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153. Immunosuppressive actions of 1,25-dihydroxyvitamin D3: preferential inhibition of Th1 functions

Author

Lemire, Jacques M., Archer, D. Clay, Beck, Lucinda, and Spiegelberg, Hans L.

Subjects
Vitamin D -- Physiological aspects, T cells -- Research, Immunosuppression -- Research, Food/cooking/nutrition
Abstract

1,25-Dihydroxyvitamin [D.sub.3] [1,25-[(OH).sub.2]-[D.sub.3]] is known to be an immunosuppressive hormone. This review primarily deals with in vitro and in vivo effects of 1,25-[(OH).sub.2]-[D.sub.3] and analogue, 1,25-dihydroxy-16ene-vitamin [D.sub.3] [l,25-[(OH).sub.2]-16ene-[D.sub.3]], on T helper subsets type 1 ([Th.sub.1]) or type 2 ([Th.sub.2]) that have distinctive functional characteristics in humans. [Th.sub.1] secrete interferon (IFN-[Gamma]), interleukin (IL-2) and induce B cells to produce immunoglobulin Ig[G.sub.2a] while [Th.sub.2] secrete IL-4, IL-10 and induce the production of Ig[G.sub.1] and IgE by B cells. The sterol inhibits the secretion of IL-12, a cytokine produced by monocytes and B cells, which leads to the activation and differentiation of [Th.sub.1]. In addition, 1,25-[(OH).sub.2]-[D.sub.3] directly inhibits IFN-[Gamma] secretion by [Th.sub.1] clones while it has little effect on IL-4 secretion by [Th.sub.2] clones. The analogue, 1,25-[(OH).sub.2]-16ene-[D.sub.3], is 100-fold more potent than 1,25-[(OH).sub.2]-[D.sub.3] in inhibiting IFN-[Gamma] secretion but also has little effect on IL-4 secretion. In mice, when given in vivo, the sterol prevents the induction of spontaneous and induced autoimmune diseases and inhibits [Th.sub.1] induce Ig[G.sub.2a] responses. These actions of the vitamin [D.sub.3] compounds suggest that it may have potential therapeutic applications in [Th.sub.1]-mediated clinical situations such as autoimmunity and transplantation. INDEXING KEY WORDS: 1,25-dihydroxyvitamin [D.sub.3]; T helper cell subset Type 1; interleukin-12; encephalomyelitis; lupus

Published
1995

155. Abstracts

Author

Korzeniewski, P., Lang, S. A., Grant, R., Loader, C., Vaghadia, H., Wong, D., Waters, T., Merrick, P., Ali, M. J., Dobkowski, W., Cornelius, T., Hawkins, R., Varkey, G. P., Claffey, Liam, Plourde, Gilles, Trahan, Michel, Morris, Joan, Dean, Deanne M., Yamaguchi, Hiroshi, Harukuni, Izumi, Naito, Hiroshi, Chan, V. W. S., Mati, N., Seyone, C., Evans, D., Chung, F., Joffe, D., Plourde, G., Villemurc, C., Hong, M., Milne, B., Loomis, C., Jhamandas, K., Priddy, R., Archer, D., Tang, T., Sabourin, M., Samanini, N., Cuillerier, D. J., Schuben, Armin, Awad, Issam A., Perez-Trepichio, Alejandro D., Ebrahim, Zeyd Y., Bloomfield, Eric L., Zexu, Fang, Zhengnua, Gu, Qing, Zou, Balhua, Sung, Miller, D. R., Martineau, R. J., Wynands, J. E., Hill, J. D., Knill, R. L., Skinner, M. I., Novick, T. V., McLean, R. F., Kolton, M., Noble, W. H., Sullivan, P. J., Cheng, D. C. H., Chapman, K. R., Ong, D., Roraanelli, J., Smallman, Bettina, Nathan, Howard J., Murphy, J. T., Hall, R. I., Moffitt, E. A., Hudson, R. J., Pascoe, E. A., Anderson, B. A., Thomson, I. R., Kassum, D. A., Shanks, A., Rosenbloom, M., Sidi, A., Gehrig, T. R., Fool, J. M., Rush, W., Martin, A. J., Cooper, P. D., Maltby, J. R., Johnson, D., Hurst, T., Mayers, I., Wigglesworth, D. F., Rose, D. K., Kay, J. C., Mazer, C. D., Yang, H., Beattie, W. S., Doyle, D. John, Demajo, Wlifred, Comfort, V. Kim, Code, William E., Rooney, Michael E., Clark, F. J. S., Sutton, I. R., Mutch, W. A. C., Thomson, I. R., Teskey, J. M., Thiessen, O. B., Rosanbloom, M., Tang, T. K. K., Robblee, J. A., Nathan, H. J., Wynands, J. E., Eagle, C. J., Belenkle, I., Chan, K. L., Tyberg, J. V., Stockwell, M., Zintel, T., Gallagher, G., Kavanagh, B., Sandier, A., Lawson, S., Chung, F., Ong, D., Isabel, L., Trépanier, C. A., Campbell, David C., Randall, Thomas E., Growe, Gershon H., Scarth, Irene, Sawchuk C. W. T., Ong B., Unruh H., Horan T., Greengrass R., Mark, D., Kitts, J. B., Curran, M. J., Lindsay, P., Polis, T., Coté, Sylvain, Socci, Maria, Wiesel, Saul, Conway, J. B., Seyone, C., Goldberg, J., Chung, F., Rose, D. Keith, Cohen, Marsha M., Rogers, Kent H., Duncan P. G., Pope W. D. B., Tweed W. A., Biehl D., Novick, T. V., Skinner, M. I., Mathieu, Alix, Villeneuve, Edith, Goldsmith, Charles H., Allen, Gregory C., Smith, Charles E., Pinchak, Alfred C., Hagen, Joan F., Hudson, J. C., Gennings, C., Tyler, B. L., Keenan, R. L., Chung, F., Seyone, C., Matl, N., Ong, D., Powell, P., Tessler, M. J., Kleiman, S. J., Wiesel, S., Tetzlaff, John E., Yoon, Helen J., Baird, Bruce, Walsh, Michael, Hondorp, Gregory, Wassef, Medhat R., Munshi, C., Brooks, J., Nimphius, N., Tweed, W. A., Lee, T. L., Tweed, W. A., Phua, W. T., Chong, K. Y., Lim, E., Finegan, B. A., Coulson, C., Lopaschuk, G. D., Clanachan, A. S., Fournier L., Cloutier R., Major D., Sharpe, M. D., Wexler, H. R., Dhamee, M. Saeed, Rooney, R., Ong, S. K., O’Leary, E., McCarroll, M., Phelan, D., Young, T., Coghlan, D., O’Leary, E., Blunnie, W. P., Splinter, W. M., Splinter, W. M., Ryan T., Maguire M., Bouchier-Hayes D., Cunningham A. J., Kamath, M. V., Fallen, E. L., Murkin, J. M., Shannon, N. A., Montgomery, C. J., Karl, H. W., Raymond, Jacques, Drolet, Pierre, Tanguay, M., Blaise, G., Garceau, D., Dumont, L., Omri, A., Sharkawi, M., Billard, V., Bourgain, J. L., Panos, A., Mazer, C. D., Lichtenstein, S. V., Bevan, J. C., Popovic, V., Baxter, M. R. N., Donati, F., Bevan, D. R., Bachman, C., Kopelow, M., Donen, N., Umôn, D. T., Kemp, S., Hartley, E., Sikich, N., Roy, W. L., Lerman, J., Cooper, Richard M., Yentis, S. M., Bissonnette, B., Halpern, L., Roy, L., Burrows, F. A., Fear, D. W., Hillier, S., Sloan, M., Crawford, M., Blssonnette, B., Sikich, N., Friedlander, M., Sandier, A. N., Panos, L., Winton, T., Benureof, J., Karski J., Teasdale S., Cruise C., Skala R., Zulys V., Ong, D., Chow, F., Packota, G., Yip, R., Bradley, J., Arellano, R., Sussman, G., Sosis, M., Braverman, B., Sosis, M., Ivankovich, A. D., Manganas, M., Lephay, A., Fournier, Th., Kadri, N., Ossart, M., Sandier, A. N., Turner, K. E., Wick, V., Wherrett, C., Sullivan, P. J., Dyck, J. B., Varvel, J., Shafer, S. L., Fiset, P., Balendran, P., Meistelman, C., Lira, E., Sloan, M., Nigrovic, V., Banoub, M., Splinter, W. M., Roberts, D. W., Rhine, E. J., MacNeill, H. B., Bonn, G. E., Clarke, W. M., Noel, L. P., Ryan T., Moriarty J., Bouchier-Hayes D., Cunningham A. J., Sandier, A. N., Baxter, A. D., Norman, P., Samson, B., Hull, K., Chung, F., Mali, N., Evans, D., Cruise, C., Shumka, D., Seyone, C., Leung, Peter T., Badner, N. H., Komar, W. E., Rajasingham, M., Farren, B., Vaillancourt, G., Cournoyer, S., Hollmann, C., Breen, T. W., Janzen, J. A., Crochetiere, C. T., McMorland, G. H., Douglas, M. J., Kamani, A. A., Arora, Sunil K., Tunstall, M., Ross, J., Mayer, D. C., Weeks, S. K., Norman, P., Daley, D., Sandier, A., Guay, J., Gaudreault, P., Boulanger, A., Tang, A., Lortie, L., Dupuis, C., Backman, S. B., Bachoo, M., Polosa, C., Moudgil, G. C., Frame, B., Blajchman, H. A., Singal, D. P., Albert, J. -F., Ratcliff, A., Law, J. -C., Varvel, J., Hung, O., Shafer, S. L., Fiset, P., Balendran, P., Burgess, P. M., Doak, G. J., Duke, P. C., Sloan, P. A., Mather, L. E., McLean, C. F., Rutten, A. J., Nation, R. L., Milne, R. W., Runciman, W. B., Somoggi, A. A., Haack, Carol, Shafer, Steven L., Irish, Craig L., Weisleider, Louis, Mazer, C. David, Bell, Robert S., Dejonckheere, M., Levarlet, M., d’Hollander, A., Taylor, R. H., Sikich, N., Campbell, F., McLeod, M. E., Swartz, J., Spahr-Schopfer, I., McIntyre, B. G., Roy, W. L., Laycock, G. J. A., Mitchell, I. M., Morton, N. S., Logan, R. W., Campbell, F., Yentis, S. M., Fear, D., Halpem, L., Sloan, M., Badgwell, J. Michael, Kleinman, Sam, Yentis, S. M., Britton, J. T., Hannallah, R. S., Schafer, P. O., Norden, J. M., Splinter, W. M., Menard, E. A., Derdamezi, J. B., Ghurch, J. G., Britt, B. A., Radde, I. C., Sosis, M., Kao, Y. James, Norton, Richard G., Volgyesi, G. A., Spahr-Schopfer, I., Sosis, M., Plum, Mark, Sosis, M., Smith, C. E., Pinchak, A. C., Hancock, D. E., Owen, P., McMeekin, J., Hanson, S., Cujec, B., Feindel, C. M., Cruz, J., Boylen, P., Ong, D., Murphy, J. T., Dupuis, J. Y., Nathan, H. J., Cattran, C., Wynands, J. E., Murphy, J. T., Kinley, C. E., Sulliyan, J. A., Landymore, R. W., Robblee, James A., Labow, Rosalind, Buckley, D. N., Sharpe, M. D., Guiraudon, G., Klein, G., Yee, R., Black, J., Devitt, J. H., McLellan, B. A., Dubbin, J., Ehrlich, L. E., Ralley, F. E., Robbins, G. R., Symcs, J. F., Bourke, M., Nathan, H., Wynands, J. E., Maritime Heart Centre, and Maritime Heart Centre

Published
1991
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158. Effect of deep-sea sedimentary calcite preservation on atmospheric CO2 concentration

Author

Archer, D. and Maier-Reimer, E.

Subjects
Oceanography -- Observations, Deep-sea sounding -- Usage, Rocks, Sedimentary -- Research, Calcite -- Research, Environmental issues, Science and technology, Zoology and wildlife conservation
Abstract

Decrease in the calcite deposition rate results in a decrease of atmospheric CO2 concentration to the glacial level, and the pH of the ocean is determined by the supply of Ca2CO3 to the ocean by terrestrial weathering and the removal of carbonate by burial on sediments. The pH of the ocean is used to determine atmospheric CO2 concentration. Dissolution of Ca2CO3 in sedimentary pore water is obtained by the degradation of organic carbon in sediments.

Published
1994

161. Enhanced binding of antibodies generated during chronic HIV infection to mucus component MUC16

Author

Hendrik Streeck, Jeffrey R. Schneider, Kelly M. Fahrbach, Alison E. Mahan, Bronwyn M. Gunn, Thomas J. Hope, Shiv Pillai, Bruce D. Walker, Igal Szleifer, Anna Licht, Archer D. Smith, Neil L. Kelleher, Patrick F. Kiser, David C. Malaspina, Meegan R. Anderson, Ivan Zvonar, Anais Chapel, Marcus M. Karim, Todd J. Suscovich, Arthur Y. Kim, Galit Alter, Maryam Shansab, Marcus Altfeld, Jacquelynn Tedesco, Georg M. Lauer, and Arangassery Rosemary Bastian

Subjects
0301 basic medicine, Glycan, Glycosylation, Immunology, Medizin, Antibody Affinity, HIV Infections, HIV Antibodies, Article, Virus, Immunoglobulin G, 03 medical and health sciences, chemistry.chemical_compound, mucin, Immunity, Antibody glycosylation, Humans, Immunology and Allergy, Mucous Membrane, biology, Mucin, HIV, Membrane Proteins, Immunoglobulin Fc Fragments, Mucus, 030104 developmental biology, chemistry, Mucosal immunology, CA-125 Antigen, Vagina, HIV-1, biology.protein, Female, Antibody, Protein Binding
Abstract

Transmission of HIV across mucosal barriers accounts for the majority of HIV infections worldwide. Thus, efforts aimed at enhancing protective immunity at these sites are a top priority, including increasing virus-specific antibodies (Abs) and antiviral activity at mucosal sites. Mucin proteins, including the largest cell-associated mucin, mucin 16 (MUC16), help form mucus to provide a physical barrier to incoming pathogens. Here, we describe a natural interaction between Abs and MUC16 that is enhanced in specific disease settings such as chronic HIV infection. Binding to MUC16 was independent of IgG subclass, but strongly associated with shorter Ab glycan profiles, with agalactosylated (G0) Abs demonstrating the highest binding to MUC16. Binding of Abs to epithelial cells was diminished following MUC16 knockdown, and the MUC16 N-linked glycans were critical for binding. Further, agalactosylated VRC01 captured HIV more efficiently in MUC16. These data point to a novel opportunity to enrich Abs at mucosal sites by targeting Abs to MUC16 through changes in Fc glycosylation, potentially blocking viral movement and sequestering the virus far from the epithelial border. Thus, next-generation vaccines or monoclonal therapeutics may enhance protective immunity by tuning Ab glycosylation to promote the enrichment of Abs at mucosal barriers.

Published
2016
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167. Royal Academy of Medicine in Ireland Section of Ophthalmology: Proceedings of meeting held March, 1996

Author

Best, R. M., Traub, A. I., Hadden, D. R., Chakravarthy, U., Archer, D. B., Flitcroft, D. I., Saidléar, C. A., Eustace, P., Mulherin, M., Hulsmans, F., Geijssen, H. C., Greve, E. L., Kamalaraji, S., Earley, O., Mahon, G., Collins, A., Fulcher, T., Griffin, M., Firth, R., O’Meara, N., Acheson, R., Minihan, M., Murray, A., Moin, M., Aftab, S. A., Iqbal, F., Kinsella, F., Nolan, J., Hassim, A. A., and Mulvihill, A.

Published
1997
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168. The role of ocean transport in the uptake of anthropogenic CO2

Author

Cao, L., Eby, M., Ridgwell, A., Caldeira, K., Archer, D., Ishida, A., Joos, F., Matsumoto, K., Mikolajewicz, U., Mouchet, A., James Orr, Plattner, G. -K, Schlitzer, R., Tokos, K., Totterdell, I., Tschumi, T., Yamanaka, Y., Yool, A., Laboratoire des Sciences du Climat et de l'Environnement [Gif-sur-Yvette] (LSCE), Institut national des sciences de l'Univers (INSU - CNRS)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université de Versailles Saint-Quentin-en-Yvelines (UVSQ), Modelling the Earth Response to Multiple Anthropogenic Interactions and Dynamics (MERMAID), Institut national des sciences de l'Univers (INSU - CNRS)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université de Versailles Saint-Quentin-en-Yvelines (UVSQ)-Institut national des sciences de l'Univers (INSU - CNRS)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université de Versailles Saint-Quentin-en-Yvelines (UVSQ), Université de Versailles Saint-Quentin-en-Yvelines (UVSQ)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Institut national des sciences de l'Univers (INSU - CNRS)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS), and Université de Versailles Saint-Quentin-en-Yvelines (UVSQ)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Institut national des sciences de l'Univers (INSU - CNRS)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS)-Université de Versailles Saint-Quentin-en-Yvelines (UVSQ)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Institut national des sciences de l'Univers (INSU - CNRS)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS)

Subjects
[SDU.OCEAN]Sciences of the Universe [physics]/Ocean, Atmosphere, 530 Physics, [SDU.ENVI]Sciences of the Universe [physics]/Continental interfaces, environment, ComputingMilieux_MISCELLANEOUS
Abstract

We compare modeled oceanic carbon uptake in response to pulse CO2 emissions using a suite of global ocean models and Earth system models. In response to a CO2 pulse emission of 590 Pg C (corresponding to an instantaneous doubling of atmospheric CO2 from 278 to 556 ppm), the fraction of CO2 emitted that is absorbed by the ocean is: 37±8%, 56±10%, and 81±4% (model mean ±2σ ) in year 30, 100, and 1000 after the emission pulse, respectively. Modeled oceanic uptake of pulse CO2 on timescales from decades to about a century is strongly correlated with simulated present-day uptake of chlorofluorocarbons (CFCs) and CO2 across all models, while the amount of pulse CO2 absorbed by the ocean from a century to a millennium is strongly correlated with modeled radiocarbon in the deep Southern and Pacific Ocean. However, restricting the analysis to models that are capable of reproducing observations within uncertainty, the correlation is generally much weaker. The rates of surface-to-deep ocean transport are determined for individual models from the instantaneous doubling CO2 simulations, and they are used to calculate oceanic CO2 uptake in response to pulse CO2 emissions of different sizes pulses of 1000 and 5000 Pg C. These results are compared with simulated oceanic uptake of CO2 by a number of models simulations with the coupling of climate-ocean carbon cycle and without it. This comparison demonstrates that the impact of different ocean transport rates across models on oceanic uptake of anthropogenic CO2 is of similar magnitude as that of climate-carbon cycle feedbacks in a single model, emphasizing the important role of ocean transport in the uptake of anthropogenic CO2.

Published
2018
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169. Fasciola hepatica in UK horses

Author

Howell, A. K., primary, Malalana, F., additional, Beesley, N. J., additional, Hodgkinson, J. E., additional, Rhodes, H., additional, Sekiya, M., additional, Archer, D., additional, Clough, H. E., additional, Gilmore, P., additional, and Williams, D. J. L., additional

Published
2019
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175. Irish college of ophthalmologists: Proceedings of annual conference held april 29th & 30th 1993.

Author

O’Sullivan, J., Kilmartin, D., Saidlear, C., Eustace, P., Kinsella, F., Best, R. M., Hope-Ross, M., Kervick, G. N., Robinson, F. O., Page, A. B., Archer, D. B., Joyce, P. W., Raj, P. Sunder, Kirby, J., Watson, A. P., Villada, J. R., Foley-Nolan, A, Beigi, B., Vincent, M., Brennan, M., Murphy, M. F., Sharma, N. K., Madden, M., Burke, J. P., Scott, W. E., Kutschke, P. J., Orton, H. P., West, J., Strachan, I. M., Hockey, M. S., Ferguson, D. G., Heravi, M. H., and Lotery, A. J.

Published
1993
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176. The Critical Role of Global and Culturally Responsive Leadership for Higher Education in the 21st-Century.

Author

Archer, D. Eric and Yuqian Zhang

Subjects
EDUCATIONAL leadership, HIGHER education
Abstract

This short essay discusses the critical role of global and culturally responsive leadership for higher education in the 21st-Century. Using the concept of Complex Adaptive Systems (CAS), global and culturally responsive leadership should be emergent and interactive to respond in an agile way to the fast-paced, volatile context of the knowledge era. [ABSTRACT FROM AUTHOR]

Published
2021

179. Applying Label-Free Quantitation to Top Down Proteomics

Author

Paul M. Thomas, Richard D. LeDuc, Neil L. Kelleher, Bryan P. Early, John P. Savaryn, Owen S. Skinner, Ioanna Ntai, Ryan T. Fellers, Kyunggon Kim, and Archer D. Smith

Subjects
Proteomics, 0303 health sciences, Chemistry, Pipeline (computing), 010401 analytical chemistry, Proteins, Saccharomyces cerevisiae, Computational biology, Replicate, Top-down proteomics, 01 natural sciences, Molecular biology, Article, Histone Deacetylases, 0104 chemical sciences, Analytical Chemistry, 03 medical and health sciences, Label-free quantification, Volcano plot, Biological variation, Mutation, 030304 developmental biology, Total protein
Abstract

With the prospect of resolving whole protein molecules into their myriad proteoforms on a proteomic scale, the question of their quantitative analysis in discovery mode comes to the fore. Here, we demonstrate a robust pipeline for the identification and stringent scoring of abundance changes of whole protein forms

Published
2014
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183. Successful treatment of a splenic abscess secondary to migrant metallic wires in a horse.

Author

Thomson, C., Archer, D., Ahern, B., and Medina‐Torres, C. E.

Subjects
*METALLIC wire, *OPERATIVE surgery, *ABSCESSES, *HORSES, *SURGICAL complications, *PATHOLOGIC neovascularization, *HORSE breeds
Abstract

Summary: This case report discusses a successful partial splenectomy for treatment of a splenic abscess in a horse. A 2‐year‐old Thoroughbred colt was hospitalised 5 weeks after an episode of severe colic that was followed by gradual weight loss and anorexia, pyrexia for 5 days and dehydration on the day of referral. A large splenic abscess was identified ultrasonographically. Following initial medical treatment, an exploratory laparotomy was performed. Multiple adhesions were released and a partial splenectomy conducted to remove the abscess. Migrant metallic wires penetrating from the small intestine into the splenic parenchyma were found to be the cause for the adhesions and the abscess. This paper summarises the potential advantages of utilising a partial vs. a total splenectomy and highlights the potential complications of these surgical procedure in equines. [ABSTRACT FROM AUTHOR]

Published
2020
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184. Fasciola hepatica in UK horses.

Author

Howell, A. K., Malalana, F., Beesley, N. J., Hodgkinson, J. E., Rhodes, H., Sekiya, M., Archer, D., Clough, H. E., Gilmore, P., and Williams, D. J. L.

Abstract

Summary: Background: Fasciola hepatica (liver fluke) affects grazing animals including horses but the extent to which it affects UK horses is unknown. Objectives: To define how liver fluke affects the UK horse population. Study design: Descriptive, cross‐sectional, observational study. Methods: An F. hepatica excretory‐secretory antibody detection ELISA with a diagnostic sensitivity of 71% and specificity of 97% was validated and used to analyse serum samples. An abattoir study was performed to determine prevalence. A case‐control study of 269 horses compared fluke exposure between horses with liver disease and controls. Data on clinical signs and blood test results were collected for sero‐positive horses. Genotyping of adult fluke was used to produce a multilocus genotype for each parasite. Results: Four (2.2%) of 183 horses registered in the UK, sampled in the abattoir, had adult flukes in the liver, and the sero‐prevalence of F. hepatica was estimated as 8.7%. In the case‐control study, horses showing signs consistent with liver disease had significantly higher odds of testing positive for F. hepatica on ELISA than control horses. In 23 sero‐positive horses, a range of non‐specific clinical signs and blood test abnormalities was reported, with a third of the horses showing no signs. Genotypic analysis of liver flukes from horses provided evidence that these came from the same population as flukes from sheep and cattle. Main limitations: Bias could have arisen in the prevalence and case‐control studies due to convenience sampling methods, in particular the geographic origin of the horses. Only a small number of horses tested positive so the data on clinical signs are limited. Conclusions: Exposure to liver fluke occurs frequently in horses and may be an under‐recognised cause of liver disease. Flukes isolated from horses are from the same population as those found in ruminants. When designing and implementing parasite control plans, fluke should be considered, and horses should be tested if appropriate. [ABSTRACT FROM AUTHOR]

Published
2020
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185. How to critically appraise a paper.

Author

Pinchbeck, G. L. and Archer, D. C.

Subjects
*DECISION making, *VETERINARY medicine, *EVIDENCE-based medicine
Abstract

Summary: Critical appraisal skills enabling assessment of the validity and importance of evidence are essential for clinicians to make informed decisions regarding what new information should be incorporated into their clinical practice. This review highlights key points to consider in a critical review concentrating on common study designs used in the equine literature. [ABSTRACT FROM AUTHOR]

Published
2020
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186. A novel approach for palatal cyst ablation in a horse.

Author

Sinovich, M., Kelly, P. G., and Archer, D. C.

Subjects
SOFT palate, SEMICONDUCTOR lasers, TEACHING hospitals, UNIVERSITY hospitals, COLLEGE teaching, ARTIFICIAL palates, HORSE equipment
Abstract

Summary: An 18‐month‐old Welsh Cob was referred to a university teaching hospital for investigation of abnormal respiratory noise at rest. Video‐endoscopy revealed persistent displacement of the soft palate with bilateral 2–3 cm diameter raised areas on either side of the midline. Neither trans‐nasal nor oral approaches allowed sufficient visualisation of the caudal soft palate for diagnosis or treatment. Latero‐lateral radiographs showed a blunted, thickened caudal edge of the soft palate consistent with a palatal cyst. Two palatal cysts were thermally ablated with a transendoscopic diode laser via temporary tracheotomy. The horse recovered uneventfully and resolution of the displacement was evident on follow‐up endoscopy 11 months later. This report documents a novel surgical approach to the caudal aspect of the soft palate. [ABSTRACT FROM AUTHOR]

Published
2020
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198. Rotational bands and isomeric states in 175Lu

Author

Garrett, P, primary, Archer, D, additional, Becker, J, additional, Bernstein, L, additional, Hauschild, K, additional, Henry, E, additional, McNabb, D, additional, Stoyer, M, additional, Younes, W, additional, Johns, G, additional, Nelson, R, additional, and Wilburn, W, additional

Published
2003
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200. Ubp-M serine 552 phosphorylation by cyclin-dependent kinase 1 regulates cell cycle progression

Author

David A. Schneider, Jei-Hwa Yu, Hengbin Wang, Matthew B. Renfrow, Heui-Yun Joo, Louise T. Chow, Huirong Yang, Yang Xu, and Archer D. Smith

Subjects
G2 Phase, Recombinant Fusion Proteins, Amino Acid Motifs, Receptors, Cytoplasmic and Nuclear, Karyopherins, Biology, environment and public health, Cyclin-dependent kinase, Report, CDC2 Protein Kinase, Serine, Humans, CHEK1, Phosphorylation, Molecular Biology, Cell Proliferation, Serine/threonine-specific protein kinase, Cyclin-dependent kinase 1, Cyclin-dependent kinase 2, Cyclin-dependent kinase 3, Cell Cycle Checkpoints, Cell Biology, Chromatin, Cell biology, Biochemistry, biology.protein, Ubiquitin Thiolesterase, Cell Division, HeLa Cells, Developmental Biology
Abstract

In eukaryotic cells, genomic DNA is organized into a chromatin structure, which not only serves as the template for DNA-based nuclear processes, but also as a platform integrating intracellular and extracellular signals. Although much effort has been spent to characterize chromatin modifying/remodeling activities, little is known about cell signaling pathways targeting these chromatin modulators. Here, we report that cyclin-dependent kinase 1 (CDK1) phosphorylates the histone H2A deubiquitinase Ubp-M at serine 552 (S552P), and, importantly, this phosphorylation is required for cell cycle progression. Mass spectrometry analysis confirmed Ubp-M is phosphorylated at serine 552, and in vitro and in vivo assays demonstrated that CDK1/cyclin B kinase is responsible for Ubp-M S552P. Interestingly, Ubp-M S552P is not required for Ubp-M tetramer formation, deubiquitination activity, substrate specificity, or regulation of gene expression. However, Ubp-M S552P is required for cell proliferation and cell cycle G 2/M phase progression. Ubp-M S552P reduces Ubp-M interaction with nuclear export protein CRM1 and facilitates Ubp-M nuclear localization. Therefore, these studies confirm that Ubp-M is phosphorylated at S552 and identify CDK1 as the enzyme responsible for the phosphorylation. Importantly, this study specifically links Ubp-M S552P to cell cycle G 2/M phase progression.

Published
2013
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