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8. Abstracts of papers

Author

Biessels, P. T. M., Agoston, S., Horn, A. S., van Amsterdam, J. G. C., van Buuren, K. J. H., Soudijn, W., Brussee, J., Jansen, A. C. A., Kühn, A., Buhl, T., Rodrigues de Miranda, J. F., Beld, A. J., Lambrecht, G., Mutschler, E., Bultsma, T., Linschoten, M. R., Timmerman, H., Dröge, J. H. M., Wachter, A. A. H., Gaisser, H. D., van der Goot, H., Timnerman, H., Haenen, G. R. M. M., Bast, A., Grünbauer, H. J. M., Hall, David W. R., de Wijn, Spencer R., de Jong, J., de Vries, J., de Klerk, S. J., de Haan, F. H. N., Kelder, J., de Boer, Th., de Graaf, J. S., Wieringa, J. H., Krielaart, M. J., Veenstra, D. M. J., Zuiderveld, O. P., de Mol, N. J., Nieuwenhuyse, Hugo, Koenen, J., Mohn, G. R., Salden, H. J. M., Schonewille, E., Kothuis, M. J. M., Sterk, G. J., van der Schaar, M. W. G., Rademaker, B., van de Straat, R., de Boer, H., Vromans, R. M., Tijms, R. P. J. H., Bosman, P., and Zaagsma, J.

Published
1984
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9. Abstract of papers

Author

Konings, A. W. T., Joenje, H., Bast, A., Julicher, R., Van Iersel, A. A. J., Blaauboer, B. J., Balfoort, H. W., Ronbout, P. J. A., Borm, P. J. A., Engelen, J. J. M., Wouters, E. F. M., Swaen, C. M. H., de Boorder, Tj., Bos, R. P., Prinsen, W. J. C., Jongeneelen, F. J., Theuws, J. L. G., Henderson, P. Th., Cervantes, A., Schuurhuis, G. J., Pinedo, H. M., Lankelma, J., Commandeur, J. N. M., Oostendorp, R. A. J., Schoofs, P. R., Xu, B., Vermeulen, N. P. E., Coosen, R., van Leeuwen, F. X. R., Vos, J. G., Thijssen, J. H. H., Loeber, J. G., de Mol, N. J., Becht, A. B. C., Koenen, J., Lodder, G., de Wolff, F. A., van Ginkel, M. F., van der Voet, G. B., Dogterom, P., Nagelkerke, J. F., Mulder, G. J., Edelbroek, P. M., Zitman, F. G., Evelo, C. T. A., Niessen, H. J. J. M., Roelofs, H. M. J., Falke, H. E., De Groot, A. P., Willems, M. I., Franken, M. A. M., Kapteijn, R., Krajnc, E. I., Haenen, G. R. M. M., Plug, J. P. M., Timmerman, H., Hageman, G. J., Verhagen, H., Kleinjans, J. C. S., Herweijer, M. A., Bootsman, T. C., Scholte, B. J., Planta, R. J., Kroese, E. D., Tijdens, R. B., Meerman, J. H. N., Lusthof, K. J., Decuyper, J. G. A., Groothuis-Pielage, I. L., de Mol, N. J., Rietjens, I. M. C. M., Vos, R. M. E., Alink, G. M., van Bladeren, P. J., Rietveld, E. C., Ketels, H. H. T. M., Wetzer, A. M. A. C., Seutter-Berlage, F., Rombout, P., Dormans, J., van Bree, L., Marra, M., Til, H. P., Woutersen, R. A., Feron, V. J., Clary, J. J., Brandsma, A. E., de Wofff, F. A., van de Straat, R., de Vries, J., Boere, A. J. F., Rombout, P. J. A., Rietjens, I., Alink, G., van Erp, Yvette H. M., Heirbaut, Petra R. C. M., Koopmans, Marion J. E., Weterings, Peter J. J. M., van Loveren, H., de Klerk, A., Hakkert, B., Vertagen, H., Thijssen, H. H. W., Wester, P. W., Canton, J. H., Weterings, Peter J. J. M., and van Erp, Yvette H. M.

Published
1987
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11. Intravenous NPA for the treatment of infarcting myocardium early; InTIME-II, a double-blind comparison of single-bolus lanoteplase vs accelerated alteplase for the treatment of patients with acute myocardial infarction

Author

Braunwald, E., Neuhaus, K. -L., Antman, E., Chew, P., Skene, A., Wilcox, R., Ambrosioni, E., Anderson, J., Apetrei, E., Bata, I., Carrageta, M., Col, J., Dalby, A., Davies, R., Deckers, J., Eichman, D., Grande, P., Greene, R., Gurfinkel, E., Heikkilä, J., Henry, T., Hillis, D., Hochman, J., Huber, K., Kostis, J., Klinke, P., López-Sendón, J., Mckendall, G., Móller, B., Moore, P., Morris, A., Mueller, H., Östör, E., Oto, A., Ruda, M., Sadowski, Z., Schweiger, M., Sequeira, R., Shah, P., Shannon, R., Smith, B., Sobel, B., Steingart, R., Tebbe, U., Toman, J., Traboulsi, M., Vahanian, A., Warnica, J. W., Willerson, J., Deitchman, D., Davidson, L., Folgia, T., Foxley, A., Goodman, J., Hauck, C., Henry, D., Mccabe, C., Pangerl, A., Thomson, A., Wagner, M., Kennedy, J. W., Cairns, J., Demets, D., Julian, D., Simoons, M., Charlesworth, A., Easton, J. D., Ferbert, A., Feske, S., Kuhn, P., Moseley, J., Rogg, J. M., Reichmann, H., Sloan, M., von Kummer, R., Zamani, A., Coulter, S., Giugliano, R., Skene, A. M., Ardill, R., Ince, Y., Peters, A., Ward, K., Wolf, L., Curtis, N., De Brés, J., Stead, S., Watson, S., Cutler, S., Friedman, J., Helfrick, R., Williams, S., Klimovsky, J., Kumagai, S., Adams, E., Anderson, C., Bauhuber, I., Bennett, L., Biro, E., Boyce, E., Bregman, B., Carvalho, P., Ciganovic, D., Csukas, M., Cuenca, P., De Cuyper, S., Diez, P., Dijkhuizen, M., Dille-Amo, C., Gonzalez-Santis, A., Gursoy, M., Hammarstrom, K., Harasta, E., Ingman, E., Kelemen, B., Keulen, I., Koren, A., Langthaler, G., Lemaire, F., Little, I., Montalban, C., Nijssen, K., Neumueller, I., Palander, M., Pekuri, T., Persson, U., Pilz, J., Oudotova, S., Pisklakov, V., Proinov, F., Ptaszynska, A., Read, J., Retei, S., Romeyer, F., Romanini, M., Saar, L., Salein, D., Samsonov, M., Simeon-Dubach, D., Simmonds, J., Skaza, M., Skvortsova, N., Smidlova, Z., Spitzerova, H., Strijdveen, I., Szajewski, T., Ugurnal, B., Valcarce, M., van Rompaey, I., Walker, A., Zak, E., Zimova, N., Barrero, C., Beck, E., Bruno, M. L., Caccavo, A., Cagide, A., Campo, A., Cermesoni, R., Chahin, M., Dutra, O., Estrada, J., Falu, E. A., Gagliardi, J., Garre, L. E., Liprandi, A. S., Luciardi, H., Mautner, B., Muntaner, J., Nau, G., Salzberg, S., Santopinto, J., Sinisi, A., Torres, H., Eber, B., Elliott, P., Hiemetsberger, H., Juhasz, M., Kühn, P., Leisch, F., Niktardjam, M., Reisinger, J., Schmalix, G., Schuster, R., Sihorsch, K., Silberhauer, K., Slany, J., Steinbach, K., Tragl, K. H., Valentin, A., Al Shwafi, K., Dasnoy, P., De Clippel, M., de Meester, A., De Raedt, H. J. L. P., Emonts, M., Evrard, P., Eycken, M., Geboers, M., Heyndrickx, G., Lauwers, K., Mitrie, K., Pirenne, B., Renard, M., Somers, Y., Timmermans, P., Van Kuyk, M., Van Mieghem, W., Vermeulen, J., Verrostte, J. M., Albuquerque, D., Ayoub, J. C. A., Carvalho, A., Cesar, L., Gebara, O., Golin, V., Knobel, E., Leaes, P., Neto, J. A. M., Nicolau, J. C., Piegas, L. S., Rabelo, A., Rassi, A., Sila, L., Simao, A. F., Ashton, T., Baillie, H., Bhargava, R., Bota, G., Cameron, W., Chan, N., Chan, Y. K., Daly, P. A., Darcel, I., Davies, E., Desjardin, L., Dhingra, S., Ducas, J., Ervin, F. L., Fortin, C., Fowlis, R., Fulop, J., Furey, M., Gagnon, S., Gebhardt, V., Giannaccro, P., Gosselin, G., Graham, J., Grondin, F., Heath, J. W., Henderson, M., Hilton, D. R., Hiscock, J., Hui, W., Kaza, L., Kesselman, T., Kouz, S., Kucerak, M., Lahoude, N., Lamothe, M., Lebouthillier, P., Lenis, J., Levesque, P., Lopez, J. F., Lubelsky, B., Macritchie, D., Mayer, J. -P., Mcdowell, J. D., Montigny, M., Orestien-Lyall, T., Parekh, P., Pistawka, K., Price, J. B., Pruneau, G., Quinn, B., Reid, B. R., Richmond, M., Rose, B., Schuld, R., Sharma, N. K., Shetty, P., Stanton, E., Strauss, H. D., Sussex, B., Theroux, P., Turabian, M., Turner, C., Vizel, S., Walker, M., Weeks, A., Winkler, L., Zacharias, G., Zimmerman, R., Bartolucci, J., Castro, P., Diaz, M. A., Illanes, G., Potthoff, S., Sanchez, E. C., Silva, L. M., Yovanovich, J., Zanetti, F. L., Alan, D., Balázová, K., Boček, P., Cerny, J., Fischerova, B., Holub, M., Hradec, J., Janota, T., Janský, P., Kasper, J., Klimsa, Z., Motovská, Z., Pleva, L., Pluhacek, L., Pšenčka, M., Semrád, B., Spinar, J., Staněk, V., Štípal, R., Suítil, P., Vítovec, J., Wichterie, D., Widimský, P., Zeman, K., Andersen, C. B., Kriegbaum, J., Nielsen, N., Nielsen, P. E., Schou, J. B., Teesalu, R., Voitk, J., Haapamäki, H. V. H., Halkosaari, M., Härkönen, M., Jägerholm, S., Kärjä-Koskenkari, P., Karthunen, P., Kesäniemi, Y. A., Koskivirta, H., Lehto, P., Lilja, M., Paakkinen, S., Palomäki, A. K., Pietilä, K., Tuominen, J., Viopio-Pulkki, L., Ylönen, H., Adi, I., Admant, P., Akadirik, A., Alagha, Z., Alhabaj, S., Amat, G., Andre, A. A., Apffel, F., Aswad, K., Baradat, G., Bareiss, P., Barthers, F. B., Baudet, M., Baudouy, M., Bearez, E. M., Berthou, J. D., Berzin, B., Bessede, G., Blanc, J. J., Bocara, A., Bonneau, A., Bourdad, C., Bouvier, J. M., Cassagnes, J., Cassat, A., Cazaux, P., Charbonnier, B., Clementy, J., Cohen, A., Coisne, D., Colin, P., Croizier, O., D’Hautefeuille, B., D’Ivernois, C., Daumas, P. L., Dauphin, C. L., Deforet, M. F., Degand, B., Dequeker, J. L., Dickele, M. C., Dugrand, P., Durand, S., Ebagosti, A., Elharrar, C., Equine, O., Fichter, E., Flork, L., Fouche, R., Fourchard, V., Fourme, T., Fournier, P. Y., Funck, F., Galley, D., Garbarz, E., Ghadban, W., Gladin, M., Grall, J. Y., Grand, A., Gryman, R., Guillard, N., Guillo, P., Haftel, Y., Hannebicque, G., Henry, R., Huret, J. F., Janin-Magnificat, L., Jarnier, J., Joly, A., Kamal, H., Khalife, A., Roynard, J. L., Lang, M., Lapeyssonnie, A., Ledain, L., Lejeune, P., Lemetayer, L., Lepori, R., Lombart, A., Lusson, J. R., Magnin, O., Marquand, A., Martelet, M. M., Martelli, A., Mathurin, C., Mentre, B., Messager, D., Morizot, M., Mouallem, M. J., Mouhoub, O., Mycimski, C., Nallet, O., Olive, T., Pacouret, G., Palcoux, M. C., Poulard, J. E., Pruvost, A., Quiret, J. C., Richard, C., Richard, P., Rickaud, P., Riehl-Aleil, V., Rifai, A., Rocher, R., Rotreff, P., Segrestin, B., Slama, M. S., Sultan, P., Tabone, X., Talbodec, A., Tissot, M. T., Toussaint, C., Veyrat, A., Zerrouk, Z., Adamczak, M., Altmann, E., Altybernd, B., Andreassen, G., Andresen, D., Appenrodt, H., Bachmann, S., Bäcker, U., Beckert, U., Behr, H. M., Beier, W., Beier, T., Berger, D., Bernsmeier, R., Beythien, R. D., Biechl, E., Biedermann, G., Bischoff, K. O., Blerich, J., Boch, H. B., Bonzel, T., Both, A. R., Breidenbach, K., Breuer, M., Breuer, H. W. M., Brunkhorst, F. B., Bruns, A., Bundschu, H. D., Burkhardt, W., Busse, H. J., Caesar, K., Cailloud, J., Chlosta, A., Chorlanopoulos, E., Consemüller, S., Decker, W., Dichgans, M., Dick, R., Diederich, K. W., Dienst, C., Dietz, A., Dißmann, R., Ditter, H., Doering, W., Drost, H., Dundalek, E. D., Eckardt, D., Edelmann, A., Eggeling, T., Eggert, G., Eichner, R., Endres, C., Engberding, R., Engel, H. J., Faehnrich, A., Fischer, J. L., Flor, A., Forycki, F. Z. F., Froböse, H. J., Fruehauf, T., Fuchs, M., Geiser, R., Geletneky, J., Gerdes, H., Gerecke, B., Gesing, S., Gieser, H., Girth, E., Glogner, P., Glover, M., Goetz, J., Goetz, H., Göttfert, G., Gottwik, M., Gregori, B., Grieshaber, M., Großmann, C., Gruber, G., Gunold, H., Häßler, W. H., Hackenjos, B., Hader, O., Hamer, H., Harmjanz, D., Hasst, G., Haun, H., Hauptmann, K. E., Hegge, F. J., Heinze, A., Heinze, R., Henrichs, K. J., Hergenröther, H., Herrmann, F., Herzig, C., Hey, D., Hill, S., Hinzmann, S., Hoffmann, S., Höfs, T., Höhler, H., Holle, G., Höltman, B. J., Horacek, T., Hossmann, V., Hübner, F. S., Hülskamp, C., Hunecke, R., Hust, M., Jaeckh, G., Jebens, C., Jennen, E., Jost, M., Justiz, R., Kallmann, L., Kalscheur, F., Kaschner, W., Kaspar, W., Kauder, E., Keitel, B., Keller, H., Kemkes, T., Kerler, N., Kester, M., Kettner, W., Kilp, M., Kirklies, A., Klaus, A., Klein, H. H., Klenböck, J. R., Kley, H. K., Klingenbeck, R., Koch, H., Kohler, B., Kohler, J., Kolloch, R., Konermann, M., Körber, H. G., Kother, T. K., Kötter, V., Kottwitz, B., Kozariszcsuk, G., Kracht, T., Kratzsch, G., Kreft, H. U., Kreuter, G., Krönert, H., Krönig, B., Krueger, E., Krülls-Münch, J., Kuckuk, H., Kuelschbach, M., Kuhrt-Lassay, O. W., Kummerhoff, P. W., Kunevt, R., Kurth, C. U., Lang, C., Lange, C., Langhoff, R., Laskus, A., Lazarus, P., Lehmann, H. U., Lenga, P., Lengfelder, W., Leupolz, W., Limbourg, P., Loos, U., Lucanus, W., Machill, K., Mäckel, P., Mackes, K. G., Maier, S., Makowski, B., Mandok, J., Manz, M., Mäurer, W., Meier, F., Meier, J., Menges, M., Merx, W., Meurers, G., Michels, U., Mickeler, C. H., Mons, D., Moos, E., Mueller, R., Müller, G., Nast, H. P., Naumann, G., Nebelsieck, H., Neubaur, J., Niederer, W., Nitsch, J., Noack, J., Nogai, K. F. W., Oberheiden, A., Obst, R., Ochs, H. R., Odemar, F., Odenthal, H. J. B., Offers, E., Öhl, S., Ohlmeier, H. A. R. M., Patzer, P., Pech, A., Peters, U., Petry, U., Pietschmann, G. J., Pistner, W., Plappert, B., Pohlmann, W. K., Pollock, B., Presser, H. J., Przytarski, K., Puerner, K. L., Raouf, N., Reike, N., Reil, G. H., Reinhard, U., Riebeling, V., Ritzmann, M., Rödder, J., Roth, E., Rüdelstein, R., Saborowski, F., Sauter, B., Sceffler, N., Schartl, A., Schifferdecker, E., Schlotterbeck, K. P., Schmidt, J., Schmidt-Dannert, D. R., Schmidt-Klewitz, H., Schmitz, H. J., Schnebelt, T., Schneider, H. L., Schneider, F. J., Schoeller, R., Scholz, D., Schoppe, W. D., Schreiner, G., Schroeder, J., Schuh, N., Schulte, K. L., Schulze, H., Schulze, H. D., Schuster, P., Schuster, H. P., Schweizer, P., Sechtem, U., Sedlmaier, H. P., Segel, S., Sehnert, W., Seidel, F., Siedentopf, K., Simon, H., Sodomann, C. P., Solbach, C., Sorges, E., Stabenow, S., Stadler, K. P., Stammwitz, E., Stein, U., Sternberg, H., Stiepak, C., Stockmann, M., Straus, W., Striegel, H., Struch, E., Strupp, G., Taubert, T. B. T., Thoeming, B., Thoß, A., Tinnappel, J., Tomsik, H., Topp, H., Troost, S., Öberreiter, A., Uebis, R., Ungler, T., Urbaszek, W., Vöhringer, H. F., von Arnim, T., von Leitner, E. R., von Löwis of Menar, A., von Mengden, H. J., von Smekal, P., Voss, W., Wacker, P., Warning, A., Warzecha, A., Wefers, U., Wehr, M., Weigel, H., Weissthanner, F., Weller, P., Werner, M., Wette, A., Wichert, H., Wielage, T., Wiese, U., Wilbrand, T. B., Wilhelms, E., Wilmsmann, G., Wolf, F. H., Wolf, T., Wonhas, F. C. M., Zastrow, B., Zeymer, U., Ziruler, S., Ziss, W., Zölch, K. A., Zwirner, K., Becker, D., Bosko, M., Csillag, I., Ermenyi, A., Fogas, J., Heltai, K., Jánosi, A., Katona, A., Kiraly, C., Kiss, B., Kutor, G., Mizik, R., Molnar, T., Mühl, M., Nagy, D., Palacti, I., Rudas, L., Sárosi, I., Simon, K., Sitkel, E., Sydó, T., Szaboki, F., Szikla, K., Szönyi, T., Timar, S., Vándor, L., Zamolyl, K., Walsh, M., Caspi, A., Swissa, M., Badano, L., Baldacci, G., Balli, E., Banda, D., Baretta, G., Boccalatte, A., Borgatti, M. L., Branzi, A., Burelli, C., Capelletti, D., Capucci, A., Caragiulo, D., Carbonieri, E., Cassin, M., Ceci, V., Cocchieri, M., Coletta, C., Conte, E., Contini, G. M., Corsini, G., D’Annunzio, E., De Blasi, M., De Luca, I., Delciterna, F., Di Pasquale, G., Diguardo, G., Fattore, L., Ferraiuulo, G., Finardi, A., Fioretti, P. M., Giunta, G., Guiducci, U., Guzzardi, G., Horando, G., Ignone, G., Lazzaroli, A., Levantesi, D., Liberati, R., Losi, E., Macor, F., Mangiameli, S., Martines, C., Meinardi, F., Morgera, T., Morozzi, L., Mostacci, M., Naccarella, F. F., Ottani, F., Palamara, A., Pani, A., Paperini, L., Pes, R., Pesola, A., Porzio, A., Raviele, A., Ricci, S., Rosi, A., Rossi, R., Rotiroti, D., Rusconi, L., Sabino, G., Saccone, V., Sanna, A., Scaramuzzino, G., Scorcu, G. P., Semprini, F., Severini, D., Staniscia, D., Tantalo, L., Tartagni, F., Terrosu, P., Tondelli, S., Trichero, R., Uslenghi, E., Vajola, S. F., Vetrano, A., Violi, E., Zardini, P., Zingarini, G. L., Zobbi, G., Zuin, G., Kalnins, U., Cârvekülg, A., Laanoca, J., Iacis, J., Lankiene, L., Laucevicius, A., Lukoseviciute, A., Palsauskaite, R., Petrauskiene, B., Soopóld, W., Uuetoa, H., Vilks, J., Vitonyte, R., Zakke, I., Dorantes, J., Hernández, H., Jerjes, C., Leva Garza, J. L., Martinez, C., Anneveldt, A., Baars, H. F., Baldew, S. C., Bendermacher, P. E. F., Boersma, L. V. A., Bos, R. J., Breedveld, R. W., Bruggink, P. W. F., Ciampricotti, R., Darmanata, J. I., de Porto, A. E., de Weerd, G. J., Deckers, J. W., Freericks, M. P., Hillebrand, F. A., Kerker, J. P., Koenen, J. C., Kofflard, M. G. M., Liem, K. L., Liem, A. H., Linssen, G. C. M., Lionarons, R. J., Peters, J. R. M., Posma, J. P., Saat, E. W. M., Savalle, L. H., Smits, W. C. G., Suttorp, M. J., Tans, A. C., Troquay, R. P. Th., van Beek, G. J., van Boven, A. J., Van der Heijden, R., Van Hessen, A., van Langeveld, R. A. M., van Lier, T. A. R., van Loo, L. W. H., van Wijngaarden, J., van Ziejl, L. G. P. M., Veerhoek, M. J., Vermer, F., Werner, H. A., Graven, T., Klykken, B., Meyerdieks, O., Omland, T. M., Otterstad, J. E., Pedersen, T., Rød, R., Banaszewski, M., Bednarkiewicz, Z., Bojarski, G., Ceremuzyñski, L., Czestochowska, E., Gajewski, M., Galewicz, M., Gorski, J., Grabczewska, Z. S., Gruchaka, M., Janicki, K., Janion, M., Jaworska, K., Jezewska, M., Kakol, J., Kizciuk, M., Kleinrok, A., Kolodziej, P., Komorowski, P., Konopka, A., Kopaczewski, J., Korecki, J., Kornacewicz-Jach, Z., Kowalewski, M., Kratochwil, D., Krolczyk, J., Krzminska-Pakula, M., Kurek, P., Kurowski, M., Kurpesa, M., Kurzawski, J., Kwiecien, R., Lenartowski, L., Lewandowski, M., Loboz-Grudzieñ, K., Luczak, G., Maliñski, A., Michalski, M., Musial, W., Nartowicz, E., Nowicka, A., Odyniec, A., Pasyk, S., Prastowski, W., Przybylski, A., Raczynska, A., Rodzik, J., Romanowski, M., Rynkiewicz, A., Rzyman, M., Sidorowicz, A., Sledziona, M., Sobiczewski, W., Sobkowicz, B., Sobolewska, J., Sokalski, L., Stepinska, J., Sterlinski, M., Stopinski, M., Świątecka, G., Szpernal, Z., Tarnowska, H., Trzos, E., Ujda, M., Wierzchowiecki, M., Wodynska, T., Wojciechowski, D., Wrabec, K., Wrzesinski, K., Zuk, P., Albuquergue, A., Costa, A., Cunha, D., Ferreira, D., Ferreira, R., Gaog Leiria, J. M., Pimenta, A., Rufino, E., Vasconcelos, J., Aldica, M., Balanescu, S., Bruckner, I. V., Capalneanu, R., Florescu, N., Georgescu, C. S., Cherasim, L., Ginshina, C., Merenta, A., Parvu, O., Radutiu, S., Savulescu, I., Vita, I., Averkov, O., Bokarev, I. N., Gratsiansky, N., Grigoriev, Y., Gruzdev, A., Kakhnovsky, I., Kheevehuk, T. V., Khrustalev, O., Kobalava, Y., Konoratieva, T. B., Koukline, Vladimir, Martiouchov, S., Pavlikova, E., Poskotinov, I., Rogalev, K., Sinopainikov, A., Syrkin, A., Tereschenko, S. T., Yavelov, I., Zavolghin, S., Čurilla, E., Kohn, R., Kovář, F., Murín, J., Poliačik, P., Drinovec, I., Horvat, M., Krivec, B., Markež, J., Pareznik, R., Pehnec, Z., Resman, J., Sifrer, F., Skale, R., Trinkaus, D., Voga, G., Baig, M. M. E., Blomerus, P., Botha, B. P., Burgess, L., Duncan, D., Duncan, D. I., Gillmer, D., Govender, N., Jardine, R. J., Kok, A., Manga, P., Naidu, R. K., Rajput, M. C., Ranjith, N., Roos, J. S., Snyders, F. A., Steingo, L., Stern, A., Tayob, F. Z., Vythilingum, S., Alonso-Orcajo, N., Arribas Jimenez, A., Ayestaran, J. I., Balsera, B. B. G., Barras, C., Castro, A., Cobo, N., Duque, A., Garcia, M. J., Goiriena, P., Gonzalez-Valdayo, M., Gulias Lopez, J. M., Jimenez Gomez, P., Lopez Garanda, V., Martín Santos, F., Nogueira, R., Pabon Osuna, P., Ponce De Leon, E., Quesada Dorador, A., Paya Serrano, R., Rodriguez, L., Rodriguez, M., Rubio, F., Ruiz-Salmeron, R., Solar, J., Toquero, J., Velasco, J., Vilar Herrero, V., Vizcaino, M., Wancisidor, X., Basilier, E., Birgersdotter, V., Björnsdotter, E., Bjurman, A., Hagström, D., Hallin, I., Hansen, O., Hemmingson, L. O., Lundkvist, L., Lycksell, M., Möller, B., Nolgard, P., Sjölund, G., Stjerna, A., Angehrn, W., de Benedetti, E., Diethelm, M., Gallino, A., Plebani, G., Vögelin, H. P., Wojtyna, W., Akgöz, H., Akgün, G., Akyürek, O., Batur, M. K., Bayata, S., Deger, N., Emel, O., Gürgün, C., Korkmaz, M. E., Kozan, O., Kumbasar, D., Muderrisoglu, H., Nisanci, Y., Ozin, B., Ozsaruhan, O., Payzin, S., Postaci, N., Sozcuer, H., Tamci, B., Topuzoglu, F., Türkoglu, C., Tutar, E., Ulucam, M., Ulusoy, T., Umman, B., Yalçinkaya, S., Yesil, M., Zoghi, M., Adams, P. C., Ahir, S., Ahsan, A. J., Akhtar, J., Albers, C. J., Al-Khafaji, M. N., Anderson, N., Bailey, R. J., Bain, R. J. I., Basu, A., Beal, A., Boyle, R. M., Brown, N., Campbell, S., Card, D., Cross, S. J., Davies, P., Davis, E. T. L., Dean, J. W., Deaner, A., Devine, M. A., Dhawan, J., Doig, J. C., Dubrey, S., Dunn, P. G., Dwight, J., Ecob, R., Fitzpatrick, H., Fletcher, S., Francis, C. M., Gershlick, A. H., Glennon, P. E., Goodfield, N. E., Grabau, W. J., Gray, M., Gray, K. E., Heath, J., Hendry, W. G., Highland, J., Hogg, K., Irving, J. B., James, M. A., Jennings, K., Joy, M., Kadr, H. H., Kahn, S., Keeling, P. J., Keir, P. M., Kemp, T. M., Kinaird, J., Kinsey, C., Knowles, K., Kooner, J. S., Lahiri, A., Lawson, C., Lewis, R., Macdermott, A. F. N., Mackay, A., Macleod, D. C., Mccance, A. J., Morrison, A., Mortimer, M., Mulvey, D., Murphy, J. J., Murray, S., Muthusamy, R., Myers, A., Nicolson, V. G., Northridge, D., Odemuyiwa, S., Oldroyd, K. G., Oliver, R. M., Pell, A. C. H., Pohl, J. E. F., Price, B., Quereshi, N., Rae, A. P., Reader, S., Reid, D. S., Reynolds, G. W., Robinson, A., Robson, R. H., Rodger, J. C., Rodrigues, E., Rose, E. L., Rowlands, D. B., Rowley, J. M., Rozkovec, A., Shreeve, J., Siklos, P., Smith, R. H., Sneddon, J. F., Somasundram, U., Squire, I., Stephens, J. D., Stephens-Lloyd, A., Strand, J. M., Stuart, J., Sutaria, N., Swan, J., Tait, G. W., Thomas, R. D., Thompson, M. A., Tildesley, G., Travill, C. M., Treadgold, J. A., Trelawney, J. M. S., Turner, D., Vallance, B. D., Wallbridge, D., Weissberg, P. L., White, E., Wicks, M., Wilcox, R. G., Wilkinson, P., Wiltshire, J. E., Wright, A., Andrea, B., Attassi, K., Bahr, R., Banas, J., Baran, K., Belknap, M., Bensman, M., Bertolet, B., Besley, D., Bethala, V., Betzu, R., Bhalla, R., Bhargava, M., Binder, A., Birkhead, R., Bodine, K., Brewer, D., Carey, S., Chengot, M., Coppola, J., Cragg, D., D’Arcy, B., Denny, D. M., Dilorenzo, P., Dixon, E., Doorey, A., Doty, D., Doty, W., Drossner, M., Eisenberg, P., Falco, T., Feldman, R., Freman, I., Frey, M., Garcia, J., Glassman, J., Goldman, S., Gomez, M., Gonzalez, M., Goodfield, P., Gottlieb, S., Grech, D., Hack, T., Haffey, T., Hanson, J., Havranek, E., Hermany, P., Hernandez, H., Herron, R., Hession, W., Hines, J., Hundley, R., Jacobs, W. C., Jerjes-Sanchez, C., Jerome, S., Josephson, R., Kalan, J., Kawalsky, D., Khan, A., Kmetzo, K., Kraemer, M., Lader, E., Landis, J., Lash, J., Leber, R., Leimbach, W., Leiva Garza, J. -L., Maddox, W., Magorien, R., Mahapatra, S., Mantecon, I., Mendelson, R., Miklin, J., Milas, J., Miller, R., Molk, B., Monrad, E. S., Morrison, J., Morse, H., Neustel, M., Nichols, D., Niederman, A., Nygaard, T., O’Connor, R., O’Riordan, W., Obermueller, S., Palmeri, S., Patel, R., Paul, T., Phiambolis, T., Piana, R., Polansky, B., Polinski, W., Ponce, G., Ribeiro, P., Roccario, E., Rogers, C. P., Rogers, W., Rosenblatt, A., Runyon, J. P., Scheel, F., Schmidt, P., Schneider, R., Schwartz, H., Shelhamer, L., Sheridan, F., Shine, W., Shook, T., Siskind, S., Slama, R., Spear, E., Stouffer, G., Strunk, B., Thadani, U., Timmis, G., Trautloff, R., Tse, A., Wohl, B., Zarren, H., Zucker, R., Kuster, F., and Pardie, J. P.

Subjects
Male, Risk, Infusions, medicine.medical_treatment, Myocardial Infarction, Bolus lytic therapy, Acute myocardial infarction, Tissue plasminogen activator, Thrombolytic drug, Double-Blind Method, Fibrinolytic Agents, medicine, Humans, Thrombolytic Therapy, Myocardial infarction, Infusions, Intravenous, Stroke, Aged, business.industry, ST elevation, Lanoteplase, Emergency department, Middle Aged, medicine.disease, Survival Analysis, Regimen, Relative risk, Anesthesia, Tissue Plasminogen Activator, Female, Intracranial Hemorrhages, Cardiology and Cardiovascular Medicine, business, Intravenous, medicine.drug
Abstract

AIMS To compare the efficacy and safety of lanoteplase, a single-bolus thrombolytic drug derived from alteplase tissue plasminogen activator, with the established accelerated alteplase regimen in patients presenting within 6 h of onset of ST elevation acute myocardial infarction. METHODS AND RESULTS 15,078 patients were recruited from 855 hospitals worldwide and randomized in a 2:1 ratio to receive either lanoteplase 120 KU. kg(-1)as a single intravenous bolus, or up to 100 mg accelerated alteplase given over 90 min. The primary end-point was all-cause mortality at 30 days and the hypothesis was that the two treatments would be equivalent. By 30 days, 6.61% of alteplase-treated patients and 6.75% lanoteplase-treated patients had died (relative risk 1.02). Total stroke occurred in 1.53% alteplase- and 1.87% lanoteplase-treated patients (ns); haemorrhagic stroke rates were 0.64% alteplase and 1.12% lanoteplase (P=0.004). The net clinical deficit of 30-day death or non-fatal disabling stroke was 7.0% and 7.2%, respectively. By 6 months, 8.8% of alteplase-treated patients and 8.7% of lanoteplase-treated patients had died. CONCLUSION Single-bolus weight-adjusted lanoteplase is an effective thrombolytic agent, equivalent to alteplase in terms of its impact on survival and with a comparable risk-benefit profile. The single-bolus regimen should shorten symptoms to treatment times and be especially convenient for emergency department or out-of-hospital administration.

Published
2000

12. Readers Report.

Author

Koenen, J. F., Lombard, Michael, Pitbladdo Jr., Richard B., Longhi, Tricia, Shapiro, Edward, Nilsson, Anna B., Yankee, Sandra, Costello, Joseph M., Bobo, Don, Bobo, Vicki, and Heyman, David L.

Subjects
LETTERS to the editor, ECONOMIC trends, ECONOMIC history, INTERNATIONAL relations
Abstract

This section presents letters to the editor referencing articles and topics discussed in previous issues including "It's Time for Germany to Stop Sitting on Its Hands," in the February 4, 1991 issue, "Economic Trends," in the January 28, 1991 issue and "Postwar Kuwait Could Be a Political Pandora's Box," in the February 11, 1991 issue.

Published
1991

14. Complete balance of energy during necking in polymeric glasses and its strain-rate dependence.

Author

Kilian, H. -G., Lagaly, G., Janssson, J. -F., Gedde, U. W., Koenen, J. A., and Kilian, H.-G.

Abstract

Some polymeric glasses, e.g., polycarbonate, deform heteregeneously after yielding by forming a neck. The boundary between two zones with different strains λ′ and λ″ propagates at constant stress with a valocity vn over the sample, changing the deformation of the material from λ′ to λ″. This process is accompanied by an exchange of mechanical work and heat. At low vn both quantities are measured in a stretching calorimeter. At higher vn, we observe the sample in the stretching device with an infrared camera. Comparison of the measured temperature pattern on the surface of the sample with a calculation using the differential equation of heat conduction including heat sources and heat loss results in the strength of the sources and, therefore, to the heat produced by the transition. The mechanical work shows a small increase with vn. The heat is constant at low vn and increases at vn≈2 · 10−4 m/s until the entire work is transformed into heat. [ABSTRACT FROM AUTHOR]

Published
1992
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15. Readers Report.

Author

Murphy, Mary Engelmann, Rosenthal, John, Violette, Susan M., Worsley, Peter K., Koenen, J. F., Yukoh, Yamamoto, Romano, Nicholas R., and Schubert, Jeff

Subjects
LETTERS to the editor, EDUCATIONAL finance, RICH people, STAPLES & stapling machines
Abstract

Several letters to the editor are presented in response to articles which appeared in previous issues, including "School Finance Reform: Don't Give Up on Vouchers," in the December 27, 1993 issue, "Aflfuent, Dual Income Families Get Creamed by the Feds," in the December 27, 1993 issue and "Power Staples," in the January 10, 1994 issue.

Published
1994

16. READERS REPORT.

Author

Deisenroth, Jairus J., Keamey, James C., Allison, W. L., Koenen, J. F., and Sorrentino, Alessandro

Subjects
LETTERS to the editor, BASEBALL, BUSINESS conditions, BUYER'S market
Abstract

Several letters to the editor are presented in response to articles published in earlier issues including "Baseball gets a brawny rival" in April 1, 1967 issue, "Markets briefs" in the same issue and "Flood of U.S. buyers hits Florence as usual" in March 18, 1967 issue.

Published
1967

20. Expression of a functional recombinant Phoneutria nigriventer toxin active on K+ channels

Author

Carneiro, A.M.D., Kushmerick, C., Koenen, J., Arndt, M.H.L., Cordeiro, M.N., Chavez-Olortegui, C., Diniz, C.R., Gomez, M.V., Kalapothakis, E., Prado, M.A.M., and Prado, V.F.

Subjects
*SPIDER venom, *POTASSIUM channels
Abstract

PnTx3-1 is a peptide isolated from the venom of the spider Phoneutria nigriventer that specifically inhibits A-type K+ currents (IA) in GH3 cells. Here we used a bacterial expression system to produce an NH2-extended mutant of PnTx3-1 (ISEF-PnTx3-1) and tested whether the toxin is functional. The recombinant toxin was purified from bacterial extracts by a combination of affinity and ion-exchange chromatography. The recombinant toxin blocked A-type K+ currents in GH3 cells in a fashion similar to that observed with the wild-type toxin purified from the spider venom. These results suggest that recombinant cDNA methods provide a novel source for the production of functional Phoneutria toxins. The recombinant ISEF-PnTx3-1 should be useful for further understanding of the role of A-type K+ currents in biological processes. [Copyright &y& Elsevier]

Published
2003
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21. WHIM Syndrome-linked CXCR4 mutations drive osteoporosis.

Author

Anginot A, Nguyen J, Abou Nader Z, Rondeau V, Bonaud A, Kalogeraki M, Boutin A, Lemos JP, Bisio V, Koenen J, Hanna Doumit Sakr L, Picart A, Coudert A, Provot S, Dulphy N, Aurrand-Lions M, Mancini SJC, Lazennec G, McDermott DH, Guidez F, Blin-Wakkach C, Murphy PM, Cohen-Solal M, Espéli M, Rouleau M, and Balabanian K

Subjects
Animals, Mice, Mutation, Osteogenesis genetics, Humans, Immunologic Deficiency Syndromes genetics, Osteoporosis genetics, Primary Immunodeficiency Diseases genetics, Receptors, CXCR4 genetics, Receptors, CXCR4 metabolism
Abstract

WHIM Syndrome is a rare immunodeficiency caused by gain-of-function CXCR4 mutations. Here we report a decrease in bone mineral density in 25% of WHIM patients and bone defects leading to osteoporosis in a WHIM mouse model. Imbalanced bone tissue is observed in mutant mice combining reduced osteoprogenitor cells and increased osteoclast numbers. Mechanistically, impaired CXCR4 desensitization disrupts cell cycle progression and osteogenic commitment of skeletal stromal/stem cells, while increasing their pro-osteoclastogenic capacities. Impaired osteogenic differentiation is evidenced in primary bone marrow stromal cells from WHIM patients. In mice, chronic treatment with the CXCR4 antagonist AMD3100 normalizes in vitro osteogenic fate of mutant skeletal stromal/stem cells and reverses in vivo the loss of skeletal cells, demonstrating that proper CXCR4 desensitization is required for the osteogenic specification of skeletal stromal/stem cells. Our study provides mechanistic insights into how CXCR4 signaling regulates the osteogenic fate of skeletal cells and the balance between bone formation and resorption., (© 2023. The Author(s).)

Published
2023
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22. Radioiodine Ablation of Thyroid Remnants in Patients with Graves' Orbitopathy.

Author

Oeverhaus M, Koenen J, Bechrakis N, Stöhr M, Herrmann K, Fendler WP, Eckstein A, and Weber M

Subjects
Humans, Iodine Radioisotopes therapeutic use, Retrospective Studies, Long-Acting Thyroid Stimulator, Thyroidectomy adverse effects, Inflammation, Graves Ophthalmopathy diagnostic imaging, Graves Ophthalmopathy radiotherapy, Graves Ophthalmopathy surgery, Thyroid Neoplasms drug therapy
Abstract

Our purpose was to assess response after ablation of thyroid remnants (ATR) with radioactive iodine therapy in patients with unstable Graves' orbitopathy (GO) after subtotal thyroidectomy. Methods: Thirty patients with mild ( n = 4, 13%), moderate-to-severe ( n = 25, 83%), or very severe GO ( n = 1, 3%) were analyzed in this retrospective study. The primary endpoint was the improvement of GO-related symptoms as assessed by clinical activity scores, NOSPECS, and soft-tissue inflammation scores at 3 and 12 mo after ATR. Ablation success was defined by a decrease in 99m Tc uptake on thyroid scintigraphy, remnant volume, and thyrotropin receptor antibody levels at 3 mo after ATR. Results: Twelve months after ATR, clinical activity scores, NOSPECS, and soft-tissue inflammation scores showed a significant decrease from 3.4 to 1.3 ( P < 0.0001), 5.9 to 4.9 ( P = 0.007), and 4.7 to 2.1 ( P = 0.0001), respectively. The GO was inactive in 27 of the 30 (90%) patients after 3 mo and in 29 (97%) after 12 mo. No new activation of GO occurred. Remnant volume (1.4 vs. 0.4 cm 3 , P = <0.0001), mean thyrotropin receptor antibody level titer (19.02 vs. 13.37 IU/L, P < 0.0001), and 99m Tc uptake (0.5% vs. 0.1%; n = 12; P = 0.04) decreased significantly until 3 mo after ATR. Discussion: Radioactive iodine therapy after thyroidectomy can successfully ablate residual thyroid remnants, leading to an improvement in GO, a reduction in inflammatory activity, and stabilization of thyroid function. Thus, scintigraphy should be considered for patients with unstable GO after thyroidectomy to rule out thyroid remnants., (© 2023 by the Society of Nuclear Medicine and Molecular Imaging.)

Published
2023
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23. In vitro and in vivo study on the osseointegration of BCP-coated versus uncoated nondegradable thermoplastic polyurethane focal knee resurfacing implants.

Author

Jeuken RM, Roth AK, Peters MJM, Welting TJM, van Rhijn LW, Koenen J, Peters RJRW, Thies JC, and Emans PJ

Subjects
Animals, Calcification, Physiologic, Cells, Cultured, Fluorine Radioisotopes, Goats, Humans, Knee Prosthesis, Mesenchymal Stem Cells, Positron Emission Tomography Computed Tomography, Sodium Fluoride, Surface Properties, Titanium, Coated Materials, Biocompatible chemistry, Hydroxyapatites chemistry, Knee surgery, Osseointegration, Polyurethanes chemistry, Prostheses and Implants
Abstract

Focal knee resurfacing implants (FKRIs) are intended to treat cartilage defects in middle-aged patients. Most FKRIs are metal-based, which hampers follow-up of the joint using magnetic resonance imaging and potentially leads to damage of the opposing cartilage. The purpose of this study was to develop a nondegradable thermoplastic polyurethane (TPU) FKRI and investigate its osseointegration. Different surface roughness modifications and biphasic calcium phosphate (BCP) coating densities were first tested in vitro on TPU discs. The in vivo osseointegration of BCP-coated TPU implants was subsequently compared to uncoated TPU implants and the titanium bottom layer of metal control implants in a caprine model. Implants were implanted bilaterally in stifle joints and animals were followed for 12 weeks, after which the bone-to-implant contact area (BIC) was assessed. Additionally, 18F-sodium-fluoride (18F-NaF) positron emission tomography PET/CT-scans were obtained at 3 and 12 weeks to visualize the bone metabolism over time. The BIC was significantly higher for the BCP-coated TPU implants compared to the uncoated TPU implants (p = .03), and did not significantly differ from titanium (p = .68). Similar 18F-NaF tracer uptake patterns were observed between 3 and 12 weeks for the BCP-coated TPU and titanium implants, but not for the uncoated implants. TPU FKRIs with surface modifications could provide the answer to the drawbacks of metal FKRIs., (© 2020 The Authors. Journal of Biomedical Materials Research Part B: Applied Biomaterials published by Wiley Periodicals LLC.)

Published
2020
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24. Atypical Chemokine Receptor 3 (ACKR3): A Comprehensive Overview of its Expression and Potential Roles in the Immune System.

Author

Koenen J, Bachelerie F, Balabanian K, Schlecht-Louf G, and Gallego C

Subjects
Animals, Gene Expression, Humans, Immune System immunology, Immune System metabolism, Receptors, CXCR genetics, Immunity, Cellular physiology, Neutrophils immunology, Neutrophils metabolism, Receptors, CXCR immunology, Receptors, CXCR metabolism
Abstract

Atypical chemokine receptor 3 (ACKR3), previously known as C-X-C chemokine receptor type 7 (CXCR7), has emerged as a key player in several biologic processes, particularly during development. Its CXCL11 and CXCL12 scavenging activity and atypical signaling properties, together with a new array of other nonchemokine ligands, have established ACKR3 as a main regulator of physiologic processes at steady state and during inflammation. Here, we present a comprehensive review of ACKR3 expression in mammalian tissues in search of a possible connection with the receptor function. Besides the reported roles of ACKR3 during development, we discuss the potential contribution of ACKR3 to the function of the immune system, focusing on the myeloid lineage., (Copyright © 2019 by The American Society for Pharmacology and Experimental Therapeutics.)

Published
2019
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25. A rat homologue of CED-6 is expressed in neurons and interacts with clathrin.

Author

Martins-Silva C, Ferreira LT, Cyr M, Koenen J, Fernandes DR, Carvalho NR, Ribeiro CB, Marion S, Chavez-Olortegui C, Prado MA, and Prado VF

Subjects
Amino Acid Sequence, Animals, Apoptosis Regulatory Proteins, Base Sequence, Brain anatomy & histology, Caenorhabditis elegans Proteins genetics, Caenorhabditis elegans Proteins metabolism, Cell Line, Transformed, Choroid Plexus metabolism, Choroid Plexus ultrastructure, Clathrin-Coated Vesicles, Endocytosis physiology, Humans, Mice, Molecular Sequence Data, Nerve Tissue Proteins genetics, Nerve Tissue Proteins isolation & purification, Neurons cytology, Phosphoproteins genetics, Phosphoproteins isolation & purification, Presynaptic Terminals ultrastructure, Protein Transport physiology, Rabbits, Rats, Synaptic Transmission physiology, Synaptosomes metabolism, Synaptosomes ultrastructure, Brain metabolism, Clathrin metabolism, Nerve Tissue Proteins metabolism, Neurons metabolism, Phosphoproteins metabolism, Presynaptic Terminals metabolism
Abstract

We isolated from a brain library a cDNA encoding an isoform of rat CED-6 that has not been previously described. This transcript results from alternative splicing of the ced-6 gene present on chromosome 9. We expressed this isoform as his-tagged protein in E. coli and used the purified protein to raise antibodies to investigate the expression of CED-6 in rat brain. Immunoblot analysis showed the presence of CED-6 as a doublet of approximately 34 and 33 kDa in cortex, hippocampus and cerebellum, indicating that the protein was present in different regions of the brain. Subcellular fractionation experiments showed that CED-6 immunoreactivity did not concentrate in GFAP-containing glial vesicles, whereas it showed a distribution similar to the synaptotagmin in synaptosomes-enriched fractions, suggesting that CED-6 is present in neurons. CED-6 immunoreactivity was also investigated using immunohistochemistry analysis and it was found in several brain regions, being particularly strong in the cell body of some groups of neurons such as Purkinje cell layer of cerebellum, and pyramidal cells of the hippocampal formation and also in epithelial cells from the choroid plexus. Importantly, CED-6 immunoreactivity colocalized with a neuronal marker but not with a glial marker. Considering that several PTB-containing proteins bind clathrin, we investigated whether rat CED-6 would also have this property. Yeast two-hybrid and GST pull-down analysis indicated that ratCED-6 interacts with clathrin and in cultured cells we detected colocalization between CED-6 and clathrin-coated vesicles. The present findings suggest that CED-6 may have a role in endocytic trafficking or signaling in neurons.

Published
2006
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26. Mice deficient for the vesicular acetylcholine transporter are myasthenic and have deficits in object and social recognition.

Author

Prado VF, Martins-Silva C, de Castro BM, Lima RF, Barros DM, Amaral E, Ramsey AJ, Sotnikova TD, Ramirez MR, Kim HG, Rossato JI, Koenen J, Quan H, Cota VR, Moraes MF, Gomez MV, Guatimosim C, Wetsel WC, Kushmerick C, Pereira GS, Gainetdinov RR, Izquierdo I, Caron MG, and Prado MA

Subjects
Acetylcholine analysis, Acetylcholine metabolism, Animals, Blotting, Northern, Blotting, Southern, Brain pathology, Brain physiopathology, Brain Chemistry, Chromatography, High Pressure Liquid, Female, Male, Membrane Potentials physiology, Mice, Mice, Transgenic, Microdialysis, Motor Activity physiology, Neuromuscular Junction pathology, Neuromuscular Junction physiopathology, Neuromuscular Junction Diseases pathology, Neuromuscular Junction Diseases physiopathology, Polymerase Chain Reaction, RNA, Messenger analysis, Synaptic Transmission physiology, Vesicular Acetylcholine Transport Proteins genetics, Brain metabolism, Neuromuscular Junction metabolism, Neuromuscular Junction Diseases etiology, Recognition, Psychology physiology, Vesicular Acetylcholine Transport Proteins deficiency
Abstract

An important step for cholinergic transmission involves the vesicular storage of acetylcholine (ACh), a process mediated by the vesicular acetylcholine transporter (VAChT). In order to understand the physiological roles of the VAChT, we developed a genetically altered strain of mice with reduced expression of this transporter. Heterozygous and homozygous VAChT knockdown mice have a 45% and 65% decrease in VAChT protein expression, respectively. VAChT deficiency alters synaptic vesicle filling and affects ACh release. Whereas VAChT homozygous mutant mice demonstrate major neuromuscular deficits, VAChT heterozygous mice appear normal in that respect and could be used for analysis of central cholinergic function. Behavioral analyses revealed that aversive learning and memory are not altered in mutant mice; however, performance in cognitive tasks involving object and social recognition is severely impaired. These observations suggest a critical role of VAChT in the regulation of ACh release and physiological functions in the peripheral and central nervous system.

Published
2006
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27. Structural requirements for steady-state localization of the vesicular acetylcholine transporter.

Author

Ferreira LT, Santos MS, Kolmakova NG, Koenen J, Barbosa J Jr, Gomez MV, Guatimosim C, Zhang X, Parsons SM, Prado VF, and Prado MA

Subjects
Amino Acid Sequence, Animals, Cell Line, Clathrin physiology, Endocytosis physiology, Mice, Molecular Sequence Data, Mutagenesis, Site-Directed, PC12 Cells, Protein Conformation, Rats, Tissue Distribution, Vesicular Acetylcholine Transport Proteins, Homeostasis, Membrane Transport Proteins genetics, Membrane Transport Proteins metabolism, Synaptic Vesicles metabolism
Abstract

The vesicular acetylcholine transporter (VAChT) regulates the amount of acetylcholine stored in synaptic vesicles. However, the mechanisms that control the targeting of VAChT and other synaptic vesicle proteins are still poorly comprehended. These processes are likely to depend, at least partially, on structural determinants present in the primary sequence of the protein. Here, we use site-directed mutagenesis to evaluate the contribution of the C-terminal tail of VAChT to the targeting of this transporter to synaptic-like microvesicles in cholinergic SN56 cells. We found that residues 481-490 contain the trafficking information necessary for VAChT localization and that within this region L485 and L486 are strictly necessary. Deletion and alanine-scanning mutants lacking most of the carboxyl tail of VAChT, but containing residues 481-490, were still targeted to microvesicles. Moreover, we found that clathrin-mediated endocytosis of VAChT is required for targeting to microvesicles in SN56 and PC12 cells. The data provide novel information on the mechanisms and structural determinants necessary for VAChT localization to synaptic vesicles.

Published
2005
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28. Irreversible binding with biological macromolecules and effects in bacterial mutagenicity tests of the radical cation of promethazine and photoactivated promethazine. Comparison with chlorpromazine.

Author

De Mol NJ, Becht AB, Koenen J, and Lodder G

Subjects
Animals, Binding Sites, Biotransformation radiation effects, Cations, Cattle, Chlorpromazine metabolism, Chlorpromazine radiation effects, DNA metabolism, DNA Repair drug effects, Escherichia coli drug effects, Escherichia coli genetics, Mutagenicity Tests, Photochemistry, Promethazine metabolism, Promethazine radiation effects, Protein Binding, RNA metabolism, Salmonella typhimurium drug effects, Salmonella typhimurium genetics, Chlorpromazine toxicity, Mutagens, Promethazine toxicity
Abstract

The irreversible binding of the radical cation of promethazine (PMZ+.) to DNA and protein in vitro and bacterial macromolecules in situ has been studied. Binding experiments were performed with synthesized [35S] promethazine. The results are compared to those with the chlorpromazine radical cation (CPZ+.). Secondary reaction products which result from fission of the alkylamino side chain are involved in the macromolecular binding of PMZ+. Compared to CPZ+. the covalent DNA binding of PMZ+. is significantly less. A larger amount of PMZ+. binds to single-stranded DNA than to double-stranded DNA. The extent of binding to proteins and RNA is of the same order as that of CPZ+. Bacterial mutagenicity tests show that the low genotoxicity of PMZ+. is related to the low DNA binding. The bacterial cytotoxicity is possibly related to the covalent protein binding. Similar results have been obtained with photoactivated promethazine (PMZ) and chlorpromazine (CPZ). The role of radical cations in the photosensitization and metabolic activation of phenothiazine drugs is discussed.

Published
1986
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29. Degradation products of the promethazine radical cation.

Author

De Mol NJ and Koenen J

Subjects
Cations, Chromatography, High Pressure Liquid, Free Radicals, Horseradish Peroxidase, Hydrogen Peroxide, Magnetic Resonance Spectroscopy, Mass Spectrometry, Promethazine analysis
Abstract

The degradation products of the promethazine radical cation, generated from promethazine with horseradish peroxidase/H2O2, have been investigated. Several products have been identified which resulted from fission of the bond between the two ethanamine carbon atoms of the N10 side chain. The main product (approx. 90%) was identified as 10-formyl-5-oxophenothiazine. The likely structure of three minor products was also elucidated. The degradation of the promethazine radical cation is different from that of radical cations derived from the propanamine side chain containing phenothiazine drugs.

Published
1985
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