About this Journal Submit a Manuscript Table of Contents
Veterinary Medicine International
Volume 2012 (2012), Article ID 172072, 8 pages
http://dx.doi.org/10.1155/2012/172072
Research Article

Single Intramammary Infusion of Recombinant Bovine Interleukin-8 at Dry-Off Induces the Prolonged Secretion of Leukocyte Elastase, Inflammatory Lactoferrin-Derived Peptides, and Interleukin-8 in Dairy Cows

1Dairy Hygiene Research Division, Hokkaido Research Station, National Institute of Animal Health (NIAH), National Agriculture and Food Research Organization (NARO), 4 Hitsujigaoka, Sapporo 062-0045, Japan
2Intellectual Property and Technology Management Section, NIAH, NARO, 3-1-1 Kannnondai, Tsukuba 305-0856, Japan
3Pathology and Pathophysiology Research Division, NIAH, NARO, 3-1-1 Kannnondai, Tsukuba 305-0856, Japan
4Laboratory of Biochemistry, Department of Biomedical Sciences, Graduate School of Veterinary Medicine, Hokkaido University, Sapporo 060-0818, Japan

Received 11 April 2012; Accepted 25 June 2012

Academic Editor: Jyoji Yamate

Copyright © 2012 Atsushi Watanabe et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Linked References

  1. B. Moser, M. Wolf, A. Walz, and P. Loetscher, “Chemokines: multiple levels of leukocyte migration control,” Trends in Immunology, vol. 25, no. 2, pp. 75–84, 2004. View at Publisher · View at Google Scholar · View at Scopus
  2. M. Baggiolini, B. Dewald, and B. Moser, “Interleukin-8 and related chemotactic cytokines—CXC and CC chemokines,” Advances in Immunology, vol. 55, pp. 97–179, 1994. View at Scopus
  3. K. Kimura, J. P. Goff, M. E. Kehrli, and T. A. Reinhardt, “Decreased neutrophil function as a cause of retained placenta in dairy cattle,” Journal of Dairy Science, vol. 85, no. 3, pp. 544–550, 2002. View at Scopus
  4. J. L. Caswell, D. M. Middleton, and J. R. Gordon, “The importance of interleukin-8 as a neutrophil chemoattractant in the lungs of cattle with pneumonic pasteurellosis,” Canadian Journal of Veterinary Research, vol. 65, no. 4, pp. 229–232, 2001. View at Scopus
  5. C. Riollet, P. Rainard, and B. Poutrel, “Cells and cytokines in inflammatory secretions of bovine mammary gland,” Advances in Experimental Medicine and Biology, vol. 480, pp. 247–258, 2000. View at Scopus
  6. D. D. Bannerman, M. J. Paape, J. W. Lee, X. Zhao, J. C. Hope, and P. Rainard, “Escherichia coli and Staphylococcus aureus elicit differential innate immune responses following intramammary infection,” Clinical and Diagnostic Laboratory Immunology, vol. 11, no. 3, pp. 463–472, 2004. View at Publisher · View at Google Scholar · View at Scopus
  7. D. D. Bannerman, M. J. Paape, J. P. Goff, K. Kimura, J. D. Lippolis, and J. C. Hope, “Innate immune response to intramammary infection with Serratia marcescens and Streptococcus uberis,” Veterinary Research, vol. 35, no. 6, pp. 681–700, 2004. View at Publisher · View at Google Scholar · View at Scopus
  8. D. D. Bannerman, A. Chockalingam, M. J. Paape, and J. C. Hope, “The bovine innate immune response during experimentally-induced Pseudomonas aeruginosa mastitis,” Veterinary Immunology and Immunopathology, vol. 107, no. 3-4, pp. 201–215, 2005. View at Publisher · View at Google Scholar · View at Scopus
  9. A. C. W. Kauf, R. F. Rosenbusch, M. J. Paape, and D. D. Bannerman, “Innate immune response to intramammary Mycoplasma bovis infection,” Journal of Dairy Science, vol. 90, no. 7, pp. 3336–3348, 2007. View at Publisher · View at Google Scholar · View at Scopus
  10. P. Rainard, A. Fromageau, P. Cunha, and F. B. Gilbert, “Staphylococcus aureus lipoteichoic acid triggers inflammation in the lactating bovine mammary gland,” Veterinary Research, vol. 39, no. 5, article 52, 2008. View at Publisher · View at Google Scholar · View at Scopus
  11. H. Simojoki, T. Salomäki, S. Taponen, A. Iivanainen, and S. Pyörälä, “Innate immune response in experimentally induced bovine intramammary infection with Staphylococcus simulans and S. epidermidis,” Veterinary Research, vol. 42, no. 1, pp. 49–58, 2011. View at Publisher · View at Google Scholar · View at Scopus
  12. M. Paape, J. Mehrzad, X. Zhao, J. Detilleux, and C. Burvenich, “Defense of the bovine mammary gland by polymorphonuclear neutrophil leukocytes,” Journal of Mammary Gland Biology and Neoplasia, vol. 7, no. 2, pp. 109–121, 2002. View at Publisher · View at Google Scholar · View at Scopus
  13. C. Burvenich, V. Van Merris, J. Mehrzad, A. Diez-Fraile, and L. Duchateau, “Severity of E. coli mastitis is mainly determined by cow factors,” Veterinary Research, vol. 34, no. 5, pp. 521–564, 2003. View at Publisher · View at Google Scholar · View at Scopus
  14. G. B. Mitchell, B. N. Albright, and J. L. Caswell, “Effect of interleukin-8 and granulocyte colony-stimulating factor on priming and activation of bovine neutrophils,” Infection and Immunity, vol. 71, no. 4, pp. 1643–1649, 2003. View at Publisher · View at Google Scholar · View at Scopus
  15. M. R. Barber and T. J. Yang, “Chemotactic activities in nonmastitic and mastitic mammary secretions: presence of interleukin-8 in mastitic but not nonmastitic secretions,” Clinical and Diagnostic Laboratory Immunology, vol. 5, no. 1, pp. 82–86, 1998. View at Scopus
  16. J. L. Caswell, D. M. Middleton, and J. R. Gordon, “Production and functional characterization of recombinant bovine interleukin-8 as a specific neutrophil activator and chemoattractant,” Veterinary Immunology and Immunopathology, vol. 67, no. 4, pp. 327–340, 1999. View at Publisher · View at Google Scholar · View at Scopus
  17. K. N. Galvão, G. M. Pighetti, S. H. Cheong, D. V. Nydam, and R. O. Gilbert, “Association between interleukin-8 receptor-α (CXCR1) polymorphism and disease incidence, production, reproduction, and survival in Holstein cows,” Journal of Dairy Science, vol. 94, no. 4, pp. 2083–2091, 2011. View at Publisher · View at Google Scholar · View at Scopus
  18. M. G. H. Stevens, L. J. Peelman, B. De Spiegeleer et al., “Differential gene expression of the toll-like receptor-4 cascade and neutrophil function in early- and mid-lactating dairy cows,” Journal of Dairy Science, vol. 94, no. 3, pp. 1277–1288, 2011. View at Publisher · View at Google Scholar · View at Scopus
  19. R. J. Harmon and F. H. S. Newbould, “Neutrophil leukocytes as a source of lactoferrin in bovine milk,” American Journal of Veterinary Research, vol. 41, no. 10, pp. 1603–1606, 1980.
  20. L. Brandolini, R. Bertini, C. Bizzarri et al., “IL-1β primes IL-8-activated human neutrophils for elastase release, phospholipase D activity, and calcium flux,” Journal of Leukocyte Biology, vol. 59, no. 3, pp. 427–434, 1996. View at Scopus
  21. B. Korkmaz, T. Moreau, and F. Gauthier, “Neutrophil elastase, proteinase 3 and cathepsin G: physicochemical properties, activity and physiopathological functions,” Biochimie, vol. 90, no. 2, pp. 227–242, 2008. View at Publisher · View at Google Scholar · View at Scopus
  22. Y. Komine, T. Kuroishi, J. Kobayashi et al., “Inflammatory effect of cleaved bovine lactoferrin by elastase on staphylococcal mastitis,” Journal of Veterinary Medical Science, vol. 68, no. 7, pp. 715–723, 2006. View at Publisher · View at Google Scholar · View at Scopus
  23. N. Boudjellab, H. S. Chan-Tang, X. Li, and X. Zhao, “Interleukin 8 response by bovine mammary epithelial cells to lipopolysaccharide stimulation,” American Journal of Veterinary Research, vol. 59, no. 12, pp. 1563–1567, 1998. View at Scopus
  24. M. R. Barber, A. G. Pantschenko, L. S. Hinckley, and T. J. Yang, “Inducible and constitutive in vitro neutrophil chemokine expression by mammary epithelial and myoepithelial cells,” Clinical and Diagnostic Laboratory Immunology, vol. 6, no. 6, pp. 791–798, 1999. View at Scopus
  25. A. Watanabe, Y. Yagi, H. Shiono, Y. Yokomizo, and S. Inumaru, “Effects of intramammary infusions of interleukin-8 on milk protein composition and induction of acute-phase protein in cows during mammary involution,” Canadian Journal of Veterinary Research, vol. 72, no. 3, pp. 291–296, 2008. View at Scopus
  26. J. Hirota, S. Shimizu, A. Watanabe et al., “Establishment of a quantitative bovine CXCL8 sandwich ELISA with newly developed monoclonal antibodies,” European Cytokine Network, vol. 22, no. 1, pp. 73–80, 2011. View at Publisher · View at Google Scholar · View at Scopus
  27. M. M. Bradford, “A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein dye binding,” Analytical Biochemistry, vol. 72, no. 1-2, pp. 248–254, 1976. View at Scopus
  28. W. N. Fishbein, “Quantitative densitometry of 1-50 μg protein in acrylamide gel slabs with coomassie blue,” Analytical Biochemistry, vol. 46, no. 2, pp. 388–401, 1972. View at Scopus
  29. K. L. Smith, J. H. Harrison, D. D. Hancock, D. A. Todhunter, and H. R. Conrad, “Effect of vitamin E and selenium supplementation on incidence of clinical mastitis and duration of clinical symptoms,” Journal of Dairy Science, vol. 67, no. 6, pp. 1293–1300, 1984. View at Scopus
  30. V. D. Bhatt, M. S. Patel, C. G. Joshi, and A. Kunjadia, “Identification and antibiogram of microbes associated with bovine mastitis,” Animal Biotechnology, vol. 22, no. 3, pp. 163–169, 2011. View at Publisher · View at Google Scholar · View at Scopus
  31. National Mastitis Council: Subcommittee on Screening Tests, “Direct microscopic somatic cell count in milk,” Journal of Milk and Food Technology, vol. 31, pp. 350–354, 1968.
  32. R. H. Miller, M. J. Paape, R. R. Peters, and M. D. Young, “Total and differential somatic cell counts and N-acetyl-beta-D-glucosaminidase activity in mammary secretions during dry period,” Journal of Dairy Science, vol. 73, no. 7, pp. 1751–1755, 1990. View at Scopus
  33. L. Bouchard, S. Blais, C. Desrosiers, X. Zhao, and P. Lacasse, “Nitric oxide production during endotoxin-induced mastitis in the cow,” Journal of Dairy Science, vol. 82, no. 12, pp. 2574–2581, 1999. View at Scopus
  34. A. Watanabe, I. Uchida, K. Nakata, Y. Fujimoto, and S. Oikawa, “Molecular cloning of bovine (Bos taurus) cDNA encoding a 94-kDa glucose-regulated protein and developmental changes in its mRNA and protein content in the mammary gland,” Comparative Biochemistry and Physiology B, vol. 130, no. 4, pp. 547–557, 2001. View at Publisher · View at Google Scholar · View at Scopus
  35. B. J. Nonnecke and K. L. Smith, “Biochemical and antibacterial properties of bovine mammary secretion during mammary involution and at parturition,” Journal of Dairy Science, vol. 67, no. 12, pp. 2863–2872, 1984. View at Scopus
  36. W. L. Hurley, “Mammary gland function during involution,” Journal of Dairy Science, vol. 72, no. 6, pp. 1637–1646, 1989. View at Scopus
  37. S. Kandasamy, B. B. Green, A. L. Benjamin, and D. E. Kerr, “Between-cow variation in dermal fibroblast response to lipopolysaccharide reflected in resolution of inflammation during Escherichia coli mastitis,” Journal of Dairy Science, vol. 94, no. 12, pp. 5963–5975, 2011. View at Publisher · View at Google Scholar · View at Scopus
  38. M. H. Weng, T. C. Yu, S. E. Chen et al., “Regional accretion of gelatinase B in mammary gland during gradual and acute involution of dairy animals,” Journal of Dairy Research, vol. 75, no. 2, pp. 202–210, 2008. View at Publisher · View at Google Scholar · View at Scopus
  39. T.-C. Yu, C.-J. Chang, C.-H. Ho et al., “Modifications of the defense and remodeling functionalities of bovine neutrophils inside the mammary gland of milk stasis cows received a commercial dry-cow treatment,” Veterinary Immunology and Immunopathology, vol. 144, no. 3-4, pp. 210–219, 2011. View at Publisher · View at Google Scholar · View at Scopus
  40. F. L. Schanbacher, R. E. Goodman, and R. S. Talhouk, “Bovine mammary lactoferrin: implications from messenger ribonucleic acid (mRNA) sequence and regulation contrary to other milk proteins,” Journal of Dairy Science, vol. 76, no. 12, pp. 3812–3831, 1993. View at Scopus
  41. D. Patel, R. A. Almeida, J. R. Dunlap, and S. P. Oliver, “Bovine lactoferrin serves as a molecular bridge for internalization of Streptococcus uberis into bovine mammary epithelial cells,” Veterinary Microbiology, vol. 137, no. 3-4, pp. 297–301, 2009. View at Publisher · View at Google Scholar · View at Scopus
  42. P. Hyvönen, S. Käyhkö, S. Taponen, A. Von Wright, and S. Pyörälä, “Effect of bovine lactoferrin on the internalization of coagulase-negative staphylococci into bovine mammary epithelial cells under in-vitro conditions,” Journal of Dairy Research, vol. 76, no. 2, pp. 144–151, 2009. View at Publisher · View at Google Scholar · View at Scopus
  43. H. W. Barkema, Y. H. Schukken, and R. N. Zadoks, “Invited review: the role of cow, pathogen, and treatment regimen in the therapeutic success of bovine Staphylococcus aureus mastitis,” Journal of Dairy Science, vol. 89, no. 6, pp. 1877–1895, 2006. View at Scopus
  44. P. Gruet, P. Maincent, X. Berthelot, and V. Kaltsatos, “Bovine mastitis and intramammary drug delivery: review and perspectives,” Advanced Drug Delivery Reviews, vol. 50, no. 3, pp. 245–259, 2001. View at Publisher · View at Google Scholar · View at Scopus
  45. P. M. Sears and K. K. McCarthy, “Management and treatment of staphylococcal mastitis,” Veterinary Clinics of North America, vol. 19, no. 1, pp. 171–185, 2003. View at Publisher · View at Google Scholar · View at Scopus
  46. L. Sutra and B. Poutrel, “Virulence factors involved in the pathogenesis of bovine intramammary infections due to Staphylococcus aureus,” Journal of Medical Microbiology, vol. 40, no. 2, pp. 79–89, 1994. View at Scopus
  47. S. Taponen and S. Pyörälä, “Coagulase-negative staphylococci as cause of bovine mastitis-Not so different from Staphylococcus aureus?” Veterinary Microbiology, vol. 134, no. 1-2, pp. 29–36, 2009. View at Publisher · View at Google Scholar · View at Scopus
  48. A. M. Alluwaimi, “The cytokines of bovine mammary gland: prospects for diagnosis and therapy,” Research in Veterinary Science, vol. 77, no. 3, pp. 211–222, 2004. View at Publisher · View at Google Scholar · View at Scopus