R., Hii, S., Hensley, M., Rowland, S., Windler, S., Johansson, M., Eriksson, P., Peker, Y., Råstam, L., Lindblad, U., Grote, L., Zou, D., Radlinski, J., Eder, D., Plens, C. M., Garcia Gonzaga, F. M., Farias Sa, P., Franco Oliveira, L. V., Faria Sa, P., Yoon, I.-Y., Chung, S., Hee Lee, C., Kim, J.-W., Faludi, B., Wang, X., Li, Q., Wan, H., Li, M., Pallayova, M., Donic, V., Tomori, Z., Ioacara, S., Olech, T., Mccallum, C., Bowes, M., Bowes, J., Chia, M., Gilbert, S. S., Sajkov, D., Teichtahl, H., Stevenson, I., Cunnington, D., Kalman, J., Szaboova, E., Higami, S., Kryger, M., Higami, Y., Suzuki, C., Kitano, H., Carin, S., Olof, S., Yngve, G., Gösta, B., Carlberg, B., Stenlund, H., Franklin, K. A., Oliveira, A., Vasconcelos, L., Martinez, D., Goncalves, S. C., Gus, M., Silva, E. O. A., Fuchs, S. C., Fuchs, F. D., Li, A., Au, J., Ho, C., Sung, R., Wing, Y., Tada, H., Terada, N., Togawa, K., Nakagawa, Y., Kishida, K., Kihara, S., Hirata, A., Sonoda, M., Nishizawa, H., Nakamura, T., Shimomura, I., Funahashi, T., Andrewartha, P., Sasse, A., Becker, M., Troester, N., Olschewski, H., Lisamayerkard, L., Glos, M., Blau, A., Peter, J.-G., Chesworth, W., Wilson, G., Piper, A., Chuang, L.-P., Lin, S.-W., Wang, C.-J., Li, H.-Y., Chou, Y.-T., Fu, J.-Y., Liao, Y.-F., Tsai, Y.-H., Chan, K., Laks, L., Nishibayashi, M., Miyamoto, M., Miyamoto, T., Hirata, K., Hoever, P., De Haas, S., Chiossi, E., Van Gerven, J., Dingemanse, J., Winkler, J., Cavallaro, M., Narui, K., Kasai, T., Dohl, T., Takaya, H., Kawana, F., Ueno, K., Panjwani, U., Thakur, L., Anand, J. P., Banerjee, P. K., Leigh, M., Paduch, A., Armstrong, J., Sampson, D., Kotajima, F., Mochizuki, T., Lorr, D., Harder, H., Chesworth, M., Becker, H., Abd-Elaty, N. M., Elprince, M., Ismail, N., Elserogi, W., Yeo, A., George, K., Thomson, K., Stadler, D., Bradley, J., Paul, D., Schwartz, A., Hagander, L., Harlid, R., Hultcrantz, E., Haraldsson, P., Cho, J.-G., Narayan, J., Nagarajah, M., Perri, R., Johnson, P., Burgess, K., Chau, N., Mcevoy, R. D., Arnardottir, E. S., Thorleifsdottir, B., Olafsson, I., Gislason, T., Tsuiki, S., Fujimatsu, S., Munezawa, T., Sato, Y., Subedi, P., Ainslie, P., Topor, Z., Whitelaw, W., Chan, M., So, H., Lam, H., Ng, S., Chan, I., Lam, C., Saigusa, H., Higurashi, N., He, Z. M., Cui, X. C., Li, J., Dong, X., Lv, Y., Zhou, M., Han, X., An, P., Wang, L., Macey, P. M., Serber, S., Cross, R., Yan-Go, F., Marshall, M., Rees, D., Lee, S. H., Ho Cho, J. I., Shin, C., Lee, J. Y., Kwon, S. Y., Kim, T.-H., Vedam, H., Barnes, D., Walter, H., Karin, J., Hermann, P., Belyavskiy, E., Galitsyn, P., Arbolishvili, G., Litvin, A., Chazova, I., Mareev, V., Ramar, K., Khan, A., Gay, P., Strömberg, A., Ulander, M., Fridlund, B., Mårtensson, J., Yee, B., Desai, A., Buchanan, P., Crompton, R., Melehan, K., Wong, P., Tee, A., Ng, A., Darendeliler, M. A., Ye, L., Maislin, G., Hurley, S., Mccluskey, S., Weaver, T., Yun, C.-H., Ji, K.-H., Ahn, J. Y., Lee, H.-W., Zhang, X., Yin, K., Zhaofang, G., Chong, L., Navailles, B., Zenou, E., Cheze, L., Pignat, J.-C., Tang, T., Remmers, J., Vasilakos, K., Denotti, A., Gilholme, J., Castronovo, V., Marelli, S., Aloia, M., Fantini, M. L., Kuo, T., Manconi, M., Zucconi, M., Ferini-Strambi, L., Livia Fantini, M., Giarolli, L., Oldani, A., Lee, Y., Trenell, M., Berend, N., Wang, M., Liang, Z., Lei, F., Komada, I., Nishikawa, M., Sriram, K., Mignone, L., Antic, R., Fujiwara, K., Beaudry, M., Gauthier, L., Laforte, M., Lavigne, G., Wylie, P., Orr, W., Grover, S., Geisler, P., Engelke, E., Cossa, G., Veitch, E., Brillante, R., Mcardle, N., Murphy, M., Singh, B., Gain, K., Maguire, C., Mutch, S., Brown, S., Asciuto, T., Newsam, C., Fransson, A., Ísacsson, G., Tsou, M.-C., Hsu, S.-P., Almendros, I., Acerbi, I., Vilaseca, I., Dcruz, O., Vaughn, B., Muenzer, J., Lacassagne, L., Montemayor, T., Roch-Paoli, J., Qian, J., Petocz, P., Chan, M. R., Munro, J., Zimmerman, M., Stanchina, M., Millman, R., Cassel, W., Ploch, T., Loh, A., Koehler, U., Jerrentrup, A., Greulich, T., Doyle, G., Pascoe, T., Jorgensen, G., Baglioni, C., Lombardo, C., Espie, C., Violani, C., Edell-Gustafsson, U., Swahn, E., Ejdeback, J., Tygesen, H., Johansson, A., Neckelmann, D., Hilde Nordhus, I., Zs-Kovács, Á., Vámos, E., Zs-Molnár, M., Maisuradze, L., Gugushvili, J., Darchia, N., Gvilia, I., Lortkipanidze, N., Oniani, N., Wang-Weigand, S., Mayer, G., Roth-Schechter, B., Hsu, S.-C., Yang, C.-M., Liu, C.-Y., Ito, H., Omvik, S., Nordhus, I. H., Farber, R., Scharf, M., Harris-Collazo, R., Pereira, J., Andras, S., Ohayon, M., David, B., Morgan, K., Voorn, T., Vis, J., Kuijer, J., Fortier-Brochu, E., Beaulieu-Bonneau, S., Ivers, H., Morin, C., Beaulieu-Benneau, S., Harris, J., Bartlett, D., Paisley, L., Moncada, S., Toelle, B., Bonnet, M. H., Arand, D., Bonnet, J., Bonnet, M., Doi, Y., Edéll-Gustafsson, U., Strijers, R., Fernando, A., Arroll, B., Warman, G., Funakura, M., Shikano, S., Unemoto, Y., Fujisawa, M., Hong, S.-C., Jeong, J.-H., Shin, Y.-K., Han, J.-H., Lee, S.-P., Lee, J.-H., Mignot, E., Nakajima, T., Hayashida, K., Honda, M., Ardestani, P., Etemadifar, M., Nejadnik, H., Maghzi, A. H., Basiri, K., Ebrahimi, A., Davoodi, M., Peraita-Adrados, R., Vicario, J. L., Shin, H.-B., Marti, I., Carriero, L., Fulda, S., Beitinger, P., Pollmacher, T., Lam, J. S. P., Fong, S. Y. Y., Tang, N. L. S., Ho, C. K. W., Li, A. M. C., Wing, Y. K., Guilleminault, C., Black, J., Wells, C., Kantor, S., Janisiewicz, A., Scammell, T., Tanaka, S., Smith, A., Neufing, P., Gordon, T., Fuller, P., Gompf, H., Pedersen, N., Saper, C., Lu, J., Sasai, T., Donjacour, C., Fronczek, R., Le Cessie, S., Lammers, G. J., van Dijk, J. G., Hayashi-Ogawa, Y., Okuda, M., Lam, V. K.-H., Chen, A. L., Ho, C. K.-W., Wing, Y.-K., Lehrhaft, B., Brilliante, R., van Der Zande, W., Overeem, S., van Dijk, G., Lammers, J. G., Opazo, C. J., Jeong, D.-U., Sung, Y. H., Lyoo, I. K., Takahashi, Y., Murasaki, M., Bloch, K., Jung, H., Dahab, M. M., Campos, T. F., Mccabe, S., Maravic, K., Wiggs, L., Connelly, V., Barnes, J., Saito, Y., Ogawa, M., Murata, M., Nadig, U., Rahman, A., Aritake, K., D’Cruz, O., Suzuki, K., Kaji, Y., Takekawa, H., Nomura, T., Yasui, K., Nakashima, K., Bahammam, A., Rab, M. G., Owais, S., Alsuwat, K., Hamam, K., Zs, M., Boroojerdi, B., Giladi, N., Wood, D., Sherman, D., Chaudhuri, R., Partinen, M., Abdo, F., Bloem, B., Kremer, B., Verbeek, M., Cronlein, T., Mueller, U., Hajak, G., Zulley, J., Namba, K., Li, L., Mtsuura, M., Kaneita, Y., Ohida, T., Cappeliez, B., Moutrier, R., De, S., Dwivedi, S., Chambers, D., Gabbay, E., Watanabe, A., Valle, C., Kauati, A., Watanabe, R., Chediek, F., Botte, S., Azevedo, E., Kempf, J., Cizza, G., Torvik, S., Brancati, G., Smirne, N., Bruni, A., Goff, E., Freilich, S., Malaweera, A., Simonds, A., Mathias, C., Morrell, M., Rinsky, B., Fonarow, G., Gradinger, F. P., Boldt, C., Geyh, S., Stucki, A., Dahlberg, A., Michel, F., Savard, M.-H., Savard, J., Quesnel, C., Hirose, K., Takahara, M., Mizuno, K., Sadachi, H., Nagashima, Y., Yada, Y., Cheung, C.-F., Lau, C., Lai, W., Sin, K., Tam, C., Hellgren, J., Omenaas, E., Gíslason, T., Jögi, R., Franklin, K., Torén, K., Wang, F., Kadono, M., Shigeta, M., Nakazawa, A., Ueda, M., Fukui, M., Hasegawa, G., Yoshikawa, T., de Niet, G., Tiemens, B., Lendemeijer, B., Hutschemaekers, G., Gauthier, A.-K., Chevrette, T., Chevrier, E., Bouvier, H., Parry, B., Meliska, C., Nowakowski, S., Lopez, A., Martinez, F., Sorenson, D., Lien, M. L., Lattova, Z., Maurovich-Horvat, E., Nia, S., Pollmächer, T., Poulin, J., Chouinard, S., Stip, E., Guillem, F., Venne, D., Caouette, M., Lamont, M.-E., Lázár, A., Lázár, Z., Bíró, A., Gyõri, M., Tárnok, Z., Prekop, C., Gádoros, J., Halász, P., Bódizs, R., Okun, M., Hanusa, B., Hall, M., Wisner, K., Pereira, M., Kumar, R. A. J. E. S. H., Macey, P. A. U. L., Woo, M. A. R. Y., Serber, S. T. A. C. Y., Valladares, E. D. W. I. N., Harper, R. E. B. E. C. C. A., Harper, R. O. N. A. L. D., Puttonen, S., Härmä, M., Vahtera, J., Kivimäki, M., Lamarche, L., Hemmeter, U. M., Thum, A., Rocamora, R., Giesler, M., Haag, A., Dodel, R., Krieg, J. C., Shechter, A., L’Esperance, P., Boivin, D. B., Vu, M.-T., and Richards, H.
- Published
- 2007
- Full Text
- View/download PDF
4. A novel phenotype of sporadic Creutzfeldt-Jakob disease
- Author
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Giaccone, G., Di Fede, G., Mangieri, M., Limido, L., Capobianco, R., Suardi, S., Grisoli, M., Binelli, S., Fociani, P., Bugiani, O., and Tagliavini, F.
- Subjects
Creutzfeldt-Jakob disease -- Genetic aspects ,Creutzfeldt-Jakob disease -- Diagnosis ,Creutzfeldt-Jakob disease -- Case studies ,Prions -- Health aspects ,Prions -- Genetic aspects ,Phenotype -- Analysis ,Health ,Psychology and mental health - Published
- 2007
5. Striking alterations of EEG and sleep patterns in transgenic mice expressing a mutant prion protein linked to inherited Creutzfeldt-Jakob disease: P451
- Author
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FERRARI, L., DOSSENA, S., MANGIERI, M., GAROFOLI, A., FORLONI, G., TAGLIAVINI, F., CHIESA, R., and IMERI, L.
- Published
- 2008
6. Atypical tauopathy with massive involvement of the white matter
- Author
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Giaccone, G., Marcon, G., Mangieri, M., Morbin, M., Rossi, G., Fetoni, V., Patriarca, C., Catania, M., Fede, G. D., and Tagliavini, F.
- Published
- 2008
7. Studio clinico, neuropatologico e bio-molecolare della malattia di Creutzfeldt-Jakob associata a mutazione V210I del gene della proteina prionica
- Author
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FOGLIA C, NIGRO M, PUOTI, Gianfranco, PISCOSQUITO G, CANDELARESI P, GARGIULO MG, ANZILOTTI S, DI FEDE G, MANGIERI M, LIMIDO L, GIACCONE G, ROSSI G, TAGLIAVINI F, COTRUFO R., COPPOLA, Cinzia, Foglia, C, Nigro, M, Puoti, Gianfranco, Coppola, Cinzia, Piscosquito, G, Candelaresi, P, Gargiulo, Mg, Anzilotti, S, DI FEDE, G, Mangieri, M, Limido, L, Giaccone, G, Rossi, G, Tagliavini, F, and Cotrufo, R.
- Published
- 2009
8. Experimental Therapy with Quinacrine in Creutzfeldt-Jakob disease
- Author
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PUOTI, Gianfranco, GIACCONE G, TAGLIAVINI F, DE ANGELIS G, DI FEDE G, LIMIDO L, TUCCI C, SCALELLA G, MANGIERI M, BUGIANI O. AND COTRUFO R., Puoti, Gianfranco, Giaccone, G, Tagliavini, F, DE ANGELIS, G, DI FEDE, G, Limido, L, Tucci, C, Scalella, G, Mangieri, M, and Bugiani, O. AND COTRUFO R.
- Published
- 2004
9. Creutzfeldt-Jakob disease (CJD) associated with V210I PRNP mutation: phenotypic and molecular genetic analysis
- Author
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PUOTI, Gianfranco, DI FEDE G, MANGIERI M, LIMIDO L, GIACCONE G, ROSSI G, COTRUFO R, BUGIANI O, TAGLIAVINI F., Puoti, Gianfranco, DI FEDE, G, Mangieri, M, Limido, L, Giaccone, G, Rossi, G, Cotrufo, R, Bugiani, O, and Tagliavini, F.
- Published
- 2003
10. Mutations in MAPT give rise to aneuploidy in animal models of tauopathy
- Author
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Rossi, G, Conconi, D, Panzeri, E, Paoletta, L, Piccoli, E, Ferretti, M, Mangieri, M, Ruggerone, M, Dalpra', L, Tagliavini, F, Tagliavini, F., CONCONI, DONATELLA, PANZERI, ELENA, DALPRA', LEDA, Rossi, G, Conconi, D, Panzeri, E, Paoletta, L, Piccoli, E, Ferretti, M, Mangieri, M, Ruggerone, M, Dalpra', L, Tagliavini, F, Tagliavini, F., CONCONI, DONATELLA, PANZERI, ELENA, and DALPRA', LEDA
- Abstract
Tau is a major microtubule-associated protein in brain neurons. Its misfolding and accumulation cause neurodegenerative diseases characterized by brain atrophy and dementia, named tauopathies. Genetic forms are caused by mutations of microtubule-associated protein tau gene (MAPT). Tau is expressed also in nonneural tissues such as lymphocytes. Tau has been recently recognized as a multifunctional protein, and in particular, some findings supported a role in genome stability. In fact, peripheral cells of patients affected by frontotemporal dementia carrying different MAPT mutations showed structural and numerical chromosome aberrations. The aim of this study was to assess chromosome stability in peripheral cell from two animal models of genetic tauopathy, JNPL3 and PS19 mouse strains expressing the human tau carrying the P301L and P301S mutations, respectively, to confirm the previous data on humans. After demonstrating the presence of mutated tau in spleen, we performed standard cytogenetic analysis of splenic lymphocytes from homozygous and hemizygous JNPL3, hemizygous PS19, and relevant controls. Losses and gains of chromosomes (aneuploidy) were evaluated. We detected a significantly higher level of aneuploidy in JNPL3 and PS19 than in control mice. Moreover, in JNPL3, the aneuploidy was higher in homozygotes than in hemizygotes, demonstrating a gene dose effect, which appeared also to be age independent. Our results show that mutated tau is associated with chromosome instability. It is conceivable to hypothesize that in genetic tauopathies the aneuploidy may be present also in central nervous system, possibly contributing to neurodegeneration.
- Published
- 2014
11. A new function of microtubule-associated protein tau: involvement in chromosome stability
- Author
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Rossi, G, Dalpra', L, Crosti, F, Lissoni, S, Sciacca, F, Catania, M, Di Fede, G, Mangieri, M, Giaccone, G, Croci, D, Tagliavini, F, DALPRA', LEDA, LISSONI, SARA, Sciacca, FL, Tagliavini, F., Rossi, G, Dalpra', L, Crosti, F, Lissoni, S, Sciacca, F, Catania, M, Di Fede, G, Mangieri, M, Giaccone, G, Croci, D, Tagliavini, F, DALPRA', LEDA, LISSONI, SARA, Sciacca, FL, and Tagliavini, F.
- Abstract
Tau is a microtubule-associated protein that promotes assembly and stabilization of cytoskeleton microtubules. It is mostly expressed in neuronal and glial cells but it is also present in non-neural cells such as fibroblasts and lymphocytes. An altered tau produces cytoskeleton pathology resulting in neurodegenerative diseases such as Alzheimer's disease and tauopathies. Tau has been suggested to be a multifunctional protein, due to its localization in different cellular compartments. However its further functions are still unclear. We analyzed the distribution of tau in human skin fibroblasts showing its localization in the nucleus and along mitotic chromosomes. Then, we investigated if an altered tau, such as the P301L mutated protein associated with frontotemporal dementia, could produce nuclear pathology. We found that patients carrying the mutation consistently had several chromosome aberrations in their fibroblasts and lymphocytes: chromosome and chromatid breakages or gaps, aneuploidies, translocations, in addition to chromatin bridges and decondensed chromosomes. Our findings argue for a role of tau in chromosome stability by means of its interaction with both microtubules and chromatin.
- Published
- 2008
12. A novel phenotype of sporadic Creutzfeldt-Jakob disease
- Author
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Giaccone, G, primary, Di Fede, G., additional, Mangieri, M., additional, Limido, L., additional, Capobianco, R., additional, Suardi, S., additional, Grisoli, M., additional, Binelli, S., additional, Fociani, P., additional, Bugiani, O., additional, and Tagliavini, F., additional
- Published
- 2009
- Full Text
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13. A family with Alzheimer disease and strokes associated with A713T mutation of the APP gene
- Author
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Rossi, G., primary, Giaccone, G., additional, Maletta, R., additional, Morbin, M., additional, Capobianco, R., additional, Mangieri, M., additional, Giovagnoli, A. R., additional, Bizzi, A., additional, Tomaino, C., additional, Perri, M., additional, Di Natale, M., additional, Tagliavini, F., additional, Bugiani, O., additional, and Bruni, A. C., additional
- Published
- 2004
- Full Text
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14. Creutzfeldt-Jakob disease with a novel extra-repeat insertional mutation in the PRNP gene
- Author
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Pietrini, V., primary, Puoti, G., additional, Limido, L., additional, Rossi, G., additional, Di Fede, G., additional, Giaccone, G., additional, Mangieri, M., additional, Tedeschi, F., additional, Bondavalli, A., additional, Mancia, D., additional, Bugiani, O., additional, and Tagliavini, F., additional
- Published
- 2003
- Full Text
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15. Creutzfeldt-Jakob disease with a novel extra-repeat insertional mutation in the PRNP gene
- Author
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Vladimiro Pietrini, Puoti, G., Limido, L., Rossi, G., Di Fede, G., Giaccone, G., Mangieri, M., Tedeschi, F., Bondavalli, A., Mancia, D., Bugiani, O., Tagliavini, F., Pietrini, V, Puoti, Gianfranco, Limido, L, Rossi, G, DI FEDE, G, Giaccone, G, Mangieri, M, Tedeschi, F, Bondavalli, A, Mancia, D, Bugiani, O, and Tagliavini, F.
- Subjects
Brain Chemistry ,Male ,Amyloid ,Heterozygote ,Tyrosine 3-Monooxygenase ,Prions ,Homozygote ,Immunoblotting ,Brain ,Electroencephalography ,tau Proteins ,Middle Aged ,Immunohistochemistry ,Polymerase Chain Reaction ,Creutzfeldt-Jakob Syndrome ,Prion Proteins ,14-3-3 Proteins ,Endopeptidases ,Mutation ,Humans ,Neurology (clinical) ,Protein Precursors - Abstract
—The authors investigated two unrelated patients with Creutzfeldt-Jakob disease (CJD) with clinical features of sporadic CJD (sCJD) carrying one extra octapeptide repeat in the prion protein (PrP) gene (PRNP). A synaptic type PrP distribution throughout the cerebral gray matter and plaque-like PrP deposits in the subcortical gray structures were detected immunocytochemically. The different patterns of PrP deposition were associated with distinct types of proteaseresistant PrP, similar to type 1 and type 2 of sCJD. The features suggest that this insertion is a pathogenic mutation.
16. Widespread distribution of PRPres in the brain and in peripheral tissues of an Italian patient with variant Creutzfeldt-Jakob disease (vCJD)
- Author
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Bugiani, O., Giaccone, G., Mangieri, M., Limido, L., Capobianco, R., Suardi, S., Di Fede, G., Carsana, L., Fociani, P., and Fabrizio Tagliavini
17. Experimental transmission of an atypical form of bovine spongiform encephalopathy
- Author
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Tagliavini, F., Capobianco, R., Casalone, C., Miccolo, C., Suardi, S., Mangieri, M., Limido, L., maria grazia bruzzone, Corona, C., Zanusso, G., Monaco, S., and Caramelli, M.
18. Experimental therapy with quinacrine in Creutzfeldt-Jakob disease
- Author
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Puoti, G., giorgio giaccone, Tagliavini, F., Angelis, G., Rossi, R., Limido, L., Tucci, C., Mangieri, M., and Cotrufo, R.
19. Determinants of hospitalization in a cohort of chronic dialysis patients in central Italy
- Author
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Anteo Di Napoli, Pezzotti, P., Di Lallo, D., Tancioni, V., Papini, P., Guasticchi, G., Addessi, M. A., Ajam, M. F., Alfarone, C., Ancarani, E., Baldinelli, G., Balducci, A., Barbera, V., Barone, P., Battista, M. L., Beraldi, M. P., Biagini, M., Boccia, E., Bravi, M., Brunetti, G., Bucciolini, S., Buono, A., Canulla, F., Caschera, M., Casciani, C. U., Castellano, F., Cavarretta, L., Cerulli, N., Cherubini, C., Chiappini, M. G., Colonnelli, R., Costantini, S., Cuzziol, C., D Adamo, G., Bella, E., Cicco, C., Virgiliis, G., Della Grotta, F., Di Giandomenico, W., Di Giulio, S., Di Legge, R., Di Lullo, L., Di Toro, M. R., Esposto, C., Falcone, C., Felicioni, R., Feliziani, C., Ferrazzoli, F., Filippini, A., Fini, R., Firmi, G., Flammini, A., Forte, F., Franceschelli, L., Galiardi, M. S., Gentile, M., Germani, A., Giordano, F., Giustini, A., Hassan, S., Iamundo, V., Iannacci, R., Iorio, L., Jankovic, L., Luciani, G., Manca, S., Mantella, D., Mangieri, M., Mariano, V., Marin, M., Marinelli, A., Marinelli, R., Massa, P., Mauro, L. M., Mauro, M. M., Meschini, L., Mignozzi, M., Militello, A., Misiti, L., Morabito, S., Morosetti, M., Morricone, A., Moscoloni, M., Murrone, P., Nacca, R., Nazzaro, L., Onorato, L., Pace, G., Palumbo, R., Panzieri, G., Paolozzi, G., Paone, A., Parravano, M., Pasquarelli, C., Pelosi, M., Petroni, S., Poggi, A., Polito, P., and Ponzio, R.
20. EXPERIMENTAL TRANMSISSION OF AN ATYPICAL FORM OF BOVINE SPONGIFORM ENCEPHALOPATHY.
- Author
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Tagliavini, F, Capobianco, R, Casalone, C, Miccolo, C, Suardi, S, Mangieri, M, Limido, L, Bruzzone, M G, Corona, C, Zanusso, G, Monaco, S, and Caramelli, M
- Published
- 2005
21. WIDESPREAD DISTRIBUTION OF PRPres IN THE BRAIN AND IN PERIPHERAL TISSUES OF AN ITALIAN PATIENT WITH VARIANT CREUTZFELDT-JAKOB DISEASE (vCJD).
- Author
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Bugiani, O, Giaccone, G, Mangieri, M, Limido, L, Capobianco, R, Suardi, S, Di Fede, G, Carsana, L, Fociani, P, and Tagliavini, F
- Published
- 2004
22. COAGULASE POSITIVE STAPHYLOCOCCI ENUMERATION AND ENTEROTOXINS DETECTION IN MILK AND DAIRY PRODUCTS FROM CENTRAL ITALY.
- Author
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IANNETTI, L., VISCIANO, P., MARFOGLIA, C., IANNITTO, G., PARISCIANI, G., SERICOLA, M., PETRONE, D., MANGIERI, M. S., POMILIO, F., and SCHIRONE, M.
- Subjects
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ENTEROTOXINS , *COAGULASE , *STAPHYLOCOCCUS , *DAIRY products , *LISTS , *CHEESE products , *CHEESE varieties - Abstract
This study aims at enumerating coagulase positive staphylococci (CPS) in 404 samples of milk and dairy products collected in own-checks or during the official controls from different dairy industries located in Central Italy. These microorganisms were enumerated using ISO 6888-2:1999/Amd. 1:2003 and only when they exceeded 105 CFU/g, the presence of any of the seven more common staphylococcal enterotoxins (SEA, SEB, SEC1, SEC2, SEC3, SED and SEE) was also investigated. Own-checks samples resulted always below the detection limit, whereas among those collected by the competent authorities in the framework of official controls, provola (100%) and mozzarella (22.9%) samples were positive to CPS, with mean values of 1.8x102 and 2.8x105 CFU/g respectively. Such values exceeded the maximum limits set by Commission Regulation (EC) No. 2073/2005, resulting in a request of hygiene improvements in the first case; in the second case, the presence of staphylococcal enterotoxins in 8 (2.7%) mozzarella samples out of 298 investigated cheese products was also observed, resulting in their withdrawn from the market. Therefore, this study aims at highlighting that monitoring of CPS incidence in dairy products and subsequent testing of cheeses for enterotoxins when appropriate represent an important tool for public health in order to avoid the occurrence of foodborne outbreaks. [ABSTRACT FROM AUTHOR]
- Published
- 2019
23. Sporadic Creutzfeldt-Jakob disease: the extent of microglia activation is dependent on the biochemical type of PrPSc
- Author
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Raffaella Capobianco, Giacomina Rossi, Silvia Suardi, Graziella Filippini, Roberto Cotrufo, Pietro Zerbi, Giuseppe Di Fede, Paolo Fociani, Michela Mangieri, Lucia Limido, Fabrizio Tagliavini, Gianfranco Puoti, Gabriella Marcon, Orso Bugiani, Giorgio Giaccone, Selina Iussich, Puoti, Gianfranco, Giaccone, G., Mangieri, M., Limido, L., Fociani, P., Zerbi, P., Suardi, S., Rossi, G., Iussich, S., Capobianco, R., DI FEDE, G., Marcon, G., Cotrufo, R., Filippini, G., Bugiani, O., Tagliavini, F., Puoti, G, Giaccone, G, Mangieri, M, Limido, L, Fociani, P, Zerbi, P, Suardi, S, Rossi, G, Iussich, S, Capobianco, R, DI FEDE, G, Marcon, Gabriella, Cotrufo, R, Filippini, G, and Bugiani, O
- Subjects
Adult ,Male ,Pathology ,medicine.medical_specialty ,Programmed cell death ,PrPSc Proteins ,animal diseases ,Blotting, Western ,Neuropathology ,Biology ,Creutzfeldt-Jakob Syndrome ,Pathology and Forensic Medicine ,Cellular and Molecular Neuroscience ,Degenerative disease ,medicine ,Humans ,Protein Isoforms ,Aged ,Aged, 80 and over ,Microglia ,Genetic heterogeneity ,General Medicine ,Middle Aged ,medicine.disease ,Immunohistochemistry ,Creutzfeldt-Jakob disease ,nervous system diseases ,Blot ,medicine.anatomical_structure ,nervous system ,Neurology ,Prion protein ,Western blot analysis ,Neuroglia ,Female ,Neurology (clinical) - Abstract
In prion-related encephalopathies, microglial activation occurs early and is dependent on accumulation of disease-specific forms of the prion protein (PrPSc) and may play a role in nerve cell death. Previously, we found that different types of PrPSc (i.e. type 1 and type 2) coexisted in approximately 25% of patients with sporadic Creutzfeldt-Jakob disease (CJD); and a close relationship was detected between PrPSc type, the pattern of PrP immunoreactivity, and extent of spongiform degeneration. To investigate whether microglial reaction is related to the biochemical type and deposition pattern of PrPSc, we carried out a neuropathologic and biochemical study on 26 patients with sporadic CJD, including all possible genotypes at codon 129 of the prion protein gene. By quantitative analysis, we demonstrated that strong microglial activation was associated with type 1 PrPSc and diffuse PrP immunoreactivity, whereas type 2 PrPSc and focal PrP deposits were accompanied by mild microglia reaction. These findings support the view that the phenotypic heterogeneity of sporadic CJD is largely determined by the physicochemical properties of distinct PrPSc conformers.
- Published
- 2005
24. Mutations in MAPT give rise to aneuploidy in animal models of tauopathy
- Author
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Donatella Conconi, Michela Mangieri, Laura Paoletta, Leda Dalprà, Fabrizio Tagliavini, Elena Panzeri, Maria Giulia Ferretti, Giacomina Rossi, Margherita Ruggerone, Elena Piccoli, Rossi, G, Conconi, D, Panzeri, E, Paoletta, L, Piccoli, E, Ferretti, M, Mangieri, M, Ruggerone, M, Dalpra', L, and Tagliavini, F
- Subjects
medicine.medical_specialty ,Tau protein ,Gene Dosage ,Aneuploidy ,Mice, Transgenic ,tau Proteins ,Biology ,medicine.disease_cause ,Cellular and Molecular Neuroscience ,Cytogenetics ,Mice ,Chromosome instability ,Genetics ,medicine ,MAPT ,Animals ,Humans ,Genetics(clinical) ,Lymphocytes ,Genetics (clinical) ,Hemizygote ,Mutation ,Genome ,Neurodegeneration ,Homozygote ,Chromosome Mapping ,Karyotype ,medicine.disease ,Animal models ,Tauopathy ,Disease Models, Animal ,Gene Expression Regulation ,Tauopathies ,Karyotyping ,biology.protein ,Original Article ,Tau ,Tau, MAPT, Mutation, Tauopathy, Animal, models, Cytogenetics, Aneuploidy ,Spleen - Abstract
Tau is a major microtubule-associated protein in brain neurons. Its misfolding and accumulation cause neurodegenerative diseases characterized by brain atrophy and dementia, named tauopathies. Genetic forms are caused by mutations of microtubule-associated protein tau gene (MAPT). Tau is expressed also in nonneural tissues such as lymphocytes. Tau has been recently recognized as a multifunctional protein, and in particular, some findings supported a role in genome stability. In fact, peripheral cells of patients affected by frontotemporal dementia carrying different MAPT mutations showed structural and numerical chromosome aberrations. The aim of this study was to assess chromosome stability in peripheral cell from two animal models of genetic tauopathy, JNPL3 and PS19 mouse strains expressing the human tau carrying the P301L and P301S mutations, respectively, to confirm the previous data on humans. After demonstrating the presence of mutated tau in spleen, we performed standard cytogenetic analysis of splenic lymphocytes from homozygous and hemizygous JNPL3, hemizygous PS19, and relevant controls. Losses and gains of chromosomes (aneuploidy) were evaluated. We detected a significantly higher level of aneuploidy in JNPL3 and PS19 than in control mice. Moreover, in JNPL3, the aneuploidy was higher in homozygotes than in hemizygotes, demonstrating a gene dose effect, which appeared also to be age independent. Our results show that mutated tau is associated with chromosome instability. It is conceivable to hypothesize that in genetic tauopathies the aneuploidy may be present also in central nervous system, possibly contributing to neurodegeneration.
- Published
- 2013
25. Hereditary cerebral hemorrhage with amyloidosis associated with the E693K mutation of APP
- Author
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Giuseppe Di Fede, Mauro Magoni, Michela Morbin, Fabrizio Tagliavini, Giulia Mazzoleni, Giacomina Rossi, Gianfranco Puoti, Michela Mangieri, Alessandro Padovani, Andrea Salmaggi, Giorgio M. Patruno, Raffaella Capobianco, Alessandro Romorini, Francesco Carella, Chiara Cupidi, Orso Bugiani, Gabriella Marcon, Alberto Bizzi, Annarita Giovagnoli, Giorgio Giaccone, Bugiani, O, Giaccone, G, Rossi, G, Mangieri, M, Capobianco, R, Morbin, M, Mazzoleni, G, Cupidi, C, Marcon, Gabriella, Giovagnoli, A, Bizzi, A, DI FEDE, G, Puoti, G, Carella, F, Salmaggi, A, Romorini, A, Patruno, Gm, Magoni, M, Padovani, A, and Tagliavini, F.
- Subjects
Male ,Pathology ,medicine.medical_specialty ,Subarachnoid hemorrhage ,Genotype ,Apolipoprotein E4 ,Glutamic Acid ,Neuropathology ,Amyloid beta-Protein Precursor ,Gene Frequency ,Arts and Humanities (miscellaneous) ,medicine ,Humans ,Genetic Predisposition to Disease ,Cognitive decline ,Aged ,Cerebral Hemorrhage ,Family Health ,Amyloid beta-Peptides ,business.industry ,Lysine ,Amyloidosis ,Leukoaraiosis ,Autosomal dominant trait ,Middle Aged ,medicine.disease ,Magnetic Resonance Imaging ,Peptide Fragments ,Italy ,Hemosiderin ,Mutation ,Hereditary cerebral hemorrhage with amyloidosis ,Female ,Neurology (clinical) ,business ,Amyloidosis, Familial ,Genome-Wide Association Study - Abstract
Objective To report the clinical, genetic, neuroimaging, and neuropathologic studies of patients with the hereditary cerebral hemorrhage with amyloidosis linked to the APP E693K mutation. Design Case series. Clinical details and laboratory results were collected by direct evaluation and previous medical records. DNA analysis was carried out in several affected subjects and healthy individuals. Neuropathologic examination was performed in 2 subjects. Setting Southern Lombardy, Italy. Patients Individuals with and without amyloidosis in 4 unrelated Italian families (N = 37). Main Outcome Measure Genotype-phenotype relationship. Results The affected individuals presented with recurrent headache and multiple strokes, followed by epilepsy and cognitive decline in most of them. The disease was inherited with an autosomal dominant trait and segregated with the APP E693K mutation. Neuroimaging demonstrated small to large hematomas, subarachnoid bleeding, scars with hemosiderin deposits, small infarcts, and leukoaraiosis. Amyloid-β immunoreactivity was detected in the wall of leptomeningeal and parenchymal vessels and in the neuropil, whereas phosphorylated tau, neurofibrillary changes, and neuritic plaques were absent. Conclusions These findings expand the number of APP mutations linked to hereditary cerebral hemorrhage with amyloidosis, reinforcing the link between this phenotype and codon 693 of APP .
- Published
- 2010
26. A new function of microtubule-associated protein tau: involvement in chromosome stability
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Marcella Catania, Giuseppe Di Fede, Leda Dalprà, Giacomina Rossi, Fabrizio Tagliavini, Sara Lissoni, Michela Mangieri, Francesca L. Sciacca, Francesca Crosti, Danilo Croci, Giorgio Giaccone, Rossi, G, Dalpra', L, Crosti, F, Lissoni, S, Sciacca, F, Catania, M, Di Fede, G, Mangieri, M, Giaccone, G, Croci, D, and Tagliavini, F
- Subjects
Mitosis ,tau Proteins ,Chromosomal translocation ,Microtubule ,Biology ,Chromosome ,Microtubules ,Chromosomal Instability ,Chromosome instability ,mental disorders ,medicine ,Chromosomes, Human ,Humans ,Molecular Biology ,Cells, Cultured ,Cell Nucleus ,Chromosome Aberrations ,Cell Biology ,Fibroblasts ,Middle Aged ,medicine.disease ,Mitosi ,Molecular biology ,Chromatin ,Cell biology ,Cell nucleus ,Tauopathy ,medicine.anatomical_structure ,Mutation ,Dementia ,Chromatid ,P301L tau mutation ,Tau ,Developmental Biology - Abstract
Tau is a microtubule-associated protein that promotes assembly and stabilization of cytoskeleton microtubules. It is mostly expressed in neuronal and glial cells but it is also present in non-neural cells such as fibroblasts and lymphocytes. An altered tau produces cytoskeleton pathology resulting in neurodegenerative diseases such as Alzheimer's disease and tauopathies. Tau has been suggested to be a multifunctional protein, due to its localization in different cellular compartments. However its further functions are still unclear. We analyzed the distribution of tau in human skin fibroblasts showing its localization in the nucleus and along mitotic chromosomes. Then, we investigated if an altered tau, such as the P301L mutated protein associated with frontotemporal dementia, could produce nuclear pathology. We found that patients carrying the mutation consistently had several chromosome aberrations in their fibroblasts and lymphocytes: chromosome and chromatid breakages or gaps, aneuploidies, translocations, in addition to chromatin bridges and decondensed chromosomes. Our findings argue for a role of tau in chromosome stability by means of its interaction with both microtubules and chromatin.
- Published
- 2008
27. Abbiategrasso Brain Bank Protocol for Collecting, Processing and Characterizing Aging Brains.
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Poloni TE, Medici V, Carlos AF, Davin A, Ceretti A, Mangieri M, Cassini P, Vaccaro R, Zaccaria D, Abbondanza S, Bordoni M, Fantini V, Fogato E, Cereda C, Ceroni M, and Guaita A
- Subjects
- Aged, Brain pathology, Humans, Neurodegenerative Diseases pathology, Aging pathology, Brain cytology, Specimen Handling methods, Tissue Banks
- Abstract
In a constantly aging population, the prevalence of neurodegenerative disorders is expected to rise. Understanding disease mechanisms is the key to find preventive and curative measures. The most effective way to achieve this is through direct examination of diseased and healthy brain tissue. The authors present a protocol to obtain, process, characterize and store good quality brain tissue donated by individuals registered in an antemortem brain donation program. The donation program includes a face-to-face empathic approach to people, a collection of complementary clinical, biological, social and lifestyle information and serial multi-dimensional assessments over time to track individual trajectories of normal aging and cognitive decline. Since many neurological diseases are asymmetrical, our brain bank offers a unique protocol for slicing fresh specimens. Brain sections of both hemispheres are alternately frozen (at -80 °C) or fixed in formalin; a fixed slice on one hemisphere corresponds to a frozen one on the other hemisphere. With this approach, a complete histological characterization of all frozen material can be obtained, and omics studies can be performed on histologically well-defined tissues from both hemispheres thus offering a more complete assessment of neurodegenerative disease mechanisms. Correct and definite diagnosis of these diseases can only be achieved by combining the clinical syndrome with the neuropathological evaluation, which often adds important etiological clues necessary to interpret the pathogenesis. This method can be time consuming, expensive and limited as it only covers a limited geographical area. Regardless of its limitations, the high degree of characterization it provides can be rewarding. Our ultimate goal is to establish the first Italian Brain Bank, all the while emphasizing the importance of neuropathologically verified epidemiological studies.
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- 2020
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28. "Malignant" foot drop: Enzinger epithelioid sarcoma of the common fibular nerve.
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Poloni TE, Alimehmeti R, Galli A, Gambini S, Mangieri M, and Ceroni M
- Subjects
- Humans, Keratins metabolism, Magnetic Resonance Imaging, Male, Middle Aged, Peripheral Nervous System Neoplasms diagnostic imaging, Peroneal Nerve diagnostic imaging, Peroneal Nerve pathology, Peroneal Nerve physiopathology, Sarcoma diagnostic imaging, Gait Disorders, Neurologic etiology, Peripheral Nervous System Neoplasms complications, Sarcoma complications
- Published
- 2016
- Full Text
- View/download PDF
29. High homocysteine and epistasis between MTHFR and APOE: association with cognitive performance in the elderly.
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Polito L, Poloni TE, Vaccaro R, Abbondanza S, Mangieri M, Davin A, Villani S, and Guaita A
- Subjects
- Age Factors, Aged, Aging blood, Aging psychology, Biomarkers blood, Cognition Disorders blood, Cognition Disorders diagnosis, Cognition Disorders psychology, Cross-Sectional Studies, Executive Function, Female, Gene Frequency, Genetic Association Studies, Genetic Predisposition to Disease, Geriatric Assessment, Humans, Hyperhomocysteinemia blood, Hyperhomocysteinemia diagnosis, Hyperhomocysteinemia psychology, Male, Memory, Neuropsychological Tests, Phenotype, Principal Component Analysis, Risk Factors, Up-Regulation, Aging genetics, Apolipoproteins E genetics, Cognition, Cognition Disorders genetics, Epistasis, Genetic, Homocysteine blood, Hyperhomocysteinemia genetics, Methylenetetrahydrofolate Reductase (NADPH2) genetics, Polymorphism, Genetic
- Abstract
High total homocysteine (tHcy) is associated with cognitive impairment in the elderly. The impact of high tHcy on different cognitive domains deserves further investigation, as does the role of the C677T polymorphism of the 5,10 methylenetetrahydrofolate reductase (MTHFR) gene. A cross-sectional analysis of 903 subjects from the population-based "InveCe.Ab" study was performed. The participants had no psychosis or active neurological disorders. They underwent a neuropsychological assessment. Principal component analysis allowed cognitive performance to be condensed into two components: executive functions and memory. Novel components were evaluated for association with tHcy, controlling for potential confounders. Regression models showed that high serum tHcy was associated with lower executive functions, but not with memory. MTHFR C677T TT was associated with higher tHcy but did not affect cognitive performance per se. However, when combined with the apolipoprotein E (APOE)-ε4 allele, it was a risk factor for lower executive performance, independently of tHcy levels. In summary, high tHcy per se, or MTHFR C677T TT in combination with the APOE-ε4 allele, might be associated primarily with executive dysfunctions rather than memory loss., (Copyright © 2015 Elsevier Inc. All rights reserved.)
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- 2016
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30. Transgenic fatal familial insomnia mice indicate prion infectivity-independent mechanisms of pathogenesis and phenotypic expression of disease.
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Bouybayoune I, Mantovani S, Del Gallo F, Bertani I, Restelli E, Comerio L, Tapella L, Baracchi F, Fernández-Borges N, Mangieri M, Bisighini C, Beznoussenko GV, Paladini A, Balducci C, Micotti E, Forloni G, Castilla J, Fiordaliso F, Tagliavini F, Imeri L, and Chiesa R
- Subjects
- Animals, Brain pathology, Brain physiopathology, Disease Models, Animal, Electroencephalography, Magnetic Resonance Imaging, Maze Learning, Mice, Mice, Inbred C57BL, Mice, Transgenic, Microscopy, Electron, Transmission, Mutation, Phenotype, Prion Proteins, Insomnia, Fatal Familial genetics, Insomnia, Fatal Familial physiopathology, Prions genetics
- Abstract
Fatal familial insomnia (FFI) and a genetic form of Creutzfeldt-Jakob disease (CJD178) are clinically different prion disorders linked to the D178N prion protein (PrP) mutation. The disease phenotype is determined by the 129 M/V polymorphism on the mutant allele, which is thought to influence D178N PrP misfolding, leading to the formation of distinctive prion strains with specific neurotoxic properties. However, the mechanism by which misfolded variants of mutant PrP cause different diseases is not known. We generated transgenic (Tg) mice expressing the mouse PrP homolog of the FFI mutation. These mice synthesize a misfolded form of mutant PrP in their brains and develop a neurological illness with severe sleep disruption, highly reminiscent of FFI and different from that of analogously generated Tg(CJD) mice modeling CJD178. No prion infectivity was detectable in Tg(FFI) and Tg(CJD) brains by bioassay or protein misfolding cyclic amplification, indicating that mutant PrP has disease-encoding properties that do not depend on its ability to propagate its misfolded conformation. Tg(FFI) and Tg(CJD) neurons have different patterns of intracellular PrP accumulation associated with distinct morphological abnormalities of the endoplasmic reticulum and Golgi, suggesting that mutation-specific alterations of secretory transport may contribute to the disease phenotype.
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- 2015
- Full Text
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31. Mutations in MAPT give rise to aneuploidy in animal models of tauopathy.
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Rossi G, Conconi D, Panzeri E, Paoletta L, Piccoli E, Ferretti MG, Mangieri M, Ruggerone M, Dalprà L, and Tagliavini F
- Subjects
- Animals, Chromosome Mapping, Gene Dosage, Genome, Hemizygote, Homozygote, Humans, Karyotyping, Lymphocytes cytology, Lymphocytes metabolism, Mice, Mice, Transgenic, Spleen metabolism, Aneuploidy, Disease Models, Animal, Gene Expression Regulation, Mutation, Tauopathies genetics, tau Proteins genetics
- Abstract
Tau is a major microtubule-associated protein in brain neurons. Its misfolding and accumulation cause neurodegenerative diseases characterized by brain atrophy and dementia, named tauopathies. Genetic forms are caused by mutations of microtubule-associated protein tau gene (MAPT). Tau is expressed also in nonneural tissues such as lymphocytes. Tau has been recently recognized as a multifunctional protein, and in particular, some findings supported a role in genome stability. In fact, peripheral cells of patients affected by frontotemporal dementia carrying different MAPT mutations showed structural and numerical chromosome aberrations. The aim of this study was to assess chromosome stability in peripheral cell from two animal models of genetic tauopathy, JNPL3 and PS19 mouse strains expressing the human tau carrying the P301L and P301S mutations, respectively, to confirm the previous data on humans. After demonstrating the presence of mutated tau in spleen, we performed standard cytogenetic analysis of splenic lymphocytes from homozygous and hemizygous JNPL3, hemizygous PS19, and relevant controls. Losses and gains of chromosomes (aneuploidy) were evaluated. We detected a significantly higher level of aneuploidy in JNPL3 and PS19 than in control mice. Moreover, in JNPL3, the aneuploidy was higher in homozygotes than in hemizygotes, demonstrating a gene dose effect, which appeared also to be age independent. Our results show that mutated tau is associated with chromosome instability. It is conceivable to hypothesize that in genetic tauopathies the aneuploidy may be present also in central nervous system, possibly contributing to neurodegeneration.
- Published
- 2014
- Full Text
- View/download PDF
32. Hereditary cerebral hemorrhage with amyloidosis associated with the E693K mutation of APP.
- Author
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Bugiani O, Giaccone G, Rossi G, Mangieri M, Capobianco R, Morbin M, Mazzoleni G, Cupidi C, Marcon G, Giovagnoli A, Bizzi A, Di Fede G, Puoti G, Carella F, Salmaggi A, Romorini A, Patruno GM, Magoni M, Padovani A, and Tagliavini F
- Subjects
- Aged, Amyloid beta-Peptides metabolism, Amyloidosis, Familial complications, Amyloidosis, Familial pathology, Apolipoprotein E4 genetics, Cerebral Hemorrhage complications, Cerebral Hemorrhage pathology, Family Health, Female, Gene Frequency, Genome-Wide Association Study, Genotype, Humans, Italy, Magnetic Resonance Imaging methods, Male, Middle Aged, Peptide Fragments metabolism, Amyloid beta-Protein Precursor genetics, Amyloidosis, Familial genetics, Cerebral Hemorrhage genetics, Genetic Predisposition to Disease genetics, Glutamic Acid genetics, Lysine genetics, Mutation genetics
- Abstract
Objective: To report the clinical, genetic, neuroimaging, and neuropathologic studies of patients with the hereditary cerebral hemorrhage with amyloidosis linked to the APP E693K mutation., Design: Case series. Clinical details and laboratory results were collected by direct evaluation and previous medical records. DNA analysis was carried out in several affected subjects and healthy individuals. Neuropathologic examination was performed in 2 subjects., Setting: Southern Lombardy, Italy. Patients Individuals with and without amyloidosis in 4 unrelated Italian families (N = 37). Main Outcome Measure Genotype-phenotype relationship., Results: The affected individuals presented with recurrent headache and multiple strokes, followed by epilepsy and cognitive decline in most of them. The disease was inherited with an autosomal dominant trait and segregated with the APP E693K mutation. Neuroimaging demonstrated small to large hematomas, subarachnoid bleeding, scars with hemosiderin deposits, small infarcts, and leukoaraiosis. Amyloid-beta immunoreactivity was detected in the wall of leptomeningeal and parenchymal vessels and in the neuropil, whereas phosphorylated tau, neurofibrillary changes, and neuritic plaques were absent., Conclusions: These findings expand the number of APP mutations linked to hereditary cerebral hemorrhage with amyloidosis, reinforcing the link between this phenotype and codon 693 of APP.
- Published
- 2010
- Full Text
- View/download PDF
33. A novel phenotype of sporadic Creutzfeldt-Jakob disease.
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Giaccone G, Di Fede G, Mangieri M, Limido L, Capobianco R, Suardi S, Grisoli M, Binelli S, Fociani P, Bugiani O, and Tagliavini F
- Abstract
An atypical case of sporadic Creutzfeldt-Jakob disease (CJD) is described in a 78-year-old woman homozygous for methionine at codon 129 of the prion protein (PrP) gene. The neuropathological signature was the presence of PrP immunoreactive plaque-like deposits in the cerebral cortex, striatum and thalamus. Western blot analysis showed a profile of the pathological form of PrP (PrP(Sc)) previously unrecognised in sporadic CJD, marked by the absence of diglycosylated protease resistant species. These features define a novel neuropathological and molecular CJD phenotype.
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- 2009
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34. Mutant prion protein expression causes motor and memory deficits and abnormal sleep patterns in a transgenic mouse model.
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Dossena S, Imeri L, Mangieri M, Garofoli A, Ferrari L, Senatore A, Restelli E, Balducci C, Fiordaliso F, Salio M, Bianchi S, Fioriti L, Morbin M, Pincherle A, Marcon G, Villani F, Carli M, Tagliavini F, Forloni G, and Chiesa R
- Subjects
- Animals, Brain pathology, Brain physiopathology, Cerebral Cortex metabolism, Cerebral Cortex pathology, Cerebral Cortex physiopathology, Creutzfeldt-Jakob Syndrome genetics, Creutzfeldt-Jakob Syndrome physiopathology, Disease Models, Animal, Electroencephalography, Endoplasmic Reticulum metabolism, Endoplasmic Reticulum pathology, Energy Metabolism genetics, Evoked Potentials genetics, Memory Disorders metabolism, Memory Disorders physiopathology, Mice, Mice, Inbred C57BL, Mice, Transgenic, Movement Disorders metabolism, Movement Disorders physiopathology, Mutation genetics, Sleep Wake Disorders metabolism, Sleep Wake Disorders physiopathology, Brain metabolism, Creutzfeldt-Jakob Syndrome complications, Memory Disorders genetics, Movement Disorders genetics, Prions genetics, Sleep Wake Disorders genetics
- Abstract
A familial form of Creutzfeldt-Jakob disease (CJD) is linked to the D178N/V129 prion protein (PrP) mutation. Tg(CJD) mice expressing the mouse homolog of this mutant PrP synthesize a misfolded form of the mutant protein, which is aggregated and protease resistant. These mice develop clinical and pathological features reminiscent of CJD, including motor dysfunction, memory impairment, cerebral PrP deposition, and gliosis. Tg(CJD) mice also display electroencephalographic abnormalities and severe alterations of sleep-wake patterns strikingly similar to those seen in a human patient carrying the D178N/V129 mutation. Neurons in these mice show swelling of the endoplasmic reticulum (ER) with intracellular retention of mutant PrP, suggesting that ER dysfunction could contribute to the pathology. These results establish a transgenic animal model of a genetic prion disease recapitulating cognitive, motor, and neurophysiological abnormalities of the human disorder. Tg(CJD) mice have the potential for giving greater insight into the spectrum of neuronal dysfunction in prion diseases.
- Published
- 2008
- Full Text
- View/download PDF
35. A new function of microtubule-associated protein tau: involvement in chromosome stability.
- Author
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Rossi G, Dalprà L, Crosti F, Lissoni S, Sciacca FL, Catania M, Di Fede G, Mangieri M, Giaccone G, Croci D, and Tagliavini F
- Subjects
- Cell Nucleus chemistry, Cells, Cultured, Chromatin ultrastructure, Chromosomal Instability, Chromosomes, Human chemistry, Fibroblasts chemistry, Humans, Microtubules chemistry, Middle Aged, Mitosis, Mutation, tau Proteins analysis, tau Proteins genetics, Chromosome Aberrations, Dementia genetics, tau Proteins physiology
- Abstract
Tau is a microtubule-associated protein that promotes assembly and stabilization of cytoskeleton microtubules. It is mostly expressed in neuronal and glial cells but it is also present in non-neural cells such as fibroblasts and lymphocytes. An altered tau produces cytoskeleton pathology resulting in neurodegenerative diseases such as Alzheimer's disease and tauopathies. Tau has been suggested to be a multifunctional protein, due to its localization in different cellular compartments. However its further functions are still unclear. We analyzed the distribution of tau in human skin fibroblasts showing its localization in the nucleus and along mitotic chromosomes. Then, we investigated if an altered tau, such as the P301L mutated protein associated with frontotemporal dementia, could produce nuclear pathology. We found that patients carrying the mutation consistently had several chromosome aberrations in their fibroblasts and lymphocytes: chromosome and chromatid breakages or gaps, aneuploidies, translocations, in addition to chromatin bridges and decondensed chromosomes. Our findings argue for a role of tau in chromosome stability by means of its interaction with both microtubules and chromatin.
- Published
- 2008
- Full Text
- View/download PDF
36. The efficacy of tetracyclines in peripheral and intracerebral prion infection.
- Author
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De Luigi A, Colombo L, Diomede L, Capobianco R, Mangieri M, Miccolo C, Limido L, Forloni G, Tagliavini F, and Salmona M
- Subjects
- Animals, Cricetinae, Male, Mesocricetus, Brain Diseases drug therapy, Prion Diseases drug therapy, Tetracyclines therapeutic use
- Abstract
We have previously shown that tetracyclines interact with and reverse the protease resistance of pathological prion protein extracted from scrapie-infected animals and patients with all forms of Creutzfeldt-Jakob disease, lowering the prion titre and prolonging survival of cerebrally infected animals. To investigate the effectiveness of these drugs as anti-prion agents Syrian hamsters were inoculated intramuscularly or subcutaneously with 263K scrapie strain at a 10(-4) dilution. Tetracyclines were injected intramuscularly or intraperitoneally at the dose of 10 mg/kg. A single intramuscular dose of doxycycline one hour after infection in the same site of inoculation prolonged median survival by 64%. Intraperitoneal doses of tetracyclines every two days for 40 or 44 days increased survival time by 25% (doxycycline), 32% (tetracycline); and 81% (minocycline) after intramuscular infection, and 35% (doxycycline) after subcutaneous infection. To extend the therapeutic potential of tetracyclines, we investigated the efficacy of direct infusion of tetracyclines in advanced infection. Since intracerebroventricular infusion of tetracycline solutions can cause overt acute toxicity in animals, we entrapped the drugs in liposomes. Animals were inoculated intracerebrally with a 10(-4) dilution of the 263K scrapie strain. A single intracerebroventricular infusion of 25 microg/20 microl of doxycycline or minocycline entrapped in liposomes was administered 60 days after inoculation, when 50% of animals showed initial symptoms of the disease. Median survival increased of 8.1% with doxycycline and 10% with minocycline. These data suggest that tetracyclines might have therapeutic potential for humans.
- Published
- 2008
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37. Conversion of the BASE prion strain into the BSE strain: the origin of BSE?
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Capobianco R, Casalone C, Suardi S, Mangieri M, Miccolo C, Limido L, Catania M, Rossi G, Di Fede G, Giaccone G, Bruzzone MG, Minati L, Corona C, Acutis P, Gelmetti D, Lombardi G, Groschup MH, Buschmann A, Zanusso G, Monaco S, Caramelli M, and Tagliavini F
- Subjects
- Animals, Brain metabolism, Cattle, Encephalopathy, Bovine Spongiform classification, Mice, Mice, Inbred C57BL, Mice, Transgenic, PrPC Proteins metabolism, PrPSc Proteins metabolism, Encephalopathy, Bovine Spongiform etiology, Encephalopathy, Bovine Spongiform transmission, PrPC Proteins isolation & purification, PrPSc Proteins isolation & purification
- Abstract
Atypical neuropathological and molecular phenotypes of bovine spongiform encephalopathy (BSE) have recently been identified in different countries. One of these phenotypes, named bovine "amyloidotic" spongiform encephalopathy (BASE), differs from classical BSE for the occurrence of a distinct type of the disease-associated prion protein (PrP), termed PrP(Sc), and the presence of PrP amyloid plaques. Here, we show that the agents responsible for BSE and BASE possess different biological properties upon transmission to transgenic mice expressing bovine PrP and inbred lines of nontransgenic mice. Strikingly, serial passages of the BASE strain to nontransgenic mice induced a neuropathological and molecular disease phenotype indistinguishable from that of BSE-infected mice. The existence of more than one agent associated with prion disease in cattle and the ability of the BASE strain to convert into the BSE strain may have important implications with respect to the origin of BSE and spongiform encephalopathies in other species, including humans.
- Published
- 2007
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38. The epsilon isoform of 14-3-3 protein is a component of the prion protein amyloid deposits of Gerstmann-Sträussler-Scheinker disease.
- Author
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Di Fede G, Giaccone G, Limido L, Mangieri M, Suardi S, Puoti G, Morbin M, Mazzoleni G, Ghetti B, and Tagliavini F
- Subjects
- 14-3-3 Proteins analysis, 14-3-3 Proteins immunology, Antibody Specificity, Biomarkers analysis, Biomarkers metabolism, Brain pathology, Brain physiopathology, Creutzfeldt-Jakob Syndrome pathology, Creutzfeldt-Jakob Syndrome physiopathology, Diagnosis, Differential, Gerstmann-Straussler-Scheinker Disease pathology, Gerstmann-Straussler-Scheinker Disease physiopathology, Humans, Immunohistochemistry, Neurons metabolism, Neurons pathology, Plaque, Amyloid pathology, Predictive Value of Tests, 14-3-3 Proteins metabolism, Brain metabolism, Creutzfeldt-Jakob Syndrome metabolism, Gerstmann-Straussler-Scheinker Disease metabolism, Plaque, Amyloid metabolism, Prions metabolism
- Abstract
The 14-3-3 proteins are highly conserved, ubiquitous molecules involved in a variety of biologic events, such as transduction pathway modulation, cell cycle control, and apoptosis. Seven isoforms have been identified that are abundant in the brain, preferentially localized in neurons. Remarkable increases in 14-3-3 are seen in the cerebrospinal fluid of patients with Creutzfeldt-Jakob disease (CJD), and it has been found in pathologic inclusions of several neurodegenerative diseases. Moreover, the zeta isoform has been detected in prion protein (PrP) amyloid deposits of CJD patients. To further investigate the cerebral distribution of 14-3-3 in prion-related encephalopathies, we carried out an immunohistochemical and biochemical analysis of brain tissue from patients with Gerstmann-Sträussler-Scheinker disease (GSS) and sporadic, familial and acquired forms of CJD, using specific antibodies against the seven 14-3-3 isoforms. The study showed a strong immunoreactivity of PrP amyloid plaques of GSS patients for the 14-3-3 epsilon isoform, but not for the other isoforms. The epsilon isoform of 14-3-3 was not found in PrP deposits of CJD. These results indicate that the epsilon isoform of 14-3-3 is a component of PrP amyloid deposits of GSS and suggest that this is the sole 14-3-3 isoform specifically involved in the neuropathologic changes associated with this disorder.
- Published
- 2007
- Full Text
- View/download PDF
39. Pathologic prion protein is specifically recognized in situ by a novel PrP conformational antibody.
- Author
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Moroncini G, Mangieri M, Morbin M, Mazzoleni G, Ghetti B, Gabrielli A, Williamson RA, Giaccone G, and Tagliavini F
- Subjects
- Amino Acid Motifs immunology, Antibodies chemistry, Artifacts, Brain metabolism, Brain physiopathology, Cross Reactions immunology, Humans, Immunohistochemistry trends, Plaque, Amyloid immunology, PrPSc Proteins analysis, PrPSc Proteins metabolism, Predictive Value of Tests, Prion Diseases immunology, Prion Diseases physiopathology, Protein Conformation, Antibodies immunology, Antibody Specificity immunology, Brain immunology, Immunohistochemistry methods, PrPSc Proteins immunology, Prion Diseases diagnosis
- Abstract
Prion diseases are characterized by the accumulation in the brain of abnormal conformers (PrP(Sc)) of the cellular prion protein (PrP(C)). PrP(Sc) immunohistochemistry, currently based on antibodies non-distinguishing between PrP(C) and PrP(Sc), requires pre-treatments of histological sections to eliminate PrP(C) and to denature PrP(Sc). We employed the PrP(Sc)-specific antibody 89-112 PrP motif-grafted IgG on mildly fixed, untreated brain sections from several cases of human prion diseases. The results confirmed specific binding of IgG 89-112 to a structural determinant found exclusively on native disease-associated PrP conformations and lost following tissue denaturation or cross-linking fixation. Importantly, IgG 89-112 demonstrated no reactivity with normal brain tissue or with amyloid deposits in Alzheimer disease brain sections. Thus, immunohistochemical detection of native PrP(Sc) deposits was obtained by means of a PrP(Sc)-specific antibody. Such unique reagent may have many applications in the study of prion biology and in the diagnosis and prevention of prion diseases.
- Published
- 2006
- Full Text
- View/download PDF
40. Defective tumor necrosis factor-alpha-dependent control of astrocyte glutamate release in a transgenic mouse model of Alzheimer disease.
- Author
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Rossi D, Brambilla L, Valori CF, Crugnola A, Giaccone G, Capobianco R, Mangieri M, Kingston AE, Bloc A, Bezzi P, and Volterra A
- Subjects
- Alzheimer Disease pathology, Amyloid beta-Peptides metabolism, Animals, Base Sequence, DNA Primers, Gliosis, Hippocampus metabolism, Hippocampus pathology, Immunohistochemistry, Mice, Mice, Transgenic, Signal Transduction, Alzheimer Disease metabolism, Astrocytes metabolism, Disease Models, Animal, Glutamic Acid metabolism, Tumor Necrosis Factor-alpha physiology
- Abstract
The cytokine tumor necrosis factor-alpha (TNFalpha) induces Ca2+-dependent glutamate release from astrocytes via the downstream action of prostaglandin (PG) E2. By this process, astrocytes may participate in intercellular communication and neuromodulation. Acute inflammation in vitro, induced by adding reactive microglia to astrocyte cultures, enhances TNFalpha production and amplifies glutamate release, switching the pathway into a neurodamaging cascade (Bezzi, P., Domercq, M., Brambilla, L., Galli, R., Schols, D., De Clercq, E., Vescovi, A., Bagetta, G., Kollias, G., Meldolesi, J., and Volterra, A. (2001) Nat. Neurosci. 4, 702-710). Because glial inflammation is a component of Alzheimer disease (AD) and TNFalpha is overexpressed in AD brains, we investigated possible alterations of the cytokine-dependent pathway in PDAPP mice, a transgenic model of AD. Glutamate release was measured in acute hippocampal and cerebellar slices from mice at early (4-month-old) and late (12-month-old) disease stages in comparison with age-matched controls. Surprisingly, TNFalpha-evoked glutamate release, normal in 4-month-old PDAPP mice, was dramatically reduced in the hippocampus of 12-month-old animals. This defect correlated with the presence of numerous beta-amyloid deposits and hypertrophic astrocytes. In contrast, release was normal in cerebellum, a region devoid of beta-amyloid deposition and astrocytosis. The Ca2+-dependent process by which TNFalpha evokes glutamate release in acute slices is distinct from synaptic release and displays properties identical to those observed in cultured astrocytes, notably PG dependence. However, prostaglandin E2 induced normal glutamate release responses in 12-month-old PDAPP mice, suggesting that the pathology-associated defect involves the TNFalpha-dependent control of secretion rather than the secretory process itself. Reduced expression of DENN/MADD, a mediator of TNFalpha-PG coupling, might account for the defect. Alteration of this neuromodulatory astrocytic pathway is described here for the first time in relation to Alzheimer disease.
- Published
- 2005
- Full Text
- View/download PDF
41. Sporadic Creutzfeldt-Jakob disease: the extent of microglia activation is dependent on the biochemical type of PrPSc.
- Author
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Puoti G, Giaccone G, Mangieri M, Limido L, Fociani P, Zerbi P, Suardi S, Rossi G, Iussich S, Capobianco R, Di Fede G, Marcon G, Cotrufo R, Filippini G, Bugiani O, and Tagliavini F
- Subjects
- Adult, Aged, Aged, 80 and over, Blotting, Western, Creutzfeldt-Jakob Syndrome metabolism, Creutzfeldt-Jakob Syndrome pathology, Female, Humans, Immunohistochemistry, Male, Middle Aged, Protein Isoforms metabolism, Creutzfeldt-Jakob Syndrome physiopathology, Microglia pathology, PrPSc Proteins metabolism
- Abstract
In prion-related encephalopathies, microglial activation occurs early and is dependent on accumulation of disease-specific forms of the prion protein (PrPSc) and may play a role in nerve cell death. Previously, we found that different types of PrPSc (i.e. type 1 and type 2) coexisted in approximately 25% of patients with sporadic Creutzfeldt-Jakob disease (CJD); and a close relationship was detected between PrPSc type, the pattern of PrP immunoreactivity, and extent of spongiform degeneration. To investigate whether microglial reaction is related to the biochemical type and deposition pattern of PrPSc, we carried out a neuropathologic and biochemical study on 26 patients with sporadic CJD, including all possible genotypes at codon 129 of the prion protein gene. By quantitative analysis, we demonstrated that strong microglial activation was associated with type 1 PrPSc and diffuse PrP immunoreactivity, whereas type 2 PrPSc and focal PrP deposits were accompanied by mild microglia reaction. These findings support the view that the phenotypic heterogeneity of sporadic CJD is largely determined by the physicochemical properties of distinct PrPSc conformers.
- Published
- 2005
- Full Text
- View/download PDF
42. Role of plasminogen in propagation of scrapie.
- Author
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Salmona M, Capobianco R, Colombo L, De Luigi A, Rossi G, Mangieri M, Giaccone G, Quaglio E, Chiesa R, Donati MB, Tagliavini F, and Forloni G
- Subjects
- Animals, Brain metabolism, Heterozygote, Mice, Mice, Knockout, Organ Specificity, Plasminogen genetics, Scrapie genetics, Spleen metabolism, Plasminogen physiology, PrPSc Proteins metabolism, Scrapie metabolism
- Abstract
To investigate whether plasminogen may feature in scrapie infection, we inoculated plasminogen-deficient (Plg(-/-)), heterozygous plasminogen-deficient (Plg(+/-)), and wild-type (Plg(+/+)) mice by the intracerebral or intraperitoneal (i.p.) route with the RML scrapie strain and monitored the onset of neurological signs of disease, survival time, brain, and accumulation of scrapie disease-associated forms of the prion protein (PrP(Sc)). Only after i.p. inoculation, a slight, although significant, difference in survival (P < 0.05) between Plg(-/-) and Plg(+/+) mice was observed. Neuropathological examination and Western blot analysis were carried out when the first signs of disease appeared in Plg(+/+) animals (175 days after i.p. inoculation) and when mice reached the terminal stage of illness. At the onset of symptoms, PrP(Sc) accumulation was higher in the brain and spleen of Plg(+/+) and Plg(+/-) mice than in those of Plg(-/-) mice, and these differences were paralleled by differences in the severity of spongiform changes and astrogliosis in the cerebral cortex and subcortical gray structures. Immunohistochemical analysis of the spleens before inoculation did not show any impairment of the immune system affecting follicular dendritic or lymphoid cells in Plg(-/-) mice. Once the disease progressed and mice began to die of infection, differences were no longer apparent in either brains or spleens. In conclusion, our data indicate that plasminogen has no major effect on the survival of scrapie agent-infected mice.
- Published
- 2005
- Full Text
- View/download PDF
43. Factors prolonging disability in work-related cumulative trauma disorders.
- Author
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Bonzani PJ, Millender L, Keelan B, and Mangieri MG
- Subjects
- Adult, Anger, Carpal Tunnel Syndrome classification, Carpal Tunnel Syndrome psychology, Carpal Tunnel Syndrome therapy, Costs and Cost Analysis, Cumulative Trauma Disorders classification, Cumulative Trauma Disorders economics, Cumulative Trauma Disorders therapy, Employment, Ergonomics, Female, Hand Injuries classification, Hand Injuries psychology, Hand Injuries therapy, Humans, Musculoskeletal Diseases classification, Musculoskeletal Diseases psychology, Musculoskeletal Diseases therapy, Occupational Diseases classification, Occupational Diseases economics, Occupational Diseases therapy, Retrospective Studies, Risk Factors, Soft Tissue Injuries classification, Soft Tissue Injuries psychology, Soft Tissue Injuries therapy, Stress, Psychological classification, Stress, Psychological psychology, Stress, Psychological therapy, Thoracic Outlet Syndrome classification, Thoracic Outlet Syndrome psychology, Thoracic Outlet Syndrome therapy, Workers' Compensation economics, Cumulative Trauma Disorders psychology, Disability Evaluation, Occupational Diseases psychology
- Abstract
Workers' compensation costs for management of soft tissue disorders continue to increase. The complexity of medical management of these cases has increased due to social factors. The purpose of this study is to improve the physician's ability to recognize nonmedical issues that prevent a rapid return to employment. A classification system is presented that will allow the clinician to identify administrative and pyschosocial issues that prolong disability. Additionally, the patients' job demands were classified by known ergonomic risk factors. The system was applied retrospectively to 50 random cases referred to two occupational hand clinics over a 1-year period. The results indicated that the psychosocial classification of the patient and the current employment status are the most important factors in prolonging disability workers.
- Published
- 1997
- Full Text
- View/download PDF
44. NONOBSTRUCTIVE ATELECTASIS.
- Author
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PINCK RL, BURBANK B, CUTLER SS, SBAR S, and MANGIERI M
- Subjects
- Child, Humans, Bronchography, Nervous System Physiological Phenomena, Pathology, Physiology, Pulmonary Atelectasis, Reflex
- Published
- 1965
- Full Text
- View/download PDF
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