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On February 23, 2018, PubMed Central Canada (PMC Canada) will be taken offline permanently. No author manuscripts will be deleted, and the approximately 2,900 manuscripts authored by Canadian Institutes of Health Research (CIHR)-funded researchers currently in the archive will be copied to the National Research Council’s (NRC) Digital Repository over the coming months. These manuscripts along with all other content will also remain publicly searchable on PubMed Central (US) and Europe PubMed Central, meaning such manuscripts will continue to be compliant with the Tri-Agency Open Access Policy on Publications.

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1.  Search for lepton flavour violation in the eμ continuum with the ATLAS detector in \documentclass[12pt]{minimal} \usepackage{amsmath} \usepackage{wasysym} \usepackage{amsfonts} \usepackage{amssymb} \usepackage{amsbsy} \usepackage{mathrsfs} \usepackage{upgreek} \setlength{\oddsidemargin}{-69pt} \begin{document}$\sqrt{s} = 7~\mbox{TeV}$\end{document}pp collisions at the LHC 
Aad, G. | Abbott, B. | Abdallah, J. | Abdelalim, A. A. | Abdesselam, A. | Abdinov, O. | Abi, B. | Abolins, M. | Abramowicz, H. | Abreu, H. | Acerbi, E. | Acharya, B. S. | Adams, D. L. | Addy, T. N. | Adelman, J. | Adomeit, S. | Adragna, P. | Adye, T. | Aefsky, S. | Aguilar-Saavedra, J. A. | Aharrouche, M. | Ahlen, S. P. | Ahles, F. | Ahmad, A. | Ahsan, M. | Aielli, G. | Akdogan, T. | Åkesson, T. P. A. | Akimoto, G. | Akimov, A. V. | Akiyama, A. | Aktas, A. | Alam, M. S. | Alam, M. A. | Albrand, S. | Aleksa, M. | Aleksandrov, I. N. | Aleppo, M. | Alessandria, F. | Alexa, C. | Alexander, G. | Alexandre, G. | Alexopoulos, T. | Alhroob, M. | Aliev, M. | Alimonti, G. | Alison, J. | Aliyev, M. | Allport, P. P. | Allwood-Spiers, S. E. | Almond, J. | Aloisio, A. | Alon, R. | Alonso, A. | Alviggi, M. G. | Amako, K. | Amelung, C. | Ammosov, V. V. | Amorim, A. | Amorós, G. | Amram, N. | Anastopoulos, C. | Andeen, T. | Anders, C. F. | Anderson, K. J. | Andreazza, A. | Andrei, V. | Anduaga, X. S. | Angerami, A. | Anghinolfi, F. | Anjos, N. | Annovi, A. | Antonaki, A. | Antonelli, M. | Antonelli, S. | Antonov, A. | Antos, J. | Anulli, F. | Aoun, S. | Aperio Bella, L. | Apolle, R. | Arabidze, G. | Aracena, I. | Arai, Y. | Arce, A. T. H. | Archambault, J. P. | Arfaoui, S. | Arguin, J-F. | Arik, E. | Arik, M. | Armbruster, A. J. | Arnaez, O. | Arnault, C. | Artamonov, A. | Artoni, G. | Arutinov, D. | Asai, M. | Asai, S. | Asfandiyarov, R. | Ask, S. | Åsman, B. | Asner, D. | Asquith, L. | Assamagan, K. | Astbury, A. | Astvatsatourov, A. | Atoian, G. | Aubert, B. | Auge, E. | Augsten, K. | Aurousseau, M. | Austin, N. | Avolio, G. | Avramidou, R. | Axen, D. | Azuelos, G. | Azuma, Y. | Baak, M. A. | Baccaglioni, G. | Bacci, C. | Bach, A. M. | Bachacou, H. | Bachas, K. | Bachy, G. | Backes, M. | Backhaus, M. | Badescu, E. | Bagnaia, P. | Bahinipati, S. | Bai, Y. | Bailey, D. C. | Bain, T. | Baines, J. T. | Baker, O. K. | Baker, M. 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H. | Bella, G. | Bellagamba, L. | Bellina, F. | Bellomo, G. | Bellomo, M. | Belloni, A. | Beloborodova, O. | Belotskiy, K. | Beltramello, O. | Ben Ami, S. | Benary, O. | Benchekroun, D. | Benchouk, C. | Bendel, M. | Benedict, B. H. | Benekos, N. | Benhammou, Y. | Benjamin, D. P. | Benoit, M. | Bensinger, J. R. | Benslama, K. | Bentvelsen, S. | Beretta, M. | Berge, D. | Bergeaas Kuutmann, E. | Berger, N. | Berghaus, F. | Berglund, E. | Beringer, J. | Bernardet, K. | Bernat, P. | Bernhard, R. | Bernius, C. | Berry, T. | Bertin, A. | Bertolucci, F. | Besana, M. I. | Besson, N. | Bethke, S. | Bhimji, W. | Bianchi, R. M. | Bianco, M. | Biebel, O. | Bieniek, S. P. | Biesiada, J. | Biglietti, M. | Bilokon, H. | Bindi, M. | Binet, S. | Bingul, A. | Bini, C. | Biscarat, C. | Bitenc, U. | Black, K. M. | Blair, R. E. | Blanchard, J.-B. | Blanchot, G. | Blocker, C. | Blocki, J. | Blondel, A. | Blum, W. | Blumenschein, U. | Bobbink, G. J. | Bobrovnikov, V. B. | Bocchetta, S. 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K. | Brown, G. | Brubaker, E. | Bruckman de Renstrom, P. A. | Bruncko, D. | Bruneliere, R. | Brunet, S. | Bruni, A. | Bruni, G. | Bruschi, M. | Buanes, T. | Bucci, F. | Buchanan, J. | Buchanan, N. J. | Buchholz, P. | Buckingham, R. M. | Buckley, A. G. | Buda, S. I. | Budagov, I. A. | Budick, B. | Büscher, V. | Bugge, L. | Buira-Clark, D. | Buis, E. J. | Bulekov, O. | Bunse, M. | Buran, T. | Burckhart, H. | Burdin, S. | Burgess, T. | Burke, S. | Busato, E. | Bussey, P. | Buszello, C. P. | Butler, B. | Butler, J. M. | Buttar, C. M. | Butterworth, J. M. | Buttinger, W. | Byatt, T. | Caballero, J. | Cabrera Urbán, S. | Caccia, M. | Caforio, D. | Cakir, O. | Calafiura, P. | Calderini, G. | Calfayan, P. | Calkins, R. | Caloba, L. P. | Caloi, R. | Calvet, D. | Calvet, S. | Camacho Toro, R. | Camard, A. | Camarri, P. | Cameron, D. | Cammin, J. | Campana, S. | Campanelli, M. | Canale, V. | Canelli, F. | Canepa, A. | Cantero, J. | Capasso, L. | Capeans Garrido, M. D. 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A. | Chen, C. | Chen, H. | Chen, L. | Chen, S. | Chen, X. | Cheplakov, A. | Cherkaoui El Moursli, R. | Chernyatin, V. | Cheu, E. | Cheung, S. L. | Chevalier, L. | Chiefari, G. | Chikovani, L. | Childers, J. T. | Chilingarov, A. | Chiodini, G. | Chizhov, M. V. | Choudalakis, G. | Chouridou, S. | Christidi, I. A. | Christov, A. | Chromek-Burckhart, D. | Chu, M. L. | Chudoba, J. | Ciapetti, G. | Ciba, K. | Ciftci, A. K. | Ciftci, R. | Cinca, D. | Cindro, V. | Ciobotaru, M. D. | Ciocca, C. | Ciocio, A. | Cirilli, M. | Citterio, M. | Ciubancan, M. | Clark, A. | Clark, P. J. | Cleland, W. | Clemens, J. C. | Clement, B. | Clement, C. | Clifft, R. W. | Coadou, Y. | Cobal, M. | Coccaro, A. | Cochran, J. | Coe, P. | Coelli, S. | Cogan, J. G. | Coggeshall, J. | Cogneras, E. | Cojocaru, C. D. | Colas, J. | Colijn, A. P. | Collard, C. | Collins, N. J. | Collins-Tooth, C. | Collot, J. | Colon, G. | Coluccia, R. | Comune, G. | Conde Muiño, P. | Coniavitis, E. | Conidi, M. 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G. | Dubbert, J. | Dubbs, T. | Dube, S. | Duchovni, E. | Duckeck, G. | Dudarev, A. | Dudziak, F. | Dührssen, M. | Duerdoth, I. P. | Duflot, L. | Dufour, M-A. | Dunford, M. | Duran Yildiz, H. | Duxfield, R. | Dwuznik, M. | Dydak, F. | Dzahini, D. | Düren, M. | Ebke, J. | Eckert, S. | Eckweiler, S. | Edmonds, K. | Edwards, C. A. | Efthymiopoulos, I. | Egorov, K. | Ehrenfeld, W. | Ehrich, T. | Eifert, T. | Eigen, G. | Einsweiler, K. | Eisenhandler, E. | Ekelof, T. | El Kacimi, M. | Ellert, M. | Elles, S. | Ellinghaus, F. | Ellis, K. | Ellis, N. | Elmsheuser, J. | Elsing, M. | Ely, R. | Emeliyanov, D. | Engelmann, R. | Engl, A. | Epp, B. | Eppig, A. | Erdmann, J. | Ereditato, A. | Eriksson, D. | Ernst, J. | Ernst, M. | Ernwein, J. | Errede, D. | Errede, S. | Ertel, E. | Escalier, M. | Escobar, C. | Espinal Curull, X. | Esposito, B. | Etienne, F. | Etienvre, A. I. | Etzion, E. | Evangelakou, D. | Evans, H. | Fabbri, L. | Fabre, C. | Facius, K. | Fakhrutdinov, R. M. | Falciano, S. | Falou, A. C. | Fang, Y. | Fanti, M. | Farbin, A. | Farilla, A. | Farley, J. | Farooque, T. | Farrington, S. M. | Farthouat, P. | Fasching, D. | Fassnacht, P. | Fassouliotis, D. | Fatholahzadeh, B. | Favareto, A. | Fayard, L. | Fazio, S. | Febbraro, R. | Federic, P. | Fedin, O. L. | Fedorko, I. | Fedorko, W. | Fehling-Kaschek, M. | Feligioni, L. | Fellmann, D. | Felzmann, C. U. | Feng, C. | Feng, E. J. | Fenyuk, A. B. | Ferencei, J. | Fernandes, B. | Fernando, W. | Ferrag, S. | Ferrando, J. | Ferrara, V. | Ferrari, A. | Ferrari, P. | Ferrari, R. | Ferrer, A. | Ferrer, M. L. | Ferrere, D. | Ferretti, C. | Ferretto Parodi, A. | Fiascaris, M. | Fiedler, F. | Filipčič, A. | Filippas, A. | Filthaut, F. | Fincke-Keeler, M. | Fiolhais, M. C. N. | Fiorini, L. | Firan, A. | Fischer, G. | Fischer, P. | Fisher, M. J. | Fisher, S. M. | Flammer, J. | Flechl, M. | Fleck, I. | Fleckner, J. | Fleischmann, P. | Fleischmann, S. | Flick, T. | Flores Castillo, L. R. | Flowerdew, M. J. | Föhlisch, F. | Fonseca Martin, T. | Fopma, J. | Formica, A. | Forti, A. | Fortin, D. | Fournier, D. | Fowler, A. J. | Fowler, K. | Fox, H. | Francavilla, P. | Franchino, S. | Francis, D. | Frank, T. | Franklin, M. | Franz, S. | Fraternali, M. | Fratina, S. | Freestone, J. | French, S. T. | Froeschl, R. | Froidevaux, D. | Frost, J. A. | Fukunaga, C. | Fullana Torregrosa, E. | Fuster, J. | Gabaldon, C. | Gabizon, O. | Gadfort, T. | Gadomski, S. | Gagliardi, G. | Gagnon, P. | Galea, C. | Gallas, E. J. | Gallas, M. V. | Gallo, V. | Gallop, B. J. | Gallus, P. | Galyaev, E. | Gan, K. K. | Gao, Y. S. | Gaponenko, A. | Garberson, F. | Garcia-Sciveres, M. | García, C. | García Navarro, J. E. | Gardner, R. W. | Garelli, N. | Garitaonandia, H. | Garonne, V. | Garvey, J. | Gatti, C. | Gaudio, G. | Gaumer, O. | Gaur, B. | Gauthier, L. | Gauzzi, P. | Gavrilenko, I. L. | Gay, C. | Gaycken, G. | Gazis, E. N. | Ge, P. | Gee, C. N. P. | Geerts, D. A. A. | Geich-Gimbel, Ch. | Gellerstedt, K. | Gemme, C. | Gemmell, A. | Genest, M. H. | Gentile, S. | George, M. | George, S. | Gerlach, P. | Gershon, A. | Geweniger, C. | Ghazlane, H. | Ghodbane, N. | Giacobbe, B. | Giagu, S. | Giakoumopoulou, V. | Giangiobbe, V. | Gianotti, F. | Gibbard, B. | Gibson, A. | Gibson, S. M. | Gieraltowski, G. F. | Gilchriese, M. | Gillberg, D. | Gillman, A. R. | Gingrich, D. M. | Ginzburg, J. | Giokaris, N. | Giordani, M. P. | Giordano, R. | Giorgi, F. M. | Giovannini, P. | Giraud, P. F. | Giugni, D. | Giusti, P. | Gjelsten, B. K. | Gladilin, L. K. | Glasman, C. | Glatzer, J. | Glazov, A. | Glitza, K. W. | Glonti, G. L. | Godfrey, J. | Godlewski, J. | Goebel, M. | Göpfert, T. | Goeringer, C. | Gössling, C. | Göttfert, T. | Goldfarb, S. | Goldin, D. | Golling, T. | Golovnia, S. N. | Gomes, A. | Gomez Fajardo, L. S. | Gonçalo, R. | Goncalves Pinto Firmino Da Costa, J. | Gonella, L. | Gonzalez, S. | González de la Hoz, S. | Gonzalez Silva, M. L. | Gonzalez-Sevilla, S. | Goodson, J. J. | Goossens, L. | Gorbounov, P. A. | Gordon, H. A. | Gorelov, I. | Gorfine, G. | Gorini, B. | Gorini, E. | Gorišek, A. | Gornicki, E. | Gorokhov, S. A. | Gosdzik, B. | Gosselink, M. | Gostkin, M. I. | Gouanère, M. | Gough Eschrich, I. | Gouighri, M. | Goujdami, D. | Goulette, M. P. | Goussiou, A. G. | Goy, C. | Grabowska-Bold, I. | Grabski, V. | Grafström, P. | Grah, C. | Grahn, K-J. | Grancagnolo, F. | Grancagnolo, S. | Grassi, V. | Gratchev, V. | Grau, N. | Gray, H. M. | Gray, J. A. | Graziani, E. | Grebenyuk, O. G. | Green, B. | Greenfield, D. | Greenshaw, T. | Greenwood, Z. D. | Gregor, I. M. | Grenier, P. | Griesmayer, E. | Griffiths, J.
This paper presents a search for the t-channel exchange of an R-parity violating scalar top quark (\documentclass[12pt]{minimal} \usepackage{amsmath} \usepackage{wasysym} \usepackage{amsfonts} \usepackage{amssymb} \usepackage{amsbsy} \usepackage{mathrsfs} \usepackage{upgreek} \setlength{\oddsidemargin}{-69pt} \begin{document}$\tilde{t}$\end{document}) in the e±μ∓ continuum using 2.1 fb−1 of data collected by the ATLAS detector in \documentclass[12pt]{minimal} \usepackage{amsmath} \usepackage{wasysym} \usepackage{amsfonts} \usepackage{amssymb} \usepackage{amsbsy} \usepackage{mathrsfs} \usepackage{upgreek} \setlength{\oddsidemargin}{-69pt} \begin{document}$\sqrt{s}=7~\mbox{TeV}$\end{document}pp collisions at the Large Hadron Collider. Data are found to be consistent with the expectation from the Standard Model backgrounds. Limits on R-parity-violating couplings at 95 % C.L. are calculated as a function of the scalar top mass (\documentclass[12pt]{minimal} \usepackage{amsmath} \usepackage{wasysym} \usepackage{amsfonts} \usepackage{amssymb} \usepackage{amsbsy} \usepackage{mathrsfs} \usepackage{upgreek} \setlength{\oddsidemargin}{-69pt} \begin{document}$m_{\tilde{t}}$\end{document}). The upper limits on the production cross section for pp→eμX, through the t-channel exchange of a scalar top quark, ranges from 170 fb for \documentclass[12pt]{minimal} \usepackage{amsmath} \usepackage{wasysym} \usepackage{amsfonts} \usepackage{amssymb} \usepackage{amsbsy} \usepackage{mathrsfs} \usepackage{upgreek} \setlength{\oddsidemargin}{-69pt} \begin{document}$m_{\tilde{t}}=95~\mbox{GeV}$\end{document} to 30 fb for \documentclass[12pt]{minimal} \usepackage{amsmath} \usepackage{wasysym} \usepackage{amsfonts} \usepackage{amssymb} \usepackage{amsbsy} \usepackage{mathrsfs} \usepackage{upgreek} \setlength{\oddsidemargin}{-69pt} \begin{document}$m_{\tilde{t}}=1000~\mbox{GeV}$\end{document}.
doi:10.1140/epjc/s10052-012-2040-z
PMCID: PMC4370899  PMID: 25814838
2.  A Collaboratively-Derived Science-Policy Research Agenda 
PLoS ONE  2012;7(3):e31824.
The need for policy makers to understand science and for scientists to understand policy processes is widely recognised. However, the science-policy relationship is sometimes difficult and occasionally dysfunctional; it is also increasingly visible, because it must deal with contentious issues, or itself becomes a matter of public controversy, or both. We suggest that identifying key unanswered questions on the relationship between science and policy will catalyse and focus research in this field. To identify these questions, a collaborative procedure was employed with 52 participants selected to cover a wide range of experience in both science and policy, including people from government, non-governmental organisations, academia and industry. These participants consulted with colleagues and submitted 239 questions. An initial round of voting was followed by a workshop in which 40 of the most important questions were identified by further discussion and voting. The resulting list includes questions about the effectiveness of science-based decision-making structures; the nature and legitimacy of expertise; the consequences of changes such as increasing transparency; choices among different sources of evidence; the implications of new means of characterising and representing uncertainties; and ways in which policy and political processes affect what counts as authoritative evidence. We expect this exercise to identify important theoretical questions and to help improve the mutual understanding and effectiveness of those working at the interface of science and policy.
doi:10.1371/journal.pone.0031824
PMCID: PMC3302883  PMID: 22427809
3.  The carbon monoxide releasing molecule (CORM-3) inhibits expression of vascular cell adhesion molecule-1 and E-selectin independently of haem oxygenase-1 expression 
British Journal of Pharmacology  2009;157(5):769-780.
Background and purpose:
Although carbon monoxide (CO) can modulate inflammatory processes, the influence of CO on adhesion molecules is less clear. This might be due to the limited amount of CO generated by haem degradation. We therefore tested the ability of a CO releasing molecule (CORM-3), used in supra-physiological concentrations, to modulate the expression of vascular cell adhesion molecule (VCAM)-1 and E-selectin on endothelial cells and the mechanism(s) involved.
Experimental approach:
Human umbilical vein endothelial cells (HUVECs) were stimulated with tumour necrosis factor (TNF)-α in the presence or absence of CORM-3. The influence of CORM-3 on VCAM-1 and E-selectin expression and the nuclear factor (NF)-κB pathway was assessed by flow cytometry, Western blotting and electrophoretic mobility shift assay.
Key results:
CORM-3 inhibited the expression of VCAM-1 and E-selectin on TNF-α-stimulated HUVEC. VCAM-1 expression was also inhibited when CORM-3 was added 24 h after TNF-α stimulation or when TNF-α was removed. This was paralleled by deactivation of NF-κB and a reduction in VCAM-1 mRNA. Although TNF-α removal was more effective in this regard, VCAM-1 protein was down-regulated more rapidly when CORM-3 was added. CORM-3 induced haem oxygenase-1 (HO-1) in a dose- and time-dependent manner, mediated by the transcription factor, Nrf2. CORM-3 was still able to down-regulate VCAM-1 expression in HUVEC transfected with siRNA for HO-1 or Nrf2.
Conclusions and implications:
Down-regulation of VCAM and E-selectin expression induced by CORM-3 was independent of HO-1 up-regulation and was predominantly due to inhibition of sustained NF-κB activation.
doi:10.1111/j.1476-5381.2009.00215.x
PMCID: PMC2721262  PMID: 19422386
endothelial cells; adhesion molecules; inflammation; carbon monoxide
4.  Distinguishing Characteristics of Serotonin and Non-Serotonin-Containing Cells in the Dorsal Raphe Nucleus: Electrophysiological and Immunohistochemical Studies 
Neuroscience  2003;116(3):669-683.
The membrane properties and receptor-mediated responses of rat dorsal raphe nucleus neurons were measured using intracellular recording techniques in a slice preparation. After each experiment, the recorded neuron was filled with neurobiotin and immunohistochemically identified as 5-hydroxytryptamine (5-HT)-immunopositive or 5-HT-immunonegative. The cellular characteristics of all recorded neurons conformed to previously determined classic properties of serotonergic dorsal raphe nucleus neurons: slow, rhythmic activity in spontaneously active cells, broad action potential and large afterhyperpolarization potential. Two electrophysiological characteristics were identified that distinguished 5-HT from non-5-HT-containing cells in this study. In 5-HT-immunopositive cells, the initial phase of the afterhyperpolarization potential was gradual (tau=7.3±1.9) and in 5-HT-immunonegative cells it was abrupt (tau=1.8±0.6). In addition, 5-HT-immunopositive cells had a shorter membrane time constant (tau=21.4±4.4) than 5-HT-immunonegative cells (tau=33.5±4.2). Interestingly, almost all recorded neurons were hyperpolarized in response to stimulation of the inhibitory 5-HT1A receptor. These results suggested that 5-HT1A receptors are present on non-5-HT as well as 5-HT neurons. This was confirmed by immunohistochemistry showing that although the majority of 5-HT-immunopositive cells in the dorsal raphe nucleus were double-labeled for 5-HT1A receptor-IR, a small but significant population of 5-HT-immunonegative cells expressed the 5-HT1A receptor. These results underscore the heterogeneous nature of the dorsal raphe nucleus and highlight two membrane properties that may better distinguish 5-HT from non-5-HT cells than those typically reported in the literature. In addition, these results present electrophysiological and anatomical evidence for the presence of 5-HT1A receptors on non-5-HT neurons in the dorsal raphe nucleus.
PMCID: PMC2832757  PMID: 12573710
5-HT; 5-HT1A receptor; intracellular; slice; rat
6.  Prospective case control study on genetic assocation of apolipoprotein ɛ2 with intraocular pressure 
doi:10.1136/bjo.2003.020305
PMCID: PMC1772093  PMID: 15031182
apolipoprotein E; gene polymorphism; glaucoma; intraocular pressure
7.  Inhibition of LPS-induced chemokine production in human lung endothelial cells by lipid conjugates anchored to the membrane 
British Journal of Pharmacology  2002;135(7):1665-1674.
In acute respiratory distress syndrome (ARDS) induced by endotoxins, a high production of inflammatory mediators by microvascular lung endothelial cells (LMVEC) can be observed. Activation of cells by endotoxins may result in elevated secretion of phospholipase A2 (sPLA2) which is thought to contribute to tissue damage. The present study was undertaken to investigate the role of sPLA2 in chemokine production in human lung microvascular endothelial cells (LMVEC) stimulated with the endotoxins lipopolysaccharide (LPS) and lipoteichoic acid (LTA). In particular, we investigated the effects of sPLA2 inhibitors, specifically, the extracellular PLA2 inhibitors (ExPLIs), composed of N-derivatized phosphatidyl-ethanolamine linked to polymeric carriers, and LY311727, a specific inhibitor of non-pancreatic sPLA2.ExPLIs markedly inhibited LPS and LTA induced production and mRNA expression of the neutrophile attracting chemokines IL-8, Gro-α and ENA-78, as well as of the adhesion molecules ICAM-1 and E-selectin. Concomitantly, ExPLIs inhibited the LPS-induced activation of NF-κB by LPS but not its activation by TNF-α or IL-1.Endotoxin mediated chemokine production in LMVEC seems not to involve PLA2 activity, since LPS stimulation was not associated with activation of intracellular or secreted PLA2. It therefore seems that the inhibitory effect of the ExPLIs was not due to their PLA2 inhibiting capacity. This was supported by the finding that the LPS-induced chemokine production was not affected by the selective sPLA2 inhibitor LY311727.It is proposed that the ExPLIs may be considered a prototype of potent suppressors of specific endotoxin-induced inflammatory responses, with potential implications for the therapy of subsequent severe inflammation.
doi:10.1038/sj.bjp.0704618
PMCID: PMC1573284  PMID: 11934806
Acute respiratory distress syndrome; microvascular lung endothelium; lipopolysaccharide; lipoteichonic acid; CXC-chemokines; adhesion molecules; phospholipase A2; lipid conjugates; extracellular phospholipase inhibitor
9.  Comparison of endothelin B (ETB) receptors in rabbit isolated pulmonary artery and bronchus. 
British Journal of Pharmacology  1996;118(5):1209-1217.
1. To explore potential differences between endothelin (ET) receptors in airway versus vascular smooth muscle from the same species, the ETB receptors mediating contractions produced by ET-1, ET-3 and the selective ETB ligands, sarafotoxin S6c (S6c) and BQ-3020, in rabbit bronchus and pulmonary artery were investigated by use of peptide and non-peptide ET receptor antagonists. 2. In rabbit pulmonary artery SB 209670 (10 microM), a mixed ETA/ETB receptor antagonist, was a more potent antagonist of contractions produced by S6c (pKB = 7.7; n = 9; P < 0.05), than those elicited by ET-1 (pKB = 6.7; n = 6) or ET-3 (pKB = 6.7; n = 5). BQ-788 (10 microM), an ETB receptor antagonist, inhibited responses produced by ET-3 (pKB = 5.1; n = 8), BQ-3020 (pKB = 5.2; n = 4) or S6c (pKB = 6.2; n = 9; P < 0.05 compared to potency versus ET-3- or BQ-3020-induced contractions), but was without inhibitory effect on ET-1-induced contractions (n = 5). RES-701 (10 microM), another selective ETB receptor antagonist, was without effect on contractions produced by S6c (n = 4) or ET-1 (n = 4), and potentiated ET-3- (n = 5) or BQ-3020-induced responses (n = 4). 3. The combination of BQ-788 (10 microM) and BQ-123 (10 microM), an ETA-selective receptor antagonist, antagonized contractions produced by lower concentrations of ET-1 (1 and 3 nM) in rabbit pulmonary artery, but was without effect on responses elicited by higher concentrations of ET-1 (n = 5). The combination of RES-701 (10 microM) and BQ-123 (10 microM) potentiated responses elicited by ET-1, producing a 3.7 fold shift to the left in the agonist concentration-response curve (n = 5). 4. In rabbit bronchus SB 209670 (3 microM) had similar potency for antagonism of contractions produced by ET-1 (pKB = 6.3; n = 6), ET-3 (pKB = 6.5; n = 6) or S6c (pKB = 6.1; n = 8). BQ-788 (3 microM) was without effect on responses elicited by ET-1, ET-3 or S6c (n = 6) but antagonized BQ-3020-induced contractions (pKB = 6.4; n = 4). RES-701 (3 microM) was without effect on contractions produced by S6c (n = 6) or BQ-3020 (n = 4), and potentiated rather than antagonized ET-1- or ET-3-induced responses (n = 6), reflected by a significant (about 6 fold) shift to the left in ET-1 or ET-3 concentration-response curves. The combination of BQ-788 (3 microM) and BQ-123 (3 microM) was without effect on contractions produced by ET-1 in rabbit bronchus (n = 6). The combination of RES-701 (3 microM) and BQ-123 (3 microM) potentiated responses elicited by ET-1, producing a 5.2 fold shift to the left in the agonist concentration-response curve (n = 5). 5. BQ-123 (3 or 10 microM), an ETA-selective receptor antagonist, was without effect on ET-1, ET-3 or S6c concentration-response curves (n = 3-6) in rabbit pulmonary artery or rabbit bronchus. 6. These data indicate that contractions induced by ET-1, ET-3, S6c and BQ-3020 in rabbit pulmonary artery or rabbit bronchus appear to be mediated predominantly via stimulation of ETB receptors. However, the qualitative and quantitative differences in the relative profiles of the various structurally diverse peptide and non-peptide antagonists examined suggests that responses produced by the ET ligands may not be mediated by a homogeneous ETB receptor population. In addition, the results suggest that differences exist in the ETB receptors mediating contraction in pulmonary vascular versus airway tissues in the same species. These receptors are not very sensitive to the standard ETB receptor antagonists, BQ-788 and RES-701. Furthermore, the results also provide further evidence that the potencies of ET receptor antagonists depend upon the ET agonist.
PMCID: PMC1909594  PMID: 8818345
10.  Pharmacological evidence for the presence of three distinct functional endothelin receptor subtypes in the rabbit lateral saphenous vein. 
British Journal of Pharmacology  1995;114(8):1529-1540.
1. Contraction of the rabbit isolated saphenous vein is mediated by a heterogeneous endothelin (ET) receptor population. This study has characterized these receptor subtypes by use of several pharmacologically distinct ET receptor agonists and antagonists. 2. ET-1, ET-3, sarafotoxin S6c (STXc) and [Ala3,11]ET-1 produced biphasic, concentration-dependent contractions of the saphenous vein, responses which were best fitted by a two-site model comprised of a high (pM) and a low (nM) affinity site. In contrast, IRL 1620 only recognized one of these sites. ET(16-21) was devoid of contractile activity. ET-1, ET-3 and STXc were equipotent at the high affinity site (pD2s of 12.0 +/- 0.2, 12.2 +/- 0.2 and 12.3 +/- 0.3) indicating that this site had the characteristics of an ETB receptor. In contrast, the low affinity site had the functional characteristics of an ETc receptor since the pD2s for ET-3 (10.2 +/- 0.3) and STXc (10.6 +/- 0.3) were significantly greater than that for ET-1 (9.1 +/- 0.1). These contractile responses were insensitive to BQ-123, confirming that ETA receptors were not involved in mediating this effect. 3. SB 209670 differentially antagonized the high affinity phases of the isopeptide concentration-response curves in a fashion dependent on the competing agonist: relative to the KB obtained against STXc (0.15 nM). SB 209670 was 10 fold less potent when ET-1 was used as the competing agonist. This differential effect was not evident at the low affinity site (KB = 38 nM). SB 209670 produced parallel, concentration-dependent rightward shifts in the concentration-response curve to STXc Ro 47-0203 was approximately 1 to 2 orders of magnitude less potent than SB 209670 at inhibiting the high affinity component of the concentration-response curve to STXc, whereas BQ-788 and Ro 46-2005 were approximately 3 orders of magnitude less potent than SB 209670. In addition to RES-701 and BQ-123, the high affinity site was insensitive to PD 142893 suggesting that it may represent an ETB2 receptor. Ro 47-0203 and SB 209670 were equipotent at inhibiting the low affinity component of the STXc concentration-response curve. Although Ro 46-2005, BQ-788, PD 142893 and RES-701 produced significant antagonism at the low affinity site, they were at least ten fold less potent than SB 209670.(ABSTRACT TRUNCATED AT 400 WORDS)
PMCID: PMC1510370  PMID: 7599920
11.  Purification and immunological characterization of a major low-molecular-weight lipoprotein from Borrelia burgdorferi. 
Infection and Immunity  1992;60(12):4995-5003.
Borrelia burgdorferi resembles gram-negative bacteria in having both cellular and outer membranes. We previously showed that a lipopolysaccharide (LPS)-like material could be extracted from B. burgdorferi with phenol-chloroform-petroleum ether (PCP). The PCP extract of B. burgdorferi exhibited biological activity in several in vitro assays (e.g., mitogenicity, pyrogenicity, and cytokine release). These activities suggested the presence of endotoxin. The PCP extract of B. burgdorferi, however, also contained a small amount of protein. Preliminary studies showed that monoclonal antibody prepared against this protein inhibited the mitogenic activity of the PCP extract toward murine spleen cells. The current study was therefore undertaken to characterize this protein and to establish methods for its separation from the LPS. The PCP-extracted protein consisted of a single, low-molecular-weight lipoprotein (apparent M(r), 10,000 by sodium dodecyl sulfate-polyacrylamide gel electrophoresis) (SDS-PAGE). By protein analysis, it accounted for 2% of the dry weight of defatted cells, thus making it a major constituent of the spirochete. It was purified from the LPS by initial extraction into 10% Triton X-100 followed by immunoaffinity chromatography in the presence of detergent. On removal of the LPS, the purified lipoprotein formed aggregates stable to SDS-PAGE which were detectable on Western blots (immunoblots) probed with either the monoclonal antibody or polyclonal antiserum. From a plot of the aggregate molecular weight versus aggregate size, a monomer molecular weight of 7,500 was obtained. Indirect immunofluorescence with the monoclonal antibody showed that the lipoprotein was exposed at the surface of the spirochete in only a small percentage of cells. The lipoprotein was present in several strains of B. burgdorferi but absent in other Borrelia spp., treponemes, and gram-negative human pathogens, indicating species specificity.
Images
PMCID: PMC258268  PMID: 1452330
13.  Smoking and cotton dust effects in cotton textile workers: an analysis of the shape of the maximum expiratory flow volume curve. 
Cotton textile workers have an increased prevalence of both obstructive and restrictive lung function patterns when compared to control subjects. Similar abnormal lung function patterns may occur with other respiratory diseases, notably those associated with cigarette smoking. The shape of the maximum expiratory flow volume (MEFV) curve has been used to characterize patterns of lung function abnormality. We defined a new functional parameter (angle beta) related to the shape of the MEFV curve in order better to characterize the respiratory effects of cotton dust exposure. In this study, 477 cotton textile workers, both current smokers and never smokers 45 years and older, were compared to 932 similarly aged control subjects from three communities: Lebanon and Ansonia, CT, and Winnsboro, SC. Smokers, regardless of their occupational exposure of sex, have smaller values of beta than do nonsmokers. Cotton textile workers who have more abnormal lung function than do controls, cannot be distinguished from controls by beta. We suggest that such functional differences between cotton and smoking effects may reflect injury to different portions of the bronchial tree.
PMCID: PMC1474372  PMID: 3709477
14.  Skin reactivity of unsensitized monkeys upon challenge with staphylococcal enterotoxin B: a new approach for investigating the site of toxin action. 
Infection and Immunity  1985;50(3):869-876.
The correlation between skin tests and emetic responses in unsensitized monkeys was used to elucidate the cellular site of action of staphylococcal enterotoxin B (SEB). Evidence is presented that SEB administered intradermally provoked immediate-type skin reactions associated with mild degranulation of cutaneous mast cells. The cytoplasma showed signs of synthetic and metabolic activity, with formation of vesicles and increased prominence of mitochondria. Carboxymethylation of histidine residues of SEB altered the molecule (cSEB) from more alkaline components to more acidic species with increased microheterogeneity. This modification caused a loss in toxicity and completely abrogated the skin-sensitizing activity without changing the immunological specificity. cSEB, however, could compete with SEB for binding sites on the target cell surface. Previously, compound 48/80-treated skin sites behaved refractively to challenge with SEB, indicating that mediators from cutaneous mast cells are required for SEB-induced skin reactions. Skin reactions as well as emetic responses challenged with SEB were completely inhibited by H2 receptor antagonists and calcium channel blockers but not by H1 antihistamine or competitive antagonists of serotonin. This new approach provides a model for investigating the mechanisms of SEB action.
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PMCID: PMC261160  PMID: 2866161
15.  Role for different cell proteinases in cancer invasion and cytolysis. 
British Journal of Cancer  1985;52(2):223-232.
The crucial role of non-plasminogen dependent serine proteinases is tissue invasive and cytolytic functions of Walker 256 cancer cells has been documented using a rat urinary bladder invasion and a 125I-labelled fibroblast cytolysis assay. The invasive capacity of these cancer cells was abrogated by non toxic concentrations of the serine proteinase inhibitors, diisopropylfluorophosphate and phenylmethylsulfonylfluoride, but not by metallo or cysteine proteinase inhibitors. Although tumour cell collagenase activity and plasminogen activator were demonstrated, these proteolytic enzymes were not essential in these in vitro assays. These results suggest that different categories of proteinases play specific roles in the complicated process of cancer invasion.
PMCID: PMC1977119  PMID: 2992566
16.  Direct skin test in highly sensitized guinea pigs for rapid and sensitive determination of staphylococcal enterotoxin B. 
The direct skin test in highly sensitized guinea pigs was developed as a rapid and extremely sensitive assay for detection of staphylococcal enterotoxin B (SEB) in foods. This report details the experimental conditions required to elicit optimal sensitization of guinea pigs to SEB. An intense and persistent immunoglobulin E (IgE) anti-SEB response was established in strain 13 guinea pigs pretreated with cyclophosphamide followed by four sensitizing doses of 10 micrograms of SEB 1 month apart. The conditions, however, optimal for eliciting IgE responses led to a sustained failure to produce antibody of the IgG1 subclass. With the use of highly sensitized guinea pigs, one can achieve a sensitivity ranging from 0.1 to 1.0 pg of purified SEB by the direct skin test for at least 7 months after the last challenge. For analysis of SEB in food extracts, the entire assay can be accomplished within 20 min with a sensitivity of 10 to 100 pg SEB per ml of prepared food samples, and the recovery of enterotoxin from spiked food products ranged between 75 and 89% of the amount added.
PMCID: PMC239575  PMID: 6660875
18.  Left ventricular apical thin point. 
British Heart Journal  1977;39(7):806-809.
The wall thickness of the apex of the left ventricle has been measured at its thinnest point in 60 adult hearts at necropsy. This measured 2 mm or less in 97% of them and 1 mm or less in 67%.
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PMCID: PMC483320  PMID: 884031
19.  The consultant's job 
British Medical Journal  1969;4(5682):563.
PMCID: PMC1630327
21.  Discouraging Smoking 
British Medical Journal  1962;1(5282):942.
PMCID: PMC1957519
22.  Any Complaints? 
British Medical Journal  1953;2(4845):1104.
PMCID: PMC2030083

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