Open Access
Vet. Res.
Volume 40, Number 6, November-December 2009
Number of page(s) 14
Published online 29 July 2009
How to cite this article Vet. Res. (2009) 40:60
References of  Vet. Res. (2009) 40:60
  1. Anderson C., Potter A.A., Gerlach G.F., Isolation and molecular characterization of spontaneously occurring cytolysin-negative mutants of Actinobacillus pleuropneumoniae serotype 7, Infect. Immun. (1991) 59:4110–4116 [PubMed].
  2. Apweiler R., Hermjakob H., Sharon N., On the frequency of protein glycosylation, as deduced from analysis of the SWISS-PROT database, Biochim. Biophys. Acta (1999) 1473:4–8 [PubMed].
  3. Bals R., Hiemstra P.S., Innate immunity in the lung: how epithelial cells fight against respiratory pathogens, Eur. Respir. J. (2004) 23:327–333 [CrossRef] [PubMed].
  4. Baltes N., Tonpitak W., Gerlach G.F., Hennig-Pauka I., Hoffmann-Moujahid A., Ganter M., Rothkotter H.J., Actinobacillus pleuropneumoniae iron transport and urease activity: effects on bacterial virulence and host immune response, Infect. Immun. (2001) 69:472–478 [CrossRef] [PubMed].
  5. Bartlett J.A., Fischer A.J., McCray P.B. Jr, Innate immune functions of the airway epithelium, Contrib. Microbiol. (2008) 15:147–163 [PubMed].
  6. Buettner F.F., Bendalla I.M., Bosse J.T., Meens J., Nash J.H., Hartig E., et al., Analysis of the Actinobacillus pleuropneumoniae HlyX (FNR) regulon and identification of iron-regulated protein B as an essential virulence factor, Proteomics (2009) 9:2383–2398 [CrossRef] [PubMed].
  7. Chiers K., Donne E., Van Overbeke I., Ducatelle R., Haesebrouck F., Evaluation of serology, bacteriological isolation and polymerase chain reaction for the detection of pigs carrying Actinobacillus pleuropneumoniae in the upper respiratory tract after experimental infection, Vet. Microbiol. (2002) 88:385–392 [CrossRef] [PubMed].
  8. Choi-Miura N.H., Takahashi K., Yoda M., Saito K., Hori M., Ozaki H., et al., The novel acute phase protein, IHRP, inhibits actin polymerization and phagocytosis of polymorphonuclear cells, Inflamm. Res. (2000) 49:305–310 [CrossRef] [PubMed].
  9. Cooley J., McDonald B., Accurso F.J., Crouch E.C., Remold-O'Donnell E., Patterns of neutrophil serine protease-dependent cleavage of surfactant protein D in inflammatory lung disease, J. Leukoc. Biol. (2008) 83:946–955 [CrossRef] [PubMed].
  10. Dom P., Haesebrouck F., Kamp E.M., Smits M.A., Influence of Actinobacillus pleuropneumoniae serotype 2 and its cytolysins on porcine neutrophil chemiluminescence, Infect. Immun. (1992) 60:4328–4334 [PubMed].
  11. Done S.H., Environmental factors affecting the severity of pneumonia in pigs, Vet. Rec. (1991) 128:582–586 [PubMed].
  12. Dziegielewska K.M., Andersen N.A., Saunders N.R., Modification of macrophage response to lipopolysaccharide by fetuin, Immunol. Lett. (1998) 60:31–35 [CrossRef] [PubMed].
  13. Fietta A., Bardoni A., Salvini R., Passadore I., Morosini M., Cavagna L., et al., Analysis of bronchoalveolar lavage fluid proteome from systemic sclerosis patients with or without functional, clinical and radiological signs of lung fibrosis, Arthritis Res. Ther. (2006) 8:R160 [CrossRef] [PubMed].
  14. Fournier T., Medjoubi N.N., Porquet D., Alpha-1-acid glycoprotein, Biochim. Biophys. Acta (2000) 1482:157–171 [PubMed].
  15. Gabay C., Kushner I., Acute-phase proteins and other systemic responses to inflammation, N. Engl. J. Med. (1999) 340:448–454 [CrossRef] [PubMed].
  16. Haagsman H.P., Hogenkamp A., van Eijk M., Veldhuizen E.J., Surfactant collectins and innate immunity, Neonatology (2008) 93:288–294 [CrossRef] [PubMed].
  17. Hannan P.C., Bhogal B.S., Fish J.P., Tylosin tartrate and tiamutilin effects on experimental piglet pneumonia induced with pneumonic pig lung homogenate containing mycoplasmas, bacteria and viruses, Res. Vet. Sci. (1982) 33:76–88 [PubMed].
  18. Heegaard P.M., Klausen J., Nielsen J.P., Gonzalez-Ramon N., Pineiro M., Lampreave F., Alava M.A., The porcine acute phase response to infection with Actinobacillus pleuropneumoniae. Haptoglobin, C-reactive protein, major acute phase protein and serum amyloid A protein are sensitive indicators of infection, Comp. Biochem. Physiol. B Biochem. Mol. Biol. (1998) 119:365–373 [CrossRef] [PubMed].
  19. Hege R., Zimmermann W., Scheidegger R., Stark K.D., Incidence of reinfections with Mycoplasma hyopneumoniae and Actinobacillus pleuropneumoniae in pig farms located in respiratorydisease-free regions of Switzerland–identification and quantification of risk factors, Acta Vet. Scand. (2002) 43:145–156 [CrossRef] [PubMed].
  20. Hennig-Pauka I., Jacobsen I., Blecha F., Waldmann K.H., Gerlach G.F., Differential proteomic analysis reveals increased cathelicidin expression in porcine bronchoalveolar lavage fluid after an Actinobacillus pleuropneumoniae infection, Vet. Res. (2006) 37:75–87 [CrossRef] [PubMed] [EDP Sciences].
  21. Hennig-Pauka I., Bremerich S., Nienhoff H., Schroder C., Verspohl J., Strutzberg-Minder K., et al., Respiratory disease markers in porcine bronchoalveolar lavage fluid, J. Vet. Med. A Physiol. Pathol. Clin. Med. (2007) 54:434–440 [PubMed].
  22. Hoeltig D., Hennig-Pauka I., Thies K., Rehm T., Beyerbach M., Strutzberg-Minder K., et al., A novel clinical scoring system reveals the role of innate immunity and breed in resistance to Actinobacillus pleuropneumoniae infection, BMC Vet. Res. (2009) 5:14 [CrossRef] [PubMed].
  23. Horter D.C., Pogranichniy R.M., Chang C.C., Evans R.B., Yoon K.J., Zimmerman J.J., Characterization of the carrier state in porcine reproductive and respiratory syndrome virus infection, Vet. Microbiol. (2002) 86:213–228 [CrossRef] [PubMed].
  24. Jacobsen I., Gerstenberger J., Gruber A.D., Bossé J.T., Langford P.R., Hennig-Pauka I., et al., Deletion of the ferric uptake regulator Fur impairs the in vitro growth and virulence of Actinobacillus pleuropneumoniae, Infect. Immun. (2005) 73:3740–3744 [CrossRef] [PubMed].
  25. Janciauskiene S., Conformational properties of serine proteinase inhibitors (serpins) confer multiple pathophysiological roles, Biochim. Biophys. Acta (2001) 1535:221–235 [PubMed].
  26. Julenius K., Molgaard A., Gupta R., Brunak S., Prediction, conservation analysis, and structural characterization of mammalian mucin-type O-glycosylation sites, Glycobiology (2005) 15:153–164 [CrossRef] [PubMed].
  27. Kaysen G.A., Dubin J.A., Muller H.G., Mitch W.E., Levin N.W., Levels of alpha1 acid glycoprotein and ceruloplasmin predict future albumin levels in hemodialysis patients, Kidney Int. (2001) 60:2360–2366 [CrossRef] [PubMed].
  28. Lee T.M., Lin M.S., Chang N.C., Usefulness of C-reactive protein and interleukin-6 as predictors of outcomes in patients with chronic obstructive pulmonary disease receiving pravastatin, Am. J. Cardiol. (2008) 101:530–535 [CrossRef] [PubMed].
  29. Lee W.C., Lee K.H., Applications of affinity chromatography in proteomics, Anal. Biochem. (2004) 324:1–10 [CrossRef] [PubMed].
  30. Maes D., Segales J., Meyns T., Sibila M., Pieters M., Haesebrouck F., Control of Mycoplasma hyopneumoniae infections in pigs, Vet. Microbiol. (2008) 126:297–309 [CrossRef] [PubMed].
  31. Makris G., Wright J.D., Ingham E., Holland K.T., The hyaluronate lyase of Staphylococcus aureus–a virulence factor?, Microbiology (2004) 150:2005–2013 [CrossRef] [PubMed].
  32. Martinez Cordero E., Gonzalez M.M., Aguilar L.D., Orozco E.H., Hernandez Pando R., Alpha-1-acid glycoprotein, its local production and immunopathological participation in experimental pulmonary tuberculosis, Tuberculosis (Edinb.) (2008) 88:203–211 [CrossRef] [PubMed].
  33. Mellencamp M.A., Galina-Pantoja L., Gladney C.D., Torremorell M., Improving pig health through genomics: a view from the industry, Dev. Biol. (Basel) (2008) 132:35–41 [PubMed].
  34. Molloy M.P., Herbert B.R., Williams K.L., Gooley A.A., Extraction of Escherichia coli proteins with organic solvents prior to two-dimensional electrophoresis, Electrophoresis (1999) 20:701–704 [CrossRef] [PubMed].
  35. Nathani N., Perkins G.D., Tunnicliffe W., Murphy N., Manji M., Thickett D.R., Kerbs von Lungren 6 antigen is a marker of alveolar inflammation but not of infection in patients with acute respiratory distress syndrome, Crit. Care (2008) 12:R12 [CrossRef] [PubMed].
  36. Neumann E.J., Kliebenstein J.B., Johnson C.D., Mabry J.W., Bush E.J., Seitzinger A.H., et al., Assessment of the economic impact of porcine reproductive and respiratory syndrome on swine production in the United States, J. Am. Vet. Med. Assoc. (2005) 227:385–392 [CrossRef] [PubMed].
  37. Noel-Georis I., Bernard A., Falmagne P., Wattiez R., Database of bronchoalveolar lavage fluid proteins, J. Chromatogr. B Analyt. Technol. Biomed. Life Sci. (2002) 771:221–236 [CrossRef] [PubMed].
  38. Petersen H.H., Nielsen J.P., Heegaard P.M., Application of acute phase protein measurements in veterinary clinical chemistry, Vet. Res. (2004) 35:163–187 [CrossRef] [PubMed] [EDP Sciences].
  39. Rabilloud T., Silver staining of 2-D electrophoresis gels, Methods Mol. Biol. (1999) 112:297–305 [PubMed].
  40. Ramjeet M., Deslandes V., Goure J., Jacques M., Actinobacillus pleuropneumoniae vaccines: from bacterins to new insights into vaccination strategies, Anim. Health Res. Rev. (2008) 9:25–45 [PubMed].
  41. Raptis S.Z., Shapiro S.D., Simmons P.M., Cheng A.M., Pham C.T., Serine protease cathepsin G regulates adhesion-dependent neutrophil effector functions by modulating integrin clustering, Immunity (2005) 22:679–691 [CrossRef] [PubMed].
  42. Reading P.C., Morey L.S., Crouch E.C., Anders E.M., Collectin-mediated antiviral host defense of the lung: evidence from influenza virus infection of mice, J. Virol. (1997) 71:8204–8212 [PubMed].
  43. Shevchenko A., Wilm M., Vorm O., Mann M., Mass spectrometric sequencing of proteins silverstained polyacrylamide gels, Anal. Chem. (1996) 68:850–858 [CrossRef] [PubMed].
  44. Soerensen C.M., Holmskov U., Aalbaek B., Boye M., Heegaard P.M., Nielsen O.L., Pulmonary infections in swine induce altered porcine surfactant protein D expression and localization to dendritic cells in bronchial-associated lymphoid tissue, Immunology (2005) 115:526–535 [CrossRef] [PubMed].
  45. Treuheit M.J., Costello C.E., Halsall H.B., Analysis of the five glycosylation sites of human alpha 1-acid glycoprotein, Biochem. J. (1992) 283:105–112 [PubMed].
  46. Turner G.A., N-glycosylation of serum proteins in disease and its investigation using lectins, Clin. Chim. Acta (1992) 208:149–171 [CrossRef] [PubMed].
  47. Umstead T.M., Freeman W.M., Chinchilli V.M., Phelps D.S., Age-related changes in the expression and oxidation of bronchoalveolar lavage proteins in the rat, Am. J. Physiol. Lung Cell. Mol. Physiol. (2009) 296:L14–29 [CrossRef] [PubMed].
  48. Vaandrager A.B., van Golde L.M., Lung surfactant proteins A and D in innate immune defense, Biol. Neonate (2000) 77 (Suppl. 1):9–13 [CrossRef] [PubMed].
  49. Van Eijk M., van de Lest C.H., Batenburg J.J., Vaandrager A.B., Meschi J., Hartshorn K.L., et al., Porcine surfactant protein D is N-glycosylated in its carbohydrate recognition domain and is assembled into differently charged oligomers, Am. J. Respir. Cell Mol. Biol. (2002) 26:739–747 [PubMed].
  50. Wan J., Sun W., Li X., Ying W., Dai J., Kuai X., et al., Inflammation inhibitors were remarkably upregulated in plasma of severe acute respiratory syndrome patients at progressive phase, Proteomics (2006) 6:2886–2894 [CrossRef] [PubMed].
  51. Wang H., Zhang M., Bianchi M., Sherry B., Sama A., Tracey K.J., Fetuin (alpha2-HS-glycoprotein) opsonizes cationic macrophagedeactivating molecules, Proc. Natl. Acad. Sci. USA (1998) 95:14429–14434 [CrossRef] [PubMed].
  52. Wattiez R., Falmagne P., Proteomics of bronchoalveolar lavage fluid, J. Chromatogr. B Analyt. Technol. Biomed. Life Sci. (2005) 815:169–178 [CrossRef] [PubMed].
  53. Wu J., Kobayashi M., Sousa E.A., Liu W., Cai J., Goldman S.J., et al., Differential proteomic analysis of bronchoalveolar lavage fluid in asthmatics following segmental antigen challenge, Mol. Cell. Proteomics (2005) 4:1251–1264 [CrossRef] [PubMed].
  54. Yang F., Haile D.J., Berger F.G., Herbert D.C., Van Beveren E., Ghio A.J., Haptoglobin reduces lung injury associated with exposure to blood, Am. J. Physiol. Lung Cell. Mol. Physiol. (2003) 284:L402–L409 [PubMed].