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5. Third International Symposium for health professionals in rheumatology: Enschede 6–9 June 1990

Author

Lorig, K., Seydel, E., Taal, E., Rasker, H., Basler, H. D., Geidel, H., Leuschner, G., Verreusel, R. L. P., Lubberts E. W., Theunisse H. A. M., Falkenbach, A., Wigand, R., Kaltwasser, P., Clayson, M., Phillips, P., Graafsma, E. A. M., Riemsma, R., Brus, H., Rasker, J. J., Cziske, R., Jaeckel, W. H., Jacobi, E., Manshanden, M. A. C., Schenk, F. C., Dijkmans, B. A. C., Nordenskiöld, U., Harmer, R., Wright, V., Hill, J., Bird, H., Elst, Ph., Eshof, I. v. d., Fits, I. v. d., Laar, M. v. d., Willigen, J. v., Boomgaardt, I. K., Tulleken, J. E., de Vries, E. G. E., van Rijswijk, M. H., Lankveld, W. v., Daamen, K., Bosch, P. v. 't Pad, Richardson, M. U. S., Huiskes, C. J. A. E., Kraaimaat, F. W., Bijlsma, J. W. J., de Witte, L. P., Winants, B. A. C., Tilli, D. J. P., van der Linden, Sj., van der Horst, F. G., Groen, J. J., Sargautyté, R., Kočiùnas, R., Ammer, K., Karetta, M., Samuelsson, A., Bjelle, A., Sullivan, M., Pincus, T., Callahan, L. F., Persson, L. O., Berglund, K., Kuiper, C. H. Z., Poulsen, A., Oosterveld, F. G. J., Jacobs, J. W. G., Overmars, H. J. A., Uytterhoeven, R., Keulemans, M., Dequeker, J., Geusens, P., Struthers, T. J., Brown, J., Dapper, M. M. L., Phiferons, H., van der Velde, E. A., Janssen, M., Raspe, H. H., Mattussek, S., Deck, R., Malcus-Johnson, P., Sandqvist, G., van Veldhoven, G., Demeester, V., Bird, H. A., Maycock, J., Peeters, W., Welkenhuysen, M., Cartois, J., Wassenaar, W. H., Tulleken, J. E., Tromp, C. N., Löfkvist, U., Eberhardt, K., Kessler, S., Potthoff, P., Ekdahl, Ch., Brooks, R. H., Bakker, C. H., Rutten-van Mölken, M., van Doorslaer, E., Boykinov, I. N., Lolkema, W., van Leeuwen, M. A., Fordham, J. N., Stamp, J., Holwerda-Straver, I., Wexsahl, H., Torud, Y., Eggen, A. E., Kruse-Jensen, A., Munthe, E., Lubberts, E. W., Lacko, B. J. S., Theunisse, H. A. M., van Riel, P. L. C. M., Bos, A. M. E., Brattström, M., Thorsell, U., Widell, G., Claesson, K., Karlsson, L., Struthers, J., Doeglas, D., Suurmeijer, Th., Sanderman, R., Krol, B., Tuinstra, J., Suurmeyer, Th. P. B. M., Pelt, R. A. G. B., Goei The, H. S., Thomassen, J. M. C., Damhuis-Friedrich, E., Chikanza, I. C., Panayi, G. S., Forre, O., Fredriksen, B., Bakken, L., Guillemin, F., Larsson, B. M, Nived, K., Eberharsdt, K., Ahlund, O., Briancon, S., Baumann, M., Kroll, B., Douglas, D., Suurmeijer, T., Le Gallez, P., Siesling, M., Brown, G. M. M., Jessop, S., Ropers, G., Sangha, O., Kriegel, W., Konietzny, G., Suurmeijer, Th. P. B. M., Skarulis, R., Gaigaliene, B., Raistenskis, J., Ceremnych-Aleksejenko, E., Cobotas, M., Barlow, J. H., Macey, S. J., Struthers, G., Gorjaev, Y. A., Menshikova, L. V., Fahmy, Z., Braun, B., Lohmann, J., Members of European Research on Incapacitating Disease and Social Support, and Arthritis team

Published
1990
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8. TRACE ELEMENTS AND RHEUMATOID ARTHRITIS(RA)- PATHOGENETIC AND THERAPEUTIC ASPECTS

Author

Egil Jellum, Munthe E, and Jan Aaseth

Subjects
Arthritis, Pharmacology, Toxicology, Arthritis, Rheumatoid, Selenium, chemistry.chemical_compound, Superoxides, medicine, Humans, Metallothionein, Sulfhydryl Compounds, Chelating Agents, business.industry, Superoxide, Penicillamine, Glutathione, medicine.disease, Zinc, chemistry, Metals, Rheumatoid arthritis, Immunology, Liberation, Gold, business, Copper, Intracellular, medicine.drug
Abstract

Rheumatoid arthritis is characterized by increased activity of macrophages which produce toxic forms of oxygen. Such oxygen has been suggested as mediator also of rheumatoid inflammation. Gold accumulates in lysosomes of the macrophages and stabilizes lysosomal and other cell membranes leading to reduced liberation of toxic oxygen. Intracellular production of metallothionein can be induced. Zinc in high doses parenterally can immobilize macrophages and also induce metallothionein-like proteins. Copper and zinc are components of SOD which detoxifies oxygen, and copper-thiolate complexes are reported to be anti-inflammatory. The therapeutic effect of penicillamine and other thiols like aurothiomalate may also be related to an anti-oxidative action. Therapeutic induction of increased intracellular levels of glutathione or administration of selenium in such a form that it incorporates into glutathione-peroxidase and increases the efficacy of the enzyme may lead to accelerated metabolism of toxic oxygen.

Published
2009

10. Fourth European Workshop on Inflammation Wilrijk March 1982

Author

Hartung, H. P., Bitter-Suermann, D., Hadding, U., Maillet, F., Lambré, C., Kazatchkine, M., Kalter, E. S., van Dijk, W. C., Timmermans, A., Verhoef, J., Bouma, B. N., Doekes, G., Daha, M. R., van Es, L. A., Drummond, L., Gemmell, D. K., Rampart, M., Bult, H., Herman, A. G., Gemsa, D., Fischer, E., Jouvin, M. H., Hartwig, H. P., Parnham, M. J., Winkelmann, J., Pelletier, M., Giroud, J. P., Schreurs, A. J. M., Nijkamp, F. P., Ouwendijk, R. J. T., Zijlstra, F. J., Wilson, J. H. P., Bonta, I. L., Vincent, J. E., Thomas, L. L. M., Büller, H. R., Sturk, A., Joop, K., Cate, J. W. ten, Henricks, P., Page, C. P., Paul, W., Elliott, G. R., Adolfs, M. J. P., Rainsford, K. D., Willis, C. M., Robins, P. G., Munthe, E., Fagerhol, M., Willard, K., Jellum, E., Fontaine, J., Herchuelz, A., Famaey, J. P., Leyck, S., Etschenberg, E., Elferink, J. G. R., Riemersma, J. C., Morley, J., Cate, H. ten, Henricks, P. A., Nijkamp, F., Junien, J. L., Guillaume, M., Lakatos, C., Karran, E. H., Green, A. P., Mangan, F. R., Payne, T., Dewald, B., Siegl, H., Gubler, H. U., Ott, H., Baggiolini, M., Conti, P., Continenza, M. A., Cifone, M. G., Alesse, E., Ianni, G., Angeletti, P. U., Stolz, E., Reuse, J., Camussi G., Montrocchio G., Antro C., Tetta C., Bussolino F., Emanuelli G., Mehler, E. L., Habicht, J., Brune, K., Van Gossum, A., Cremer, M., Delronche, M., Appelboom, T., Pierart, M., Görtz, R., Deby, C., Deby-Dupont, G., Boogaerts, M. A., Vermylen, J., Deckmyn, H., Moldow, C. F., Verwilghen, R., Schrauwen, E., Weyns, A., Gillebert, Ch., Houvenaghel, A., Wickens, D. G., Dormandy, T. L., and Laekeman, G. M.

Published
1982
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11. Third Eular Workshop on Rheumatology Research: Mainz February 1983

Author

Gleichmann, E., van Rappard-van der Veen, F. M., Rolink, A. G., Pals, S. T., Trautwein, G., Hewicker, M., Waterfield, J. D., Maini, R. N., Botzenhardt, U., Müller, J., Lemmel, E. -M., Bartlett, R., Steldern, D. v., Field, M., Schrieber, L., Melsom, R. D., Venables, P. J., McCarthy, D. A., de Vries, B. J., van den Berg, W. B., van de Putte, L. B. A., van den Berg, W. B., Lens, J. W., Kruijsen, M. W. M., Brackertz, D., Mohr, W., Fritsch, R., Holmdahl, R., Rubin, K., Klareskog, L., Radaszkiewicz, T., Dreher, R., Köhler, G., Rieber, P., Weber, U., Kirchhoff, H., Heitmann, J., Hermanns, W., Schulz, L. Cl., Marquardt, J., Rojem, P., Schulz, L. C., Brighton, S. W., Vermeulen, W. A., Madhok, R., Sturrock, R. D., Forbes, C., Bennett, D., Leibold, W., Hangoc, G., Böhm, K. H., Rimpler, M., Grabczewska, E., Maslinski, W., Krzystyniak, K., Ryzewski, J., Mbuyi, J. M., Dequeker, J., Junker, P., Oxlund, H., Lorenzen, G. H., Lorenzen, I., Van Paassen, H. C., De Vries, E., Mallee, C., Bijvoet, O. L. M., Cats, A., Ball, J., Wessinghage, D., Kirkpatrick, C. J., Verbruggen, G., Luyten, F., Veys, E. M., Annefeld, M., Velvart, M., Fehr, K., Seidel, J., Menninger, H., Gurr, E., Stangel, W., Deicher, H., Fobbe, C., Starck, P., Kleesiek, K., Greiling, H., Biemond, P., Swaak, A. J. G., Koster, J. F., Hall, N. D., Maslen, C., McKeown, M. J., Parnham, M. J., Bittner, C., Hurst, N. P., Bessac, B., Nuki, G., Neumüller, J., Dunky, A., Senautka, G., Eberl, R., Lemmel, E. M., Lindgren, J. A., Appelboom, T., Gortz, R., Madia, W., Loos, M., Heinz, H. P., Mortazavi-Milani, S. M., Holborow, E. J., Lindblad, S., Hedfors, E., Meijer, C. J. L. M., Lafeber, G. J. M., Vulpen-Cnossen, J., Damsteeg, W. G. M., Warnatz, H., Lemm, G., van der Weij, J. P., van der Veen, C. J. P., Burmester, G. R., Menche, D., Merryman, P., Dimitriu-Bona, A., Klein, M., Winchester, R., Corke, C. F., Gul, V., Stierle, H., Huskisson, E. C., Holborrow, E. J., Froebel, K., Dickson, R., Lewis, D., Kávai, M., Sonkoly, I., Csongor, J., Szegedi, Gy., Schmidt, R. E., Mollenhauer, E., Heinrichs, M., Rittner, C., Schneider, E. M., Pawelec, G., Müller, C., Blaurock, M., Shaw, S., Wernet, P., Winrow, V. R., Stierle, H. E., Norton, J., March, R. E., Santana, R., Deycke, K. H., Baruth, B., Weibbarth, E., Zeller, H., Ebringer, A., Geissler, N., Hildebrand, S., Kemper, A., Krapf, E., Renger, D., Schedel, I., Zeidler, H., Mielke, H., Krauledat, P. B., Krapf, F. E., Baudner, S., Linhart, H., Kalden, J. R., Maddison, P. J., Skinner, R. P., Esscher, E., Taylor, P. V., Scott, O., Scott, J. S., Miossec, P., Youinou, P., Le Goff, P., Seigneurin, J. M., Coatalem, R., Trautmann, F., Arnold, W., Hermanns, Ph., Delanghe, J., Vansteenkiste, M., Mielants, H., Munthe, E., Jellum, E., Suykens, S., Schiller, H., Schilling, F., and Emrich, E.

Published
1983
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13. IX Eular Workshop for Rheumatology Research: Molecular biology of autoantigens, autoantibodies and immunopeptides. Vienna, Austria, March 9–12, 1989

Author

Fournier, C., Texier, B., Chiocchia, G., Boissier, M. C., Herbage, D., Brown, C. M. S., Zyberk, C. Plater, Maini, R. N., Palacios, A., Sieper, J., Heinegard, D., Panayi, G. S., Gentric, A., Mackenzie, L., Lydyard, P. M., Youinou, P., Menzel, E. J., Kaik, B., Sykulev, Yu. K., Guschin, A. Je., Vasiljev, V. I., Ostreiko, K. K., Yeronina, T. V., Tumanova, I. A., Moynier, M., Abderrazik, M., Combe, B., Rucheton, M., Brochier, J., Tuomi, T., Palosuo, T., Heliövaara, M., Aho, K., McHugh, N. J., James, I. E., Kallenberg, C. G. M., Tervaert, J. W. Cohen, Goldschmeding, R., Von Dem Borne, A. E. G. K. R., Bouanani, M., Piechaczyk, M., Pau, B., Bastide, M., Le Page, S., Williams, W., Parkhouse, D., Cambridge, G., Isenberg, D. A., Nimmegeers, J., De Keyser, F., Verbruggen, G., Veys, E. M., Walravens M. J. F., Verdeyen I., Vandepol B., Cortens W., Schatteman, L., Goethals, K., Wu, D. -H., Tavoni, A., Neri, R., Garzelli, C., Vitali, C., Bombardieri, S., Logar, D., Kveder, T., Dobovisek, J., Rozman, B., Menard, H. A., Boire, G., Lopez-Longo, F. J., Masson, Ch., Lapointe, S., Clair, E. W. St., Zerva, L., Moutsopoulos, H. M., Keene, J. D., Pisetsky, D. S., Van Dam, A. P., Cuypers, H. T. M., Winkel, I., Smeenk, R. J. T., Taylor, D., Valente, E., Foster, J. P., Williams, D. G., Stocks, M. R., Caporali, R., De Gennaro, F., Cerino, A., Cobianchi, F., Astaldi-Ricotti, G. C. B., Montecucco, C., Habets, W., Sillekens, P. T. G., Hoet, M. H., McAllister, G., Lerner, M. R., Van Venrooij, W. J., Habets, W. J., Van Der Kemp, A., De Jong, B., Scarpa, R., Pucino, A., Di Girolamo, C., della Valle, G., Larizza, G., Casiere, D., Oriente, P., Paimela, L., Palvimo, J., Kurki, P., Hassfeld, W., Steiner, G., Graninger, W., Smolen, J. S., Lopez-Longo, E. J., Larose, A., Hoet, R., Zewald, R., Smeenk, R., Brinkman, K., Van Den Brink, H., Westgeest, A., Huss, R., Krapf, E. F., Herrmann, M., Leitmann, W., Kalden, J. R., Merétey, K., Cebecauer, L., Böhm, U., Kozakova, D., Brózik, M., Temesvári, P., Nagy, L., Bozic, B., Stegnar, M., Vene, N., Peternel, P., Giuggioli, C., Monti, P., Rossi, G., Ferri, C., Chiellini, S., Baboonian, C., Venables, P. J. W., Roffe, L., Booth, J., Krapf, F., Abuljadayel, I., Ebringer, A., Cox, N. L., Brand, S. R., McIntosh, D. P., Bernstein, R. M., Van Den Broek, M. F., Van Bruggen, M. C. J., Smetsers, T., Kuyer, P., Van De Putte, L., Van Den Berg, W. B., Toivanen, A., Jalkanen, S., Lahesmaa-Rantala, R., Isomäki, O., Pekkola-Heino, K., Merilahti-Palo Saario, R., Von Essen, R., Isomäki, H., Granfors, K., Gaston, J. S. H., Life, P. F., Bailey, L., Bacon, P. A., Khalafpour, S., Wilson, C., Awad, J., Toivanen, P., Saario, R., Skurnik, M., Van Der Straeten, C., Mielants, H., Gazic, M., Hartung, K., Riedel, T., Stannat, S., Specker, Ch., Röther, E., Pirner, K., Schendel, D., Baur, M., Corvetta, A., Peter, H. H., Lakomek, H. J., Deicher, H., Andonopoulos, A. P., Papasteriades, C. A., Drosos, A. A., Dimou, G. S., Shattles, W., Venables, P., Charles, P. J., Markwick, J. R., Venables, P. J., Galeazzi, M., Lulli, P., Tuzi, T., Cappellacci, S., Morellini, M., Trabace, S., Cutrupi, F., Sorrentino, R., Botti, S., Iannicola, C., Costanzi, S., Tosi, R., Gospodinoff, A., Eliaou, J. F., Humbert, H., Balaguer, P., Nicolas, J. C., Sany, J., Clot, J., Sakkas, L. I., Bird, H., Welsh, K. I., Pitzalis, C., Kingsley, G., Haskard, D., Vischer, T. L., Bas, S., Werner-Favre, C., Wohlwend, D., Zubler, R. H., Afeltra, A., De Pita, O., Basso, P., Pietrucci, A., Ferri, G. M., Bonomo, L., Gerli, R., Cernetti, C., Bertotto, A., Agea, E., Arcangeli, C., Lanfrancone, L., Rambotti, P., Crupi, S., Baglioni, A., Spinozzi, F., Papazoglou, S., Skoumi, D., Athanasiou, P., Iliopoulos, A., Stavropoulou, A., Kontomerkos, T., Hendrich, G., Kuipers, J. G., Hammer, M., Schmidt, R. E., Manoussakis, M. N., Germandis, G., Zerva, L. V., Siouna-Fatourou, H. J., Katsikis, P. D., Mavridis, A., Toubert, A., Sadouk, M., de la Tour, B., Vaquero, C., Amor, B., Miossec, P., Naviliat, M., Cretien, I., Banchereau, J., Graninger, P., Aschauer, B., Sinski, A., Smolen, J., Krutmann, J., Kirnbauer, R., Köck, A., Schwarz, T., May, L. T., Sehgal, P. B., Luger, T. A., Field, M., Chu, C. Q., Feldmann, M., Wilbrink, B., Nietfeld, J. J., Helle, M., Boeije, L. C. M., Van Roy, J. L. A. M., Den Otter, W., Aarden, L. A., Huber-Bruning, O., Malejczyk, J., Urbanski, A., Malejczyk, M., Karbowski, A., Völker, W., Feige, U., Otter, W. Den, Malfait, A. M., Wieme, N., Gyselbrecht, L., Van de Loo, A. A. J., Van Lent, P. L. E. M., Haskard, D. O., Wellicome, S., Lanchbury, J., Thornhill, M., Krutmann, K., Gschnait, F., Yaron, M., Yaron, I., Dayer, J. -M., Bleiberg, I., Meyer, F. -A., Maury, C. P. J., Teppo, A. -M., Salo, E., Pelkonen, P., Malfait, A., Cochez, Ph., Gruschwitz, M., Müller, P. U., Wick, G., Madhok, R., Wilson, R., Frame, M., Thompson, J., Sturrock, R. D., Partsch, G., Matucci-Cerinic, M., Marabini, S., Jantsch, S., Neumüller, J., Eberl, R., van Beuningen, H. M., Arntz, O. J., Zlabinger, G. J., Steffen, C., Brand, H. S., Van Kampen, G. P. J., De Koning, M. H. M. T., Kiljan, E., Van Der Korst, J. K., Gemmell, C. G., Swaak, A. J. G., Van Rooyen, A., Hall, N. D., Woolf, A. D., Kantharia, B., Maymo, J., Blake, D. R., Goulding, N. J., Maddison, P. J., Munthe, E., Berntzen, H. B., Fagerhol, M., Mathieu, A., Pala, R., Contu, L., Cirillo, R., Garau, P., Nurchis, P., Viberti, G. C., Meyer, O., Zenklusen, C., Le Thi Huong Du, Z., Gaudouen, C., Mery, J. Ph., Ronco, P., Kahn, M. F., Rasmussen, N., Szpirt, W., Thomsen, B., Humbel, R. L., Ter Borg, E. J., Horst, G., Hummel, E., Limburg, P. C., Aeschilmann, A., Bourgeois, P., De Rooij, D. J., Van de Putte, L. B. A., Verbeek, L., Farinaro, C., Infranzi, E., Couret, M., Ackerman, C., De Vlam, K., Carapic, V., Carapic, D., Annefeld, M., Erne, B., Rosenwasser, L. J., Pazoles, C. J., Otterness, I. G., Hanson, D. C., McDonald, B., Loose, L. D., Dougados, M., Machold, K. P., Wiesenberg-Böttcher, I., Wanner, K., Pignat, W., Altmann, H., Tuschl, H., Bröll, H., Balestrieri, G., Tincani, A., Cattaneo, R., Bertoli, M. T., Martinelli, M., Allegro, F., Meroni, P. L., Balesini, G., Aichinger, G., Schlögl, E., Huber, Ch., Shoenfeld, Y., Fleishmaker, E., Mendlovic, S., Mozes, E., Blank, M., Talal, N., Hogervorst, E. J. M., Van Eden, W., Van Der Zee, R., Psychos, D., Dimou, G., Stefanaki-Nikou, S., Papadimitriou, C. S., Settas, L., Alexiou, P., Dimitriadis, G., Mataftsi, E., Soliou, E., Tourkantonis, A., Babic, M., Jeurissen, M. E. C., and Boerbooms, A. MTh

Published
1989
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16. Dendritic cells engineered to express defined allo-HLA peptide complexes induce antigen-specific cytotoxic T cells efficiently killing tumour cells

Author

Stronen, E, Abrahamsen, I W, Gaudernack, G, Wälchli, S, Munthe, E, Buus, S, Johansen, F-E, Lund-Johansen, F, Olweus, J, Stronen, E, Abrahamsen, I W, Gaudernack, G, Wälchli, S, Munthe, E, Buus, S, Johansen, F-E, Lund-Johansen, F, and Olweus, J

Abstract

Udgivelsesdato: 2009-Apr, Most tumour-associated antigens (TAA) are non-mutated self-antigens. The peripheral T cell repertoire is devoid of high-avidity TAA-specific cytotoxic T lymphocytes (CTL) due to self-tolerance. As tolerance is major histocompatibility complex-restricted, T cells may be immunized against TAA presented by a non-self human leucocyte antigen (HLA) molecule and transferred to cancer patients expressing that HLA molecule. Obtaining allo-restricted CTL of high-avidity and low cross-reactivity has, however, proven difficult. Here, we show that dendritic cells transfected with mRNA encoding HLA-A*0201, efficiently present externally loaded peptides from the antigen, Melan-A/MART-1 to T cells from HLA-A*0201-negative donors. CD8(+) T cells binding HLA-A*0201/MART-1 pentamers were detected already after 12 days of co-culture in 11/11 donors. The majority of cells from pentamer(+) cell lines were CTL and efficiently killed HLA-A*0201(+) melanoma cells, whilst sparing HLA-A*0201(+) B-cells. Allo-restricted CTL specific for peptides from the leukaemia-associated antigens CD33 and CD19 were obtained with comparable efficiency. Collectively, the results show that dendritic cells engineered to express defined allo-HLA peptide complexes are highly efficient in generating CTL specifically reacting with tumour-associated antigens.

Published
2009

24. Complement-fixing Granulocyte-specific Antinuclear Factors in Neutropenic Cases of Rheumatoid Arthritis.

Author

Wiik, A. and Munthe, E.

Subjects
*GRANULOCYTES, *ANTINUCLEAR factors, *RHEUMATOID arthritis, *NEUTROPENIA, *IMMUNOGLOBULIN G, *AUTOIMMUNE diseases
Abstract

Forty-one sera from patients with rheumatoid arthritis (RA) and accompanying neutropenia, including twenty-one with Felty's syndrome, were studied to investigate the occurrence and determine the titres of granulocytespecific antinuclear factors (GS-.A.NF) belonging to the three main immunoglobulin classes. Furthermore complement (C3) fixing GS-ANF and rheumatoid factors were titrated in the sera. Complement-fixing GS-ANF were found in thirty-five of these sera compared with only four out of twenty-eight sera from RA patients without neutropenia. Complement-fixing GS-ANF were similarly detected in all of six sera from non-arthritic patients with severe neutropenia and positive Waaler-Rose tests. Complement-fixing properties of the antibodies were mostly found in sera containing high titres of GS-ANF of the IgG and IgM classes, but the titres of complement-fixing GS-ANF were on the whole markedly lower than the corresponding IgG and IgM antibody titres. A direct autoaggressive activity of complement-fixing GS-ANF on the neutrophilic granulocytes or their precursors is suggested. [ABSTRACT FROM AUTHOR]

Published
1974

29. Fate of the gold and the thiomalate part after intramuscular administration of aurothiomalate to mice.

Author

Jellum, E, Munthe, E, Guldal, G, and Aaseth, J

Abstract

Double isotope-labelled aurothiomalate (195Au-14C-thiomalate) has been administered to mice, and the excretory fate and tissue distribution have been studied. The results show that the gold and the thiomalate separate in vivo resulting in protein-bound gold and release of free thiomalate. About half of this thiol is excreted in the urine during the first day, and the remaining half is bound to tissue membranes and cells. Although thiomalate penetrates cellular membranes slowly in vitro. the compound is found in all organs, mostly in the liver and the kidneys, after administration of aurothiomalate. Separation of the gold moiety from its thiol carrier also takes place in man. This explains the finding of free thiomalate in the urine of patients receiving aurothiomalate intramuscularly. As thiomalate has now been shown to possess penicillamine-like biological activities it is suggested that at least part of the antirheumatic effects of aurothiomalate may be due to the thiol carrier being released in the body. [ABSTRACT FROM AUTHOR]

Published
1980
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30. Studies on cold insoluble globulin. I Concentrations in citrated plasma in rheumatic disorders.

Author

Fyrand, O, Munthe, E, and Solum, N O

Abstract

Cold insoluble globulin (CIG) is a normal glycoprotein of human serum and plasma. The physiological significance of this protein is unknown, but is shows a temperature-dependent relation to fibrinogen and fibrin. It is possible that it represents a substrate for activated fibrin-stabilising factor in the polymerisation of fibrin. CIG is found on the surface of fibroblasts. In the present study CIG was estimated in citrated plasma in 115 patients with rheumatic diseases. Increased amounts were found in patients with systemic lupus erythematosus, secondary amyloidosis in classical and definite rheumatoid arthritis, and in male patients with juvenile rheumatoid arthritis. [ABSTRACT FROM PUBLISHER]

Published
1978
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31. No effect of transfer factor in juvenile rheumatoid arthritis by double-blind trial.

Author

Høyeraal, H M, Frøland, S S, Salvesen, C F, Munthe, E, Natvig, J B, Kåss, E, Blichfeldt, P, Hegna, T M, Revlem, E, Sandstad, B, and Hjort, N L

Subjects
CLINICAL trials, COMPARATIVE studies, DELAYED hypersensitivity, IMMUNOLOGY technique, LYMPHOKINES, RESEARCH methodology, MEDICAL cooperation, RESEARCH, JUVENILE idiopathic arthritis, EVALUATION research, RANDOMIZED controlled trials, BLIND experiment, ARTHRITIS Impact Measurement Scales
Abstract

A previously pilot study of treatment with transfer factor in 3 patients with juvenile rheumatoid arthritis (JRA) gave promising results. However, in this small and open study no definite conclusions could be drawn. Therefore, a double-blind group trial was performed in 12 JRA patients treated with transfer factor, and in 12 placebo-treated control patients. The patients were evaluated clinically, by laboratory tests, and by estimation of different lymphocyte populations and cell-mediated immunity in vitro and in vivo. Transfer factor was not found to be of significant therapeutic value in patients with JRA. The only statistically significant difference between the two groups was a greater reduction in the percentage of T lymphocytes in transfer factor-treated patients than in control patients. The significance of this is difficult to explain and could have appeared by chance. No side effects of treatment with transfer factor were noted. [ABSTRACT FROM PUBLISHER]

Published
1978
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32. Effect of penicillamine on complement in vitro and in vivo.

Author

Mellbye, O J and Munthe, E

Abstract

In most normal human sera the addition of penicillamine to a final concentration of 0-2 mmol/l and subsequent dialysis caused a slight reduction in serum haemolytic complement (CH50). At 200 mmol/l, CH50 activity was no longer demonstrable. Even high concentrations of penicillamine were needed to inhibit the ability of immunoglobulin to fix complement to preformed or forming immune complexes. This indicated that the reduction of CH50 observed in serum was due to an effect on the complement factors. In vivo, a dose of 240 mg penicillamine caused a slight transient reduction in CH50 in rabbit serum, while 1000 mg penicillamine had no effect on serum CH50 in patients with rheumatoid arthritis. In arthritis patients there was, however, some evidence for removal of complement deposits in synovial tissue during penicillamine treatment. Since it is theoretically possible that concentrations high enough to cause reduction of complement activity can be achieved locally in synovial tissue, the effect on complement may be one of the mechanisms by which penicillamine exerts its effect in rheumatoid arthritis. [ABSTRACT FROM PUBLISHER]

Published
1977
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33. Complement and immunoglobulins in synovial fluid from synovectomized patients with rheumatoid arthritis.

Author

Mellbye, O J, Naes, B, and Munthe, E

Subjects
AUTOANTIBODY analysis, KNEE surgery, IMMUNOGLOBULIN analysis, AGAR, COMPLEMENT (Immunology), ELECTROPHORESIS, IMMUNOELECTROPHORESIS, RHEUMATOID arthritis, SYNOVIAL fluid
Abstract

In order to see if the complement (C) consumption and conversion, which are typical of rheumatoid joints, continue after synovectomy, 23 knee joints in which synovectomy had been performed from 4-5 to 6-5 years previously, were studied. The mean ratio of the concentration of C3, C4, and C5 in synovial fluid to that in palsma of the same patient was significantly lower than the corresponding ratio for the total protein content. This was found both in joints with active arthritis and in joints without clinical signs of arthritis, and in both seropositive and seronegative patients. Conversion products of C3 were found in 7 of the synovial fluids. The study thus indicated that the complement alterations in synovectomized joints are very similar to those in nonsynovectomized rheumatoid joints. In one synovial fluid agarose electrophoresis showed multiple sharp bands in the gamma region. By crossed immunoelectrophoresis some bands seemed to contain IgG with one type of light chains only. In plasma of the same patients the bands were much weaker, indicating local production of oligoclonal IgG in the joint. [ABSTRACT FROM PUBLISHER]

Published
1976
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40. IMMUNOGLOBULIN CLASSES, SUBCLASSES AND COMPLEXES OF IgG RHEUMATOID FACTOR IN RHEUMATOID PLASMA CELLS.

Author

Munthe, E. and Natvig, J. B.

Subjects
*IMMUNOGLOBULINS, *GLOBULINS, *PLASMA cells, *RHEUMATOID factor, *IMMUNOGENETICS, *IMMUNOLOGY
Abstract

The different immunoglobulin classes, IgG subclasses and types of light chains in plasma cells of thirty-four rheumatoid synovial membranes were studied. In some of these membranes a particular Ig class or IgG subclass was selectively concentrated, indicating local production of antibodies. Large amounts of plasma cells containing IgG were detected in all tissues. In contrast, many synovial membranes contained only few plasma cells with free rheumatoid factor activity, shown by binding of aggregated IgG. However, after pepsin digestion of tissue sections, greatly increased numbers of plasma cells were able to bind IgG. Our results indicated that the majority of plasma cells of rheumatoid tissues contained rheumatoid factors, but these were mostly blocked, due to intracellular complexing of IgG rheumatoid factors. [ABSTRACT FROM AUTHOR]

Published
1972

41. SPECIFIC BINDING OF IMMUNOCONGLUTININ IN TISSUES AND SYNOVIAL FLUIDS FROM PATIENTS WITH RHEUMATOID ARTHRITIS.

Author

Mellbye, O. J. and Munthe, E.

Subjects
*TISSUES, *PEPSIN, *IMMUNOGLOBULINS, *PATIENTS, *SERUM, *GENETICS
Abstract

in eluates from rheumatoid synovial tissue, immunoconglutinin was present in only one of fifteen cases. After pepsin digestion, immunoconglutinin activity was increased or revealed in almost all eluates examined. Natural antibodies, present in the corresponding sera, could not be detected in the eluates before or after pepsin digestion. Neither was any immunoconglutinin present or revealed in eluates from non-rheumatoid synovial tissue. The experiments indicated that this antibody is specifically fixed in synovial tissue of patients with rheumatoid arthritis. The immunoconglutinin activity in the eluates was probably due to an IgG antibody. Density gradient ultracentrifugation and treatment with 2-ME indicated that both IgO and IgM immunoconglutinin were present in sera from these patients. In rheumatoid synovial fluids, immunoconglutinin was present in an amount equal to, or somewhat lower than in serum. By density gradient ultracentrifugation at pH 3.0, IgG immunoconglutinin activity seemed to be revealed or increased in most cases, indicating a fixation of this antibody also in synovial fluids. Immunoconglutinin in human sera could be absorbed out with immune precipitates exposed to fresh human serum, and this reaction seemed to increase the complement fixing ability of the precipitates. If binding of immunoconglutinin in rheumatoid synovial tissue and synovial fluids increases complement fixation and activation in a similar way, it might be a pathogenetic factor in the rheumatoid inflammation. [ABSTRACT FROM AUTHOR]

Published
1971

42. CHARACTERIZATION OF IgG COMPLEXES IN ELUATES FROM RHEUMATOID TISSUE.

Author

Munthe, E. and Natvig, J. B.

Subjects
*IMMUNOGLOBULIN G, *RHEUMATOID arthritis, *RHEUMATOID factor, *IMMUNOGLOBULIN M, *SYNOVIAL fluid, *GRANULATION tissue, *IMMUNOGENETICS
Abstract

Eluates of rheumatoid synovial and other rheumatoid granulation tissues both from seropositive and seronegative patients contained complexes of IgG, reacting with isolated IgM rheumatoid factor. According to gel filtration patterns, the molecular size of the complexes was similar to or even higher than that of heat-aggregated lgG. Patients with active disease and large amounts of IgG complexes in the tissue eluates often had low titres of free IgM rheumatoid factor both in eluates and in serum. This suggested an in vivo binding of IgM rheumatoid factor to tissue IgG complexes. A selection of Gm markers was observed in some eluates, compared to the corresponding markers in whole serum. The eluate IgG thus consisted partly of a restricted population of IgG molecules. After pepsin treatment of the IgG complexes to destroy Fc antigens, rheumatoid factor activity, not present in the untreated complexes, was revealed. This indicated that lgG antibodies to IgG took part in complex formation. [ABSTRACT FROM AUTHOR]

Published
1971

43. Restrictions Among Heavy and Light Chain Determinants of Granulocyte-Specific Antinuclear Factors.

Author

Wiik, A. and Munthe, E.

Subjects
*ANTINUCLEAR factors, *AUTOANTIBODIES, *IMMUNOGLOBULINS, *AUTOIMMUNITY, *GRANULOCYTES, *ANTIGENS, *IMMUNITY, *IMMUNOLOGY
Abstract

In fifty-five rheumatoid arthritis sera with positive granulocytespecific antinuclear factors (GS-ANF) tests were made to further characterize these antibodies. All sera contained GS-ANF of the IgG class and most of the sera also of the IgM and IgA classes, whereas only about 10 per cent of the sera contained GS-ANF of the IgD class. Most of the sera contained GS-ANF carrying both κ and λ light chain determinants, but in five cases only one of the light chain subclasses could be found. The distribution of the GS-ANF among the four subclasses of IgG showed marked variations. From one to three subclasses could be lacking or noticeably depressed. There was no predominance of any one or two subclasses. Complement (C3) fixing properties correlated with GS-ANF of the IgG1 and/or IgG3 subclasses. These properties make the GS-ANF interesting as possible pathogenic factors in rheumatoid arthritis. Some evidence is presented that the GS-ANF may be directed against several different antigens in the polymorphonuclear granulocyte nuclei. [ABSTRACT FROM AUTHOR]

Published
1972

44. Complement-Fixing Intracellular Complexes of IgG Rheumatoid Factor in Rheumatoid Plasma Cells.

Author

Munthe, E. and Natvig, J. B.

Subjects
RHEUMATOID factor, IMMUNOGLOBULIN G, PLASMA cells, SYNOVIAL membranes, CELLULAR mechanics
Abstract

Intracellular rheumatoid factor activity is found mostly in IgM plasma cells of rheumatoid synovial membranes from seropositive patients, while tissues from seronegative patients nearly always lack free rheumatoid factor. However, rheumatoid factor activity can be revealed in a considerable number of IgG plasma cells by pepsin digestion of tissues both from seropositive and seronegative patients. This activity has been further characterized by sequential double immunofluorescence staining. It was demonstrated in plasma cells representing each of the four IgG subclasses. The proportion of rheumatoid plasma cells with this activity varied in tissues from different individuals, but in some seronegative cases about 50% or more of the IgG plasma cells contained such 'hidden' rheumatoid factor. Most of the IgG rheumatoid factors in plasma cells possessed the ability to react with several IgG subclass proteins, and were thus often directed against antigens common to two or more subclasses. The results gave evidence of intracellular blocking of rheumatoid factor activity, due to IgG-IgG rheumatoid factor complexes. Additional evidence of such plasma cell complexes was obtained by observing an in vitro fixation of the complement components Clq and C3 to such cells. The fixation of aggregated IgG to extracellular deposits and to inclusions in synovial lining cells and joint fluid leukocytes was due to Clq as well as to rheumatoid factor. [ABSTRACT FROM AUTHOR]

Published
1972
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46. No effect of transfer factor in juvenile rheumatoid arthritis by double-blind trial

Author

Stig S. Frøland, T. M. Hegna, C. F. Salvesen, Kåss E, P. Blichfeldt, B. Sandstad, N. L. Hjort, J B Natvig, Hoyeraal Hm, Munthe E, and E. Revlem

Subjects
medicine.medical_specialty, Adolescent, Lymphocyte, Immunology, Transfer Factor, Lymphocyte Activation, Gastroenterology, General Biochemistry, Genetics and Molecular Biology, Double blind, Double-Blind Method, Rheumatology, In vivo, Internal medicine, medicine, Humans, Immunology and Allergy, Hypersensitivity, Delayed, In patient, Child, Clinical Trials as Topic, Group trial, business.industry, Transfer factor, Significant difference, medicine.disease, Arthritis, Juvenile, medicine.anatomical_structure, business, Juvenile rheumatoid arthritis, Research Article
Abstract

A previously pilot study of treatment with transfer factor in 3 patients with juvenile rheumatoid arthritis (JRA) gave promising results. However, in this small and open study no definite conclusions could be drawn. Therefore, a double-blind group trial was performed in 12 JRA patients treated with transfer factor, and in 12 placebo-treated control patients. The patients were evaluated clinically, by laboratory tests, and by estimation of different lymphocyte populations and cell-mediated immunity in vitro and in vivo. Transfer factor was not found to be of significant therapeutic value in patients with JRA. The only statistically significant difference between the two groups was a greater reduction in the percentage of T lymphocytes in transfer factor-treated patients than in control patients. The significance of this is difficult to explain and could have appeared by chance. No side effects of treatment with transfer factor were noted.

Published
1978

47. Some Aspects of the Mechanism of Action of Penicillamine in Rheumatoid Arthritis

Author

Jan Aaseth, Munthe E, and Egil Jellum

Subjects
Chemical Phenomena, Immunology, Bioinformatics, Arthritis, Rheumatoid, Rheumatology, Animals, Humans, Immunology and Allergy, Medicine, Sulfhydryl Compounds, Aldehydes, Immunity, Cellular, business.industry, Cell Membrane, Penicillamine, DNA, General Medicine, medicine.disease, Enzymes, Chemistry, Mechanism of action, Rheumatoid arthritis, Prostaglandins, RNA, Collagen, medicine.symptom, business, medicine.drug
Published
1979

48. Is Gold Necessary in So Called Chrysotherapy?

Author

Egil Jellum and Munthe E

Subjects
Sodium, Immunology, Anti-Inflammatory Agents, chemistry.chemical_element, Urine, Pharmacology, Injections, Intramuscular, Gold Sodium Thiomalate, Arthritis, Rheumatoid, Mice, Structure-Activity Relationship, Rheumatology, In vivo, medicine, Animals, Humans, Immunology and Allergy, Tissue Distribution, Carbon Radioisotopes, chemistry.chemical_classification, Clinical Trials as Topic, business.industry, Penicillamine, General Medicine, Response to treatment, Sodium aurothiomalate, Rats, Clinical trial, Kinetics, chemistry, Thiol, business, medicine.drug
Abstract

It is postulated that the efficacy of sodium aurothiomalate and d-penicillamine could be partly dependent on the activity of sulphydryl groups. Free thiomalate, the thiol from sodium aurothiomalate was shown to be liberated in vivo and has been detected in the blood and urine of sodium aurothiomalate-treated patients. An increase in intracellular glutathione levels in response to treatment with sodium aurothiomalate and penicillamine was demonstrated and considered to be related to these drugs' properties as thiols. A pilot clinical trial using sodium thiomalate treatment demonstrated clinical improvement in four out of six patients after one course. Two patients relapsed but both improved after a second course and there were no serious adverse reactions. It is concluded that although larger controlled clinical trials are required, the role of gold in "chrysotherapy" must remain in question.

Published
1983

49. Orthopaedic Surgery for Childhood Arthritis

Author

Munthe E, Erik Kåss, and Jan Pahle

Subjects
medicine.medical_specialty, Rheumatology, Childhood arthritis, business.industry, General surgery, Orthopedic surgery, medicine, medicine.disease, business
Published
1978

50. Fate of the gold and the thiomalate part after intramuscular administration of aurothiomalate to mice

Author

Munthe E, Jan Aaseth, G. Guldal, and Egil Jellum

Subjects
Cell Membrane Permeability, Erythrocytes, Time Factors, Immunology, Urine, Pharmacology, Gold Sodium Thiomalate, Injections, Intramuscular, General Biochemistry, Genetics and Molecular Biology, Mice, Rheumatology, In vivo, medicine, Animals, Humans, Immunology and Allergy, chemistry.chemical_classification, Thiomalates, business.industry, Penicillamine, Blood Proteins, Blood proteins, In vitro, chemistry, Excretory system, Thiol, Female, Gold, business, Research Article, Protein Binding, medicine.drug
Abstract

Double isotope-labelled aurothiomalate (195Au-14C-thiomalate) has been administered to mice, and the excretory fate and tissue distribution have been studied. The results show that the gold and the thiomalate separate in vivo resulting in protein-bound gold and release of free thiomalate. About half of this thiol is excreted in the urine during the first day, and the remaining half is bound to tissue membranes and cells. Although thiomalate penetrates cellular membranes slowly in vitro. the compound is found in all organs, mostly in the liver and the kidneys, after administration of aurothiomalate. Separation of the gold moiety from its thiol carrier also takes place in man. This explains the finding of free thiomalate in the urine of patients receiving aurothiomalate intramuscularly. As thiomalate has now been shown to possess penicillamine-like biological activities it is suggested that at least part of the antirheumatic effects of aurothiomalate may be due to the thiol carrier being released in the body.

Published
1980

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