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1. Characterization of mouse lines transgenic with the human poliovirus receptor gene

Author

G McMullen, A.J Johnson, S.P Nawoschik, J.W Coleman, A.M Deatly, Carolyn Louise Weeks-Levy, Vincent R. Racaniello, J.M McAuliffe, and Rolf E. Taffs

Subjects
Male, Genes, Viral, Transgene, Gene Dosage, Mice, Transgenic, Biology, medicine.disease_cause, Microbiology, Virus, Mice, Western blot, medicine, Animals, Humans, Receptor, Gene, Southern blot, Virulence, medicine.diagnostic_test, Poliovirus, Brain, Membrane Proteins, RNA, Virology, Molecular biology, Mice, Inbred C57BL, Infectious Diseases, Receptors, Virus, Female, Polymorphism, Restriction Fragment Length
Abstract

Two mouse lines transgenic with the human poliovirus receptor gene (PVR), TGM-PRG-1 and TGM-PRG-3, were characterized to determine whether transgene copy number and PVR expression levels influence susceptibility to poliovirus. The mouse lines have been bred for more than 10 generations and the transgene was stably transmitted to progeny as determined by Southern blot hybridization and restriction fragment length polymorphism. The transgene copy number is 10 in the TGM-PRG-3 mouse line and one in the TGM-PRG-1 mouse line. Abundance of PVR RNA is on average three-fold higher in TGM-PRG-3 relative to TGM-PRG-1 tissues, and the abundance of the receptor molecule is three-fold higher in TGM-PRG-3 central nervous system tissues compared to TGM-PRG-1 tissues as determined by Western blot analysis. When TGM-PRG-1 and TGM-PRG-3 mice were inoculated intracranially with a neurovirulent type III poliovirus strain, they developed clinical symptoms and CNS lesions characteristic of human poliomyelitis. These results indicate that the PVR gene is expressed as a functional receptor in the CNS of both mouse lines rendering the mice susceptible to poliovirus infection. Even though the two mouse lines have different copy numbers of the transgene and different levels of PVR RNA and protein, they are similar in their susceptibility to poliovirus.

Published
1998
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2. A comparative study of peritoneal mast cells from mutant IL-4 deficient and normal mice: evidence that IL-4 is not essential for mast cell development but enhances secretion via control of IgE binding and passive sensitization

Author

J.W. Coleman and E.M.S. Banks

Subjects
Serotonin, Immunology, Cytoplasmic Granules, Immunoglobulin E, Biochemistry, Mice, chemistry.chemical_compound, medicine, Animals, Immunology and Allergy, Secretion, Mast Cells, Peritoneal Cavity, Molecular Biology, Cells, Cultured, Interleukin 4, Sensitization, Mice, Knockout, biology, Degranulation, Hematology, Flow Cytometry, Mast cell, Cell biology, Mice, Inbred C57BL, Interleukin 33, Kinetics, Microscopy, Electron, medicine.anatomical_structure, chemistry, biology.protein, Interleukin-4, Histamine
Abstract

IL-4 enhances the growth and secretory function of mouse connective tissue type mast cells in vitro. To examine further the mast cell regulatory role of IL-4 we compared certain phenotypic and functional characteristics of peritoneal mast cells from mutant IL-4 deficient (IL-4(-/-)) or normal wildtype (IL-4(+/+)) mice. No differences were seen between mast cells from the two types of mouse in terms of numbers, histamine content, cell size, ultrastructure and number and size of granules. Mast cells from IL-4 deficient or wildtype mice responded equally to specific IgE/antigen and IL-4. However, Fc epsilon RI of IL-4(-/-) (in contrast to wildtype) mast cells were not pre-loaded with IgE, which would be expected to facilitate passive sensitization. Moreover, the in vitro total IgE binding capacity of mutant mast cells was significantly less than that of wildtype. Further in vitro experiments showed that IL-4 selectively enhanced IgE/antigen- rather than anti-IgE-induced degranulation from normal mast cells, and this effect was accompanied by an IL-4 induced increase in IgE binding capacity. In conclusion, IL-4 is not essential for peritoneal mast cell growth and exocytosis but regulates secretion via control of IgE binding and sensitization.

Published
1996
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3. Modified KS, AD, and C-vM tests for the Pareto distribution with unknown location and scale parameters

Author

J.E. Porter, Albert H. Moore, and J.W. Coleman

Subjects
Anderson–Darling test, Pareto principle, Kolmogorov–Smirnov test, Empirical distribution function, Shape parameter, symbols.namesake, Generalized Pareto distribution, Statistics, symbols, Applied mathematics, Pareto distribution, Electrical and Electronic Engineering, Safety, Risk, Reliability and Quality, Pareto analysis, Mathematics
Abstract

Standard goodness-of-fit tests based on the empirical CdF (Edf) require continuous underlying distributions with all parameters specified. Three modified Edf-type tests, the Kolmogorov-Smirnov (K-S), Anderson-Darling (A-D), and Cramer-von Mises (C-vM), are developed for the Pareto distribution with unknown parameters of location and scale and known shape parameter. The unknown parameters are estimated using best linear unbiased estimators. For each test, Monte Carlo techniques are used to generate critical values for sample sizes 5(5)30 and Pareto shape parameters 0.5

Published
1992
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4. Contents, Vol. 99, 1992

Author

U. Darsow, J L Macpherson, Rob C. Aalberse, William W. Busse, Tadamitsu Kishimoto, A. Neszmelyi, Chigusa Terajima, E. Perez, Yuzo Sugihara, Merideth Kelley, Mindy Tsai, C. Brom, M. Lopez, Thomas J. Schall, J. Moscoso, A. Poggi, Ana E. Sousa, M.C. Mingari, Stephan C. Bischoff, M. Morganroth, Y. Mizushima, M. Pretolani, Susetta Finotto, E. Gambassi, Francesco Balsano, Francesca Levi-Schaffer, Lisa Carter, Lennart Enerbäck, F. Sanchez, Bruce S. Bochner, K.F. Austen, Harold E. Dvorak, Matsunobu Suko, L. Lanza, Gianfranco Del Prete, M. Scudeletti, R. Fritsché, Luis M. Botana, J. Hakimi, Roberta Biagiotti, C. Stellato, Ann M. Dvorak, Sachio Endo, Gert Kunkel, V. Segal, Vincenzo Casolaro, C.M. Bachelet, Otto Scheiner, A. Ishii, Alec H. Sehon, Akira Akasawa, T. Miyamoto, Kenji Matsumoto, Thomas Bieber, P.F. Mannaioni, Y. Borel, E. Ciccone, Alistair Noble, Xiao-Jun Chen, J.C. Kips, C. Juarez, Rudolf Valenta, Manel Jordana, S.B. Lehrer, H. Friedrichs, Michael Gräfe, J. Crane, Philip S. Norman, S. Sampognaro, Maria Grazia Giudizi, F. Moreno, Peter Valent, Christoph Heusser, N. Yamashita, José M. Carballido, R.A. Pauwels, A. Moretta, M. Blanca, Marco De Carli, Fatima Ferreira, Christof Ebner, Jochen Niehus, B. Prior, Maria L. Sanz, V. Hess, Claus R. Baumgarten, Peter J. Barnes, H.R. Katz, K.H. Friedrichs, P.A. Ward, Akira Ishii, G. Marone, Werner J. Pichler, Sabina Rak, Allen P. Kaplan, Robert P. Schleimer, Mike Kenemy, G.F. Joos, H. Wagner, Doreen Rucinski, Monique Capron, Bernhard Przybilla, Mamoru lto, Christian Sillaber, Franklin Adkinson, J. Fernandez, Hirokazu Okudaira, Sesha Reddigari, P. Contini, Nicole Carballido-Perrig, Klaus Hermann, Haruhiko Koseki, F. Indiveri, C.J. Corrigan, F. Nambu, Joost J. Oppenheim, Michael Duchêne, Peter T. Peachell, Jane Warner, Shuichi Matsuda, Tohru Ando, A.F. Walls, Koji Ito, Marie-Pierre Piccinni, Yoshimichi Okayama, Fabio Almerigogna, K. Rother, Eckart Fleck, Stephen J. Galli, B. Ross, B.B. Vargaftig, S. Raspanti, Motohiro Ebisawa, Anna Ciccarelli, Yoshihiro Adachi, N.C. Barnes, Satoshi Fukuse, R. Scheper, Amato de Paulis, T. Nakagawa, Toshihiko Obata, J. Grabbe, Enrico Maggi, M.M. Glovsky, L. Mugnai, Ayami Iwasaki, A. Fischer, R. Biassoni, Jerry Dolovich, H. Behrendt, Alfonso Oriente, N. Pearce, Karl-Christian Bergmann, Takeshi Koshino, Barry K. Wershil, Peter F. Weller, D. Baker, A. Stütz, Dean Befus, A.G. Alexander, Susan M. MacDonald, Bruce H. Devens, R. Beasley, W. König, J. Obispo, A. Pistelli, Martin K. Church, Ute Bleise, Teresa M. Litchfield, Robin N. Poston, B.M. Czarnetzki, J. García, Albert Oehling, E. Masini, V. Casolaro, J. Bujanowski-Weber, Krisztina M. Zsebo, Sonja Werner, Y. Yui, Kristof Graf, Margit Tejkl, M.G. Buckley, A.L. de Weck, L.M. Lichtenstein, F. Carswell, Ekkehard Haen, Raffaele Cirillo, Steven A. Krilis, P. Welker, H. Ostmeier, C. Mayorga, Taro Tabana, Jean S. Marshall, Kenichi Tomioka, Jose Fernando Chavarria, M. G. Di Bello, Heinrich Matthys, Tak H. Lee, Shyam S. Mohapatra, Wlodzimierz Ptak, M.R. Holliday, J.H. Tavernier, Kurt Blaser, Giuseppe Spadaro, K. Ito, Gianni Marone, Sandra E. Lavens, Koji Hashimoto, Niroku Koya, W.M. Becker, Andrea Koontz, J.R. Lapa e Silva, G.M. Hänsch, Arnon Nagler, Franco Dammacco, J.G. Meingassner, B. Hitzfeld, M. Castells, A. Genovese, Shu Uno, Jacqueline M. Langdon, Donatella Macchia, Robert G. Hamilton, J. del Prado, Piotr Kuna, W. Dorsch, S Gillis, Nao Kanai, J.W. Coleman, Donald W. MacGlashan, Marco Baggiolini, Tatsuro Koshibu, Elliot C. Dick, Yoji Iikura, Matthew P. Hallsworth, Yasuhiko Makino, Toshikazu Tsubaki, Larry M. Lichtenstein, S. Terrados, Gennaro de Crescenzo, M.J. Torres, Mark A. Giembycz, Mario Ricci, Maria L. Baeza, Angel F. Lopez, Christine De Vos, Go Matsuzaki, F. Gambassi, H. Stuppner, Philip W. Askenase, Angelo Vacca, Ronald Mathison, A. Helbling, Cecilia Soh, C. Burgess, T. Shida, Isao Ohno, F. Puppo, Hirohisa Saito, David R. Webb, Masaru Taniguchi, Clemens A. Dahinden, Joseph S. Davison, Paola Parronchi, Tony Wyss-Coray, Massimo Triggiani, N. Farrow, Dietrich Kraft, M. Motoishi, Susanne Vrtala, A.B. Kay, Michele Columbo, R. Tomingas, William J. Calhoun, L. Moretta, Jonathan P. Arm, Roberto Manetti, Teiichi Matsunaga, J. Brom, Sergio Bonini, J.M. Vega, Susanne Seiberler, David Diaz-Sanchez, I. Wörner, Dontcho Z. Staynov, Judah A. Denburg, Johannes Ring, Sergio Romagnani, M. Lupini, Claus Kroegel, R.A. Peleman, Luciano Adorini, Yuko Katakai, Peter S. Creticos, A. Renda, W.A. Massey, E. Horowitz, Lawrence M. Lichtenstein, Uno Shu, Stefano Bonini, Stephen J. Lane, James Kaiser, Blanca E. García, Reinhold Hirschwehr, M. Tomassini, and Elyse Bissonnette

Subjects
business.industry, Immunology, Immunology and Allergy, Medicine, General Medicine, business
Published
1992
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5. Contents, Vol. 94, 1991

Author

Graham S. LeGros, Hiroshi Yamakawa, K. Takatsu, Ratko Djukanovic, P.G. Holt, J. Bujanowski-Weber, P. Oehme, S. Bianchj, William Roche, I. Knöller, G. Delespesse, Toru Ando, Reinhold Penner, D. Macchia, R. Djukanovic, George W. Ward, Thomas Bieber, T. Furitsu, Makoto Dohi, Susan M. MacDonald, Martin D. Chapman, F. Chavarria, R. Robert Schellenberg, Michiko Haida, Makoto Nogami, John R. Brashler, J. Brom, Pascal Chanez, A. Ciccarelli, T.D. Whalley, M.J. Carmona, E. Saito, Mamoru Ito, H. Behrendt, W. Zachgo, Gabriele Zwadlo-Klarwasser, Philip J. Thompson, Sylvia Miescher, N.P. Siemensma, A. de Paulis, G. Schultze-Werninghaus, J.-P. Kinet, B.D. Gomperts, Takeo Juji, Ikuo Akutsu, Richard J. Simpson, S. Wilson, T.H. Lee, Suhad El-Lati, Bernhard Przybilla, J. Oliver, Sesha Reddigari, Monique Vogel, Koki Takahashi, Thomas Iff, L. Mugnai, E. Neher, Nathalie Paul-Eugène, Ph. Lassalle, Takeshi Fukuda, Dean D. Metcalfe, V. Lagente, C.E. O’Neil, Go Matsuzaki, C. McMenamin, Jordan N. Fink, G. Burow, Ch. Lemmermann, Ch. Schweiger, H. Wagner, K. Kurihara, D.R. Springall, Karin Pettenburger, A. Capron, H.Y.A. Lau, R. Wahl, G.J. Gleich, K. Rother, Shigeru Takafuji, W.R. Roche, Kurt Blaser, F. Gambassi, A. Pistelli, M. Bubak, Andrew F. Walls, Jeffrey M. Drazen, S.J. Lane, Johann-Christian Virchow, Akio Mori, J.M. Polak, Dietrich Kraft, Hans L. Spiegelberg, L. Lipponer, Friederike von zur Mühlen, R. zur Strassen, Rihoux Jean-Pierre, Susanne Spitzauer, Werner J. Pichler, Karen Britten, M. Schon-Hegrad, Barbara K. Stout, John Wilson, Hirokazu Okudaira, Otto Scheiner, Mitsuko Kondo, Akira Ishii, Richard Sporik, Daniel Weinreich, M. Keating, W. Dorsch, Manel Jordana, Ch.H. Heusser, Ingrid Enander, Massimo Triggiani, T. Ishizaka, Colin J. Sanderson, Dieter Vieluf, Stephanie A. Shore, J. Anrather, S. Terrados, Claus Bachert, Rosa M. Ten, E.W. Rauterberg, E. Masini, H. Rumpold, Jean Yves Lacoste, T.H.W. Lillie, K. Ohno, Alison M. Campbell, E. Gutierrez, F.L. Pearce, Stephan C. Bischoff, R. Suau, Miguel Blanca, P.H. Howarth, P.K. Jeffery, Robert L. Barker, E. Perez, M. Pfenning, Marshall Plaut, Piotr Kuna, T. Abe, H. Rotermund, Michael A. Lett-Brown, Herbert G. Johnson, Thomas Brunner, C. Ra, U. Ganzer, N. Hyslop, Kazuhiko Akiyoshi, Alain L. de Weck, J. Bews, A. Hartnell, J. Dry, K. Nosbüsch, Rafeul Alam, G. Le Gros, V. Brinkmann, Jacqueline M. Langdon, B. Thomas, P. Heap, Corinne Petit-Frère, A.G. Fernández, Wolfgang Schmutzler, Gianni Marone, Matsunobu Suko, R.W. Gristwood, D. Kraft, G.M. Walsh, A.G. Palma-Carlos, B. Bradley, N.S. Sakaguchi, J.M. Vega, O.-H. Wilhelms, R. Wiewrodt, A. Brini, Stephen R. Durham, M. Lupini, M.A. Reed, Thierry Maisonnet, A. Witzel, Peter J. Barnes, Ch. Brander, Lawrence M. Lichtenstein, A. Koffer, Y. Delneste, Laura Palma-Carlos, Jennifer Cairns, T. Brunnee, Elliott Homer, Diana J. Quint, F. Bettens, Monique Capron, Sohei Makino, Luanda Beck, T. Imai, Takayuki Ohtoshi, A. Akasawa, Lore Koller, Yoji Iikura, Naohiro Watanabe, Ahuva Nissim, J.W. Coleman, A. Ohgimi, D. Befus, J.R. Wilkinson, H. Küster, T. Katsunuma, Ch. Ebner, K.J. Turner, M.P. Piccinni, F. Ledermann, Michael Breitenbach, Bradley J. Undem, A.B. Kay, John E. Salvaggio, Carvalho de Sousa, S.T. Holgate, B. Girn, P. Berga, S. Bent, Gerald J. Gleich, Arnold S. Kirshenbaum, P.B. Boulos, Yoshitaka Ino, M. Breitenbach, R. Rathsack, May Azzawi, Sun Ying, Philippe Godard, J.H. Widdicombe, Rudolf Valenta, Christopher Corrigan, S. Romagnani, D.M. Kemeny, Bernard Dugas, Samuel B. Lehrer, Y. Churcher, John Gordon, C. Brom, F. Leynadier, Gert Kunkel, Gerard Cox, B.F. Weber, D. Diaz-Sanchez, Shinji Motojima, J.W. Wilson, Pieter L.B. Bruijnzeel, P.F. Mannaioni, K. Britten, Allen P. Kaplan, Yutaka Morita, K. Ishida, Erika Jensen-Jarolim, Jack Gauldie, Fiona R. Lake, S. Raspanti, Andrew Grant, R. Fadel, S. Dunnette, Jean Bousquet, Ivan Aebischer, Thomas A.E. Platts-Mills, T. Wyss, Richard D. O’Connor, Larry D. Ward, A.G. Morris, Clemens A. Dahinden, Toshifumi Yuuki, P. Parronchi, Hiroyuki Mochizuki, Gail M. McNutt, D.C. Reason, Martin Krieger, Lawrence E. Gelber, Naoki Inagaki, E. Kilchherr, Elisabeth Boichot, Qiu Gang, F. Gabl, Alec H. Sehon, J.V. Collins, Shiro Kasuya, J. Blomgren, Bernadette Pignol, Motohiro Ebisawa, N. Sakaguchi, Jacalyn H. Pierce, U. Blank, Fu-Tong Liu, Robert A. Seder, R. Hilger, Richard P. Bransford, M. Linssen, Jörg Kleine-Tebbe, P.D. Pare, Kazuhiko Yamamoto, Jean Michel Mencia-Huerta, Michael K. Bach, Pierre Braquet, J. Salvaggio, Reuben J.M. Falkoff, R. Merget, J. Hards, B.J. Holt, D. Strickland, P.E.R. Tatham, A.B. Tonnel, H. Saito, François-B. Michel, K. Akimoto, Jerry Dolovich, Brian M. Greenlee, Carl G. A. Persson, Anne Kagey-Sobotka, Tim R. Mosmann, Zelig Eshhar, N. Wallen, Maria Baeza, A.J. Wardlaw, Peter H. Howarth, Robin N. Poston, W. König, R.C. Benyon, M. Lopez, D. Mijic, E. Jarolim, William E. Paul, John P. Caulfield, B. Kunz, Milton A. Martins, Yasushi Okumura, J. Knöller, R. Ciriilo, K. Nieber, Geoffrey A. Stewart, Allen C. Myers, Zami Ben-Sasson, U. Hauser, M. G. Di Bello, Michael Duchêne, C. Baumgarten, C.J. Sanderson, Koji Ito, R. Valenta, M.-H. Jouvin, Menachem Rottem, F. Carswell, A. Miranda, K.R. Tainsh, Kimm J. Hamann, Judah A. Denburg, K. Wagner, Martin K. Church, Qutayba Hamid, O. Mejan, Johannes Ring, J. Fernandez, L. Juhlin, Kiyoshi Takatsu, Martin E. Sanders, Peter W. Heymann, C.E. Reed, P. Wentz-Murtha, Fred D. Finkelman, J. Llupiá, Helmut Rumpold, Stephen T. Holgate, Conceição B. Santos, G.M. Hänsch, W.L. Liu, Christoph Walker, M. Ricci, Ph. Gosset, E. Maggi, J. Wilson, R. Moqbel, and Beda M. Stadler

Subjects
business.industry, Immunology, Immunology and Allergy, Medicine, General Medicine, business
Published
1991
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6. Contributors

Author

S.N. Abraham, L. Aloe, L. Annunziato, S. Arbilla, E. Arbustini, G.C. Baccari, P.J. Barbosa Pereira, C. Beltrame, J. Bienenstock, S.C. Bischoff, N. V-Blank, U. Blank, S. Bonini, J. Brown, P. Bruhns, C. Calabrese, P. Castaldo, M.K. Church, J.W. Coleman, W. R Coward, M. Daëron, C.A. Dahinden, F. Dal Piaz, J.E. Damen, G. De Crescenzo, A. De Paulis, H. Depoortere, A. De Santis, A.M. Dvorak, M.L. Entman, G. Florio, V. Forte, N.G. Frangogiannis, W.H. Fridman, S.J. Galli, E.W. Gelfand, A. Genovese, M. Gentile, G. Giorgio, J. Goldhill, F. Granata, J.-C. Gutierrez-Ramos, K. Hartmann, C.D. Helgason, B.M. Henz, B. Hermes, K. Hirai, S. Hirota, C.M. Hogaboam, S.T. Holgate, M. Huber, M. Hughes, Humphries R. K, M. Iikura, H.H. Jacobi, O. Johansson, G.L. Johnson, R. Kajekar, Y. Kitamura, P.A. Knight, P.T. Kovanen, S.A. Krilis, G. Krystal, C.S. Lantz, S. Lavens-Phillips, L. Li, H. Liénard, T.-J. Lin, N.W. Lukacs, D. Macglashan Jr, R. Malaviya, O. Malbec, G. Marone, J.S. Marshall, D.D. Metcalfe, A. Micera, H.R.P. Miller, G. Minopoli, S. Minucci, K. Miura, M. Miyamasu, E. Morii, A.C. Myers, T. Nishida, S.H. P. Oliveira, A. Oriente, C. Palumbo, A. Pannaccione, V. Patella, P.H. Pichat, R. Polosa, C. Pothoulakis, P. Pucci, E.J. Quackenbush, S.W. Reddel, P. Romagnani, S. Romagnani, T. Russo, A.M. Sanico, N.M. Schechter, N. Selve, G. Spadaro, R.L. Stevens, S. Strobl, M. Taglialatela, E.M. Thornton, A. Togias, M. Triggiani, M. Tsai, B.J. Undem, P. Valent, L. Verga, A.F. Walls, M. Ware, P. Welker, B.K. Wershil, S.H. Wright, M. Yamaguchi, and F.-G. Zhu

Published
2000
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7. Cell mobilisation and cytokine gene expression in a rat model of non-antigen-induced lung inflammation

Author

C.M.M. Williams and J.W. Coleman

Subjects
Male, Neutrophils, Immunology, Rat model, Cell, Inflammation, Antigen, Cell Movement, Interleukin 25, medicine, Immunology and Allergy, Animals, Cytokine genes, RNA, Messenger, Rats, Wistar, Lung, business.industry, General Medicine, Pneumonia, Rats, Eosinophils, medicine.anatomical_structure, Cytokines, medicine.symptom, business
Published
1997

8. Identification of a spleen cell-derived factor that inhibits sensitization of murine peritoneal mast cells as interferon-gamma

Author

J.W. Coleman and A.G. Morris

Subjects
medicine.medical_treatment, Immunology, Spleen, In Vitro Techniques, Interferon-gamma, Mice, medicine, Splenocyte, Immunology and Allergy, Animals, Interferon gamma, Mast Cells, Peritoneal Cavity, Sensitization, biology, business.industry, General Medicine, Mast cell, Cytokine, medicine.anatomical_structure, Monoclonal, biology.protein, Antibody, business, medicine.drug
Abstract

We present evidence that a spleen cell-derived factor that inhibits the sensitization of mouse peritoneal mast cells is IFN gamma. Conditioned medium (CM) from Con A-activated mouse spleen cells and recombinant MuIFN gamma both inhibited antigen-induced 5-HT release from peritoneal mast cells when added at the sensitization stage, but were without effect on presensitized cells. Both preparations were active at dilutions corresponding to similar levels of IFN activity (1-10 units/ml). The inhibitory activity of CM was blocked by a rat monoclonal MuIFN gamma-neutralizing antibody, thus confirming that IFN gamma was the active molecule.

Published
1991

9. A comparison of the effects of chlorpromazine and more selective histamine and 5-hydroxytryptamine antagonists on human IgG synthesis in vitro

Author

J.W. Coleman and Francisca Martinez

Subjects
Serotonin, Chlorpromazine, medicine.medical_treatment, Immunology, Mepyramine, Methysergide, Histamine Antagonists, Pharmacology, H2 antagonist, chemistry.chemical_compound, medicine, Humans, Histamine H4 receptor, Cimetidine, Cells, Cultured, business.industry, Mechanism of action, chemistry, Immunoglobulin G, Receptors, Serotonin, Leukocytes, Mononuclear, Receptors, Histamine, Serotonin Antagonists, medicine.symptom, business, Histamine, medicine.drug
Abstract

We have shown previously that chlorpromazine, a drug associated with immunological abnormalities in vivo, significantly potentiates pokeweed mitogen (PWM)-stimulated IgG synthesis by human peripheral blood mononuclear cells (PBMC) in culture. Chlorpromazine is a pharmacological antagonist of histamine and 5-hydroxytryptamine (5-HT) and thus may exert its immune-enhancing effects by competing with these amines for their respective receptors, which are known to be present on lymphocytes. In this report we show that histamine and 5-HT are present at micromolar concentrations in PBMC cultures. To examine the role of histamine and 5-HT in chlorpromazine-induced enhancement of IgG synthesis we incubated PWM-treated cells with a range of selective histamine and 5-HT antagonists, and with the amines added to cultures either alone or in combination with chlorpromazine. The H1 antagonists mepyramine and promethazine and the H2 antagonist cimetidine had no significant effect on IgG synthesis. The combined 5-HT1/5-HT2 antagonists methysergide and methiothepin also failed to modulate synthesis. Neither histamine nor 5-HT at concentrations up to 100 microM modulated IgG synthesis, nor did they abrogate the enhancement of IgG synthesis induced by chlorpromazine. We conclude that the modulation of IgG synthesis in vitro by chlorpromazine cannot be attributed to an interaction of this drug with lymphocyte receptors for histamine and 5-HT. Other possibilities for the mechanism of action of this drug on immune function are discussed.

Published
1990

10. Inhibitors of Protein and RNA Synthesis Block the Sensitization of Murine Peritoneal Mast Cells

Author

J.W. Coleman

Subjects
Serotonin, Protein synthesis inhibitor, Ratón, Immunology, General Medicine, Immunoglobulin E, Cycloheximide, Biology, Mast cell, Mice, chemistry.chemical_compound, medicine.anatomical_structure, chemistry, Peritoneum, Protein Biosynthesis, Dactinomycin, medicine, Protein biosynthesis, Animals, RNA, Immunology and Allergy, Mast Cells, Sensitization
Abstract

Addition of the protein synthesis inhibitor cycloheximide (CX, 1 μg/ml) and the RNA synthesis inhibitor actinomycin D (AD, 0.1 μg/ml) to unfractionated mouse peritoneal mast cells simultaneously with IgE anti-DNP, for 24 h prior to challenge, completely blocked antigen-induced 5-HT release. Responses to anti-IgE were strongly abrogated whereas responses to the calcium ionophore A23187 were not affected. When CX and AD were added to presensitized cells their effects on antigen and anti-IgE-induced release were much reduced. These results suggest a requirement for protein synthesis during mast cell sensitization.

Published
1991
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11. Biographical Sketch of Dr. Alec H. Sehon

Author

Matsunobu Suko, R.W. Gristwood, A.G. Palma-Carlos, T.H.W. Lillie, K. Ohno, R. Wiewrodt, K. Nosbüsch, Jacqueline M. Langdon, A. Brini, Zelig Eshhar, E. Kilchherr, V. Lagente, C.E. O’Neil, T. Katsunuma, Jean Michel Mencia-Huerta, M. Lopez, Michael K. Bach, D. Mijic, E. Jarolim, F.L. Pearce, E. Perez, Beda M. Stadler, Pierre Braquet, E. Saito, Mamoru Ito, H. Behrendt, N. Wallen, Maria Baeza, A.J. Wardlaw, Ch. Lemmermann, Ch. Schweiger, Bernadette Pignol, A. de Paulis, J. Salvaggio, Reuben J.M. Falkoff, J. Hards, William E. Paul, B.J. Holt, P. Berga, R. Djukanovic, Philip J. Thompson, Sylvia Miescher, N.P. Siemensma, Graham S. LeGros, Hiroshi Yamakawa, Yoshitaka Ino, M. Breitenbach, D. Strickland, K. Wagner, Martin K. Church, B. Bradley, Gert Kunkel, Gerard Cox, John P. Caulfield, Milton A. Martins, Yasushi Okumura, Daniel Weinreich, C.E. Reed, M.A. Reed, Thierry Maisonnet, Sesha Reddigari, Monique Vogel, Philippe Godard, J.H. Widdicombe, Robert A. Seder, F. Gabl, Christopher Corrigan, S. Romagnani, J.V. Collins, Jacalyn H. Pierce, O. Mejan, J. Fernandez, Fred D. Finkelman, J. Llupiá, O.-H. Wilhelms, H. Saito, François-B. Michel, A. Witzel, Jean Bousquet, Ivan Aebischer, Lawrence E. Gelber, Naoki Inagaki, Fu-Tong Liu, Thomas A.E. Platts-Mills, T. Wyss, D.M. Kemeny, Elisabeth Boichot, T. Imai, Y. Delneste, Ch. Brander, Stephanie A. Shore, John R. Brashler, Wolfgang Schmutzler, Richard P. Bransford, Fiona R. Lake, Ingrid Enander, W. Zachgo, Gabriele Zwadlo-Klarwasser, S. Terrados, Jennifer Cairns, Rosa M. Ten, R.C. Benyon, J.W. Coleman, Bernard Dugas, Samuel B. Lehrer, Y. Churcher, Shiro Kasuya, Takayuki Ohtoshi, G. Le Gros, D. Diaz-Sanchez, A.B. Tonnel, J. Brom, Pascal Chanez, J. Blomgren, John Gordon, P. Heap, M. Linssen, Jörg Kleine-Tebbe, Manel Jordana, Ch.H. Heusser, K. Akimoto, Jerry Dolovich, T. Ishizaka, Ratko Djukanovic, I. Knöller, Thomas Bieber, Peter H. Howarth, Helmut Rumpold, H. Rumpold, Motohiro Ebisawa, Jean Yves Lacoste, Gianni Marone, P.G. Holt, Pieter L.B. Bruijnzeel, Massimo Triggiani, Karen Britten, D.C. Reason, N. Sakaguchi, N.S. Sakaguchi, Ikuo Akutsu, G. Schultze-Werninghaus, R. Valenta, U. Blank, J.M. Vega, F. Leynadier, C. Ra, Bernhard Przybilla, K. Takatsu, Robin N. Poston, Larry D. Ward, P.K. Jeffery, Stephen R. Durham, J. Bujanowski-Weber, Nathalie Paul-Eugène, J. Dry, E.W. Rauterberg, B. Kunz, Christoph Walker, Richard J. Simpson, S. Wilson, V. Brinkmann, Ph. Lassalle, G. Burow, P.D. Pare, P. Oehme, Rafeul Alam, J. Knöller, R. Ciriilo, Conceição B. Santos, W. König, S. Bianchj, Allen C. Myers, K.R. Tainsh, Thomas Iff, E. Maggi, A. Miranda, T.D. Whalley, William Roche, Kimm J. Hamann, Lawrence M. Lichtenstein, Herbert G. Johnson, Kazuhiko Akiyoshi, Allen P. Kaplan, G. Delespesse, M.J. Carmona, H.Y.A. Lau, Kazuhiko Yamamoto, C. McMenamin, J. Wilson, Peter J. Barnes, Laura Palma-Carlos, A. Akasawa, G.M. Walsh, A. Capron, Toru Ando, W.R. Roche, Qiu Gang, Andrew F. Walls, Monique Capron, Sohei Makino, M. Lupini, Luanda Beck, J. Oliver, C. Baumgarten, L. Mugnai, C.J. Sanderson, Naohiro Watanabe, L. Lipponer, Alec H. Sehon, T. Furitsu, A. Ohgimi, Makoto Dohi, T. Brunnee, Elliott Homer, Diana J. Quint, A. Koffer, Friederike von zur Mühlen, R. Moqbel, Bradley J. Undem, Barbara K. Stout, Arnold S. Kirshenbaum, P.B. Boulos, Judah A. Denburg, M.-H. Jouvin, Werner J. Pichler, Shigeru Takafuji, M. Schon-Hegrad, Michael Breitenbach, G.M. Hänsch, Johannes Ring, J. Anrather, Robert L. Barker, Reinhold Penner, Otto Scheiner, L. Juhlin, Johann-Christian Virchow, Hirokazu Okudaira, E. Masini, S. Dunnette, Gerald J. Gleich, E. Gutierrez, Marshall Plaut, K. Nieber, F. Carswell, Piotr Kuna, R. Hilger, H. Küster, Clemens A. Dahinden, D. Macchia, W.L. Liu, M.P. Piccinni, Colin J. Sanderson, F. Gambassi, Jeffrey M. Drazen, Geoffrey A. Stewart, R. Wahl, G.J. Gleich, R. zur Strassen, R. Merget, M. Ricci, Menachem Rottem, John E. Salvaggio, Qutayba Hamid, Go Matsuzaki, Peter W. Heymann, Martin D. Chapman, P.E.R. Tatham, F. Chavarria, P. Wentz-Murtha, H. Wagner, S.J. Lane, Ph. Gosset, Akio Mori, K. Rother, Dietrich Kraft, Hans L. Spiegelberg, Kurt Blaser, A. Pistelli, Koki Takahashi, Kiyoshi Takatsu, D. Kraft, Martin E. Sanders, R. Suau, Stephen T. Holgate, T. Abe, Thomas Brunner, John Wilson, N. Hyslop, Alain L. de Weck, A. Hartnell, Corinne Petit-Frère, Zami Ben-Sasson, F. Bettens, Lore Koller, Yoji Iikura, U. Hauser, May Azzawi, Yutaka Morita, K. Ishida, M. G. Di Bello, Michael Duchêne, Koji Ito, Martin Krieger, D.R. Springall, Karin Pettenburger, J.M. Polak, Ahuva Nissim, Susanne Spitzauer, D. Befus, J.R. Wilkinson, Ch. Ebner, K.J. Turner, M. Bubak, F. Ledermann, Akira Ishii, Richard Sporik, M. Keating, A.B. Kay, Carvalho de Sousa, S.T. Holgate, B. Girn, S. Bent, Dieter Vieluf, Rihoux Jean-Pierre, W. Dorsch, Mitsuko Kondo, Claus Bachert, T.H. Lee, Suhad El-Lati, George W. Ward, E. Neher, R. Robert Schellenberg, Michiko Haida, Makoto Nogami, Brian M. Greenlee, Carl G. A. Persson, Anne Kagey-Sobotka, M. Pfenning, Dean D. Metcalfe, B.F. Weber, H. Rotermund, Shinji Motojima, J.W. Wilson, Tim R. Mosmann, Michael A. Lett-Brown, K. Kurihara, P.F. Mannaioni, Erika Jensen-Jarolim, Jack Gauldie, S. Raspanti, Andrew Grant, U. Ganzer, R. Fadel, R. Rathsack, Susan M. MacDonald, Toshifumi Yuuki, Sun Ying, B. Thomas, Rudolf Valenta, P. Parronchi, A. Ciccarelli, J.-P. Kinet, B.D. Gomperts, Takeo Juji, C. Brom, Hiroyuki Mochizuki, Gail M. McNutt, Alison M. Campbell, Takeshi Fukuda, K. Britten, Jordan N. Fink, J. Bews, Richard D. O’Connor, Stephan C. Bischoff, Miguel Blanca, P.H. Howarth, A.G. Morris, and A.G. Fernández

Subjects
Gerontology, media_common.quotation_subject, Immunology, Immunology and Allergy, Art history, General Medicine, Art, Biographical sketch, media_common
Published
1991
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12. Enzyme-linked immunosorbent assay (ELISA) for detection of antibodies to protein-reactive drugs and metabolites: criteria for identification of antibody activity

Author

J.H.K. Yeung, Malcolm D. Tingle, B.K. Park, and J.W. Coleman

Subjects
chemistry.chemical_classification, biology, Metabolite, Immunology, chemical and pharmacologic phenomena, Sulfanilamide, Molecular biology, Epitope, chemistry.chemical_compound, Enzyme, chemistry, Biochemistry, medicine, biology.protein, Immunology and Allergy, Dinitrophenyl, Antibody, Hapten, Conjugate, medicine.drug
Abstract

Certain hypersensitivity reactions to drugs are thought to depend on coupling of reactive species (the drug itself or a metabolite) to macromolecules, leading to the formation of hapten-carrier conjugates. In assays for the detection of antibodies directed against such reactive species the drug or metabolite must be used in conjugated rather than free form. We describe ELISAs for the detection of anti-dinitrophenyl (DNP), anti-captopril (CP) and anti-sulphanilamidobenzoic acid (SABA) antibodies, in which the wells of microtitre plates are coated with hapten conjugated to protein. We define coating conditions and the following 3 criteria for identification of anti-hapten activity: Immunoglobulin in the test sample binds to the immobilised hapten-protein conjugate, but not to the immobilised protein alone. Binding is inhibited by preincubation of the test sample with protein conjugates incorporating the test hapten, but not by preincubation with the same unconjugated proteins, nor protein conjugates incorporating haptenic groups unrelated to the test hapten. The inhibitory hapten-protein conjugates are shown to be inactive in unrelated antigen-antibody interactions. Binding is blocked by preincubation of the test sample with low molecular weight chemical derivatives of the reactive hapten. The inhibitory derivatives must be shown to be inactive in unrelated antigen-antibody interactions. On the basis of these criteria, IgG anti-DNP and IgG anti-CP were detected in the sera of immunized rabbits. The IgG anti-DNP antibody recognised protein-conjugated DNP, DNP-lysine, N-acetyl-DNP-lysine and DNP-S-glutathione, whereas the IgG anti-CP antibody recognised CP-S-S-protein and CP-S-S-CP. By the same criteria IgG anti-SABA was detected in the sera of immunized mice. The antibody recognised free and protein-conjugated SABA, but not free sulphanilamide.

Published
1986
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13. Neuraminidase- and benzalkonium chloride-dependent inhibition of basic peptide-induced rat mast cell secretion

Author

J.W. Coleman

Subjects
Serotonin, Immunology, Cell, Neuraminidase, Peptide, Biology, chemistry.chemical_compound, Benzalkonium chloride, medicine, Animals, Immunology and Allergy, Polylysine, Secretion, Mast Cells, chemistry.chemical_classification, Hydrogen-Ion Concentration, Immunoglobulin E, Mast cell, Rats, Sialic acid, medicine.anatomical_structure, Biochemistry, chemistry, Sialic Acids, biology.protein, Cosyntropin, Benzalkonium Compounds, Peptides, medicine.drug
Abstract

Two types of inhibition of basic peptide-induced rat mast cell secretion are reported. Pretreatment of rat peritoneal mast cells with Vibrio comma neuraminidase, an enzyme which cleaves sialic acid from oligosaccharides, led to inhibition of 5-hydroxytryptamine release induced by the basic peptides polylysine, corticotropin1–24 and a decapeptide sequence of human IgE. Inhibition was similarly observed when mast cells were challenged in the presence of the cationic cell membrane-active substance benzalkonium chloride. It is postulated that both of these experimental procedures inhibit basic peptide-induced secretion by depletion of cell surface negative charge. Sialic acid itself does not act as a specific receptor for basic peptides, since a molar excess of sialic acid in free solution failed to inhibit secretion by binding to basic peptides in the fluid phase.

Published
1982
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14. The mast cell response to substance P: Effects of neuraminidase, limulin, and some novel synthetic peptide antagonists

Author

Q. Huang, J.W. Coleman, and D.R. Stanworth

Subjects
Serotonin, Physiology, Neuraminidase, Peptide, Substance P, In Vitro Techniques, Pharmacology, Peptide hormone, Biochemistry, Structure-Activity Relationship, Cellular and Molecular Neuroscience, chemistry.chemical_compound, Endocrinology, Lectins, medicine, Animals, Secretion, Mast Cells, chemistry.chemical_classification, biology, Rats, Inbred Strains, Mast cell, In vitro, Rats, C-Reactive Protein, medicine.anatomical_structure, chemistry, Mechanism of action, biology.protein, medicine.symptom
Abstract

We have investigated certain aspects of the mechanism whereby substance P triggers secretion of 5-hydroxytryptamine (5-HT) from rat peritoneal mast cells in vitro . Substance P-induced release of 5-HT was inhibited following pretreatment of rat peritoneal cells with 0.01–1.0 units/ml neuraminidase; secretion induced by anti-IgE antibody was inhibited by pretreatment with 1.0 units/ml but not by lower concentrations of enzyme. Addition of the sialic acid-rich substances N-acetyl-neuraminlactose (up to 1.0 mM) and mucin (up to 1.0 mg/ml) to substance P in free solution failed to block the activity of the neuropeptide. Limulin, a sialic acid-specific lectin, failed to block substance P-induced secretion of 5-HT, but was found to possess intrinsic non-lytic secretory activity (at 5–20 μg/ml). Release of 5-HT induced by limulin was independent of that induced by substance P. A range of octapeptides incorporating the C-terminal sequence Gly-Ser-Phe-Phe, but differing in degree of cationicity and positioning of cationic residues in the four N-terminal positions, were tested for their capacity to antagonise the mast cell-triggering activity of substance P. A peptide incorporating two lysine residues at the N-terminus was found to have partial substance P antagonist activity; no effects on IgE-mediated secretion were observed.

Published
1986
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15. Contents, Vol. 66, 1981

Author

Pam Drysdale, Jerzy Wasserman, Lucy A. Gallinger, Kazuo Ohuchi, Anne-Marie Ros, Masamichi Ishiguro, B. Huitfeldt, Nils Thyresson, Satoko Kiso, Patrick G. Holt, M.G. Baines, S. Leivers, Atsushi Kurihara, T. F. Huff, N.R. Ling, B. Skoogh, E.C. Olson, Susumu Tsurufuji, B.S. Wostmann, R.C. Godfrey, J.W. Coleman, Robbert Benner, Lars-Victor von Stedingk, Teruko Ishizaka, J J Haaijman, P. Rubin, T. Månsson, Shin Yoshino, Roger Henriksson, W. Hijmans, Shao-Qiu Gu, H. Ginsburg, A. Van Oudenaren, Corey Weiner, Te Piao King, Hiromitsu Yoshimura, S. Ahlstedt, Hirokazu Okudaira, J. Sjövall, J Slingerland-Teunissen, F. Maesen, Per E. Alm, Gunnar D. Bloom, H.F. Pross, and Janet E. Batty

Subjects
business.industry, Immunology, Immunology and Allergy, Medicine, General Medicine, business
Published
1981
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16. Inhibition of Human Lung Mast Cell Sensitization by IgE in Allergic Sera

Author

J.W. Coleman and R.C. Godfrey

Subjects
Immunosuppression Therapy, biology, business.industry, Immunology, General Medicine, Immunoglobulin E, Mast cell, Binding, Competitive, Histamine Release, Human lung, Myeloma Proteins, medicine.anatomical_structure, Antibody Specificity, Passive sensitization, medicine, biology.protein, Humans, Immunology and Allergy, Binding Sites, Antibody, Mast Cells, business, Lung, Sensitization
Abstract

Passive sensitization of mast cells in human lung tissue by antigen-specific IgE was inhibited by allergic sera containing IgE of other specificities. IgE-free sera and heat-treated sera failed to inhibit. Inhibition by purified myeloma IgE was quantitatively similar to that produced by serum IgE. It is concluded that IgE antibodies of different antigen specificity at concentrations found in allergic sera compete for cell surface receptors on human mast cells.

Published
1981
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17. Biological variation in the immunological release of histamine from replicates of passively sensitized human lung and its relation to histamine content

Author

J.W. Coleman

Subjects
Hypersensitivity, Immediate, medicine.medical_specialty, Immunology, Immunoglobulin E, Histamine Release, Human lung, chemistry.chemical_compound, Antigen, Internal medicine, Biological variation, medicine, Immunology and Allergy, Humans, Lung, biology, General Medicine, Allergens, Endocrinology, medicine.anatomical_structure, chemistry, Passive sensitization, biology.protein, Immunity, Maternally-Acquired, Histamine
Abstract

The histamine content of weighed replicates of chopped human lung was found to vary greatly. Replicates also varied considerably in the amount of histamine released after passive sensitization with IgE and challenge with antigen. The amount of immunological release of histamine was poorly related to tissue histamine content. Consequently, expression of release as percent of content did not lead to any decrease in the amount of variation between replicates.

Published
1980

18. Essential structural requirements for triggering of mast cells by a synthetic peptide comprising a sequence in the C epsilon 4 domain of human IgE

Author

Zahida Khan, D.R. Stanworth, and J.W. Coleman

Subjects
Serotonin, Protein Conformation, Immunology, Lysine, Dose-Response Relationship, Immunologic, Peptide, Phenylalanine, Serine, Structure-Activity Relationship, Animals, Humans, Mast Cells, Molecular Biology, Cells, Cultured, chemistry.chemical_classification, Alanine, L-Lactate Dehydrogenase, Chemistry, Protein primary structure, Rats, Inbred Strains, Immunoglobulin E, Peptide Fragments, Amino acid, Rats, Biochemistry, Acetylation, Immunoglobulin epsilon-Chains, Immunoglobulin Heavy Chains
Abstract

A range of synthetic analogues of the peptides Lys-Thr-Lys-Gly-Ser-Gly-Phe-Phe-Val-PheNH 2 (human IgE e-chain 497–506 decapeptide) and Lys-Thr-Lys-Gly-Ser-Gly-Phe-PheNH 2 (e-chain 497–504 octapeptide) were tested for activity as releasers of 5-hydroxytryptamine from rat peritoneal mast cells. The following structural modifications were found to abrogate activity: N -acetylation of the α-amino group of the N -terminal lysine residue; substitution of the two lysine residues by either serine or glutamine; depletion of the two C -terminal hydrophobic residues (Val-Phe) of the decapeptide; and substitution of phenylalanine by alanine in the C -terminal position of the octapeptide. These observations point to a requirement for positively charged amino acids and hydrophobic amino acids at the N - and C -terminus respectively for triggering of mast cells by these short-chain peptides. Releasing activity was also found to depend on the stereospecific conformation of the positively charged region, since substitution of l -isomeric amino acids by d -isomeric forms in the three N -terminal positions of the decapeptide led to loss of potency. Inactive analogues of the decapeptide and octapeptide, at concns up to 10 −4 M , failed to antagonise the mediator-releasing effects of the active decapeptide at concns of 3 × 10 −6 — 10 −4 M .

Published
1984

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