Table of Contents Author Guidelines Submit a Manuscript
Mediators of Inflammation
Volume 2012, Article ID 157894, 9 pages
http://dx.doi.org/10.1155/2012/157894
Research Article

LPS Counter Regulates RNA Expression of Extracellular Proteases and Their Inhibitors in Murine Macrophages

1The Finsen Laboratory, Rigshospitalet, Copenhagen Biocenter 2200 Copenhagen, Denmark
2Biotech Research and Innovation Centre (BRIC), University of Copenhagen, 2200 Copenhagen, Denmark
3Department of Cellular and Molecular Medicine, Faculty of Health Sciences, University of Copenhagen, 2200, Copenhagen, Denmark
4Section for Metabolic Receptology and Enteroendocrinolgy, Novo Nordisk Foundation Center for Basic Metabolic Research, University of Copenhagen, 2200 Copenhagen, Denmark

Received 26 September 2011; Revised 5 December 2011; Accepted 21 December 2011

Academic Editor: Stefanie B. Flohé

Copyright © 2012 Andreas Hald 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. A. Parihar, T. D. Eubank, and A. I. Doseff, “Monocytes and macrophages regulate immunity through dynamic networks of survival and cell death,” Journal of Innate Immunity, vol. 2, no. 3, pp. 204–215, 2010. View at Publisher · View at Google Scholar · View at Scopus
  2. P. Libby, “Atherosclerosis: the new view,” Scientific American, vol. 286, no. 5, pp. 46–55, 2002. View at Google Scholar · View at Scopus
  3. R. A. Mukhtar, O. Nseyo, M. J. Campbell, and L. J. Esserman, “Tumor-associated macrophages in breast cancer as potential biomarkers for new treatments and diagnostics,” Expert Review of Molecular Diagnostics, vol. 11, no. 1, pp. 91–100, 2011. View at Publisher · View at Google Scholar · View at Scopus
  4. C. Nathan and A. Ding, “Nonresolving Inflammation,” Cell, vol. 140, no. 6, pp. 871–882, 2010. View at Publisher · View at Google Scholar · View at Scopus
  5. J. Larmann, T. Frenzel, A. Hahnenkamp et al., “In vivo fluorescence-mediated tomography for quantification of urokinase receptor-dependent leukocyte trafficking in inflammation,” Anesthesiology, vol. 113, no. 3, pp. 610–618, 2010. View at Publisher · View at Google Scholar · View at Scopus
  6. P. A. O'Connell, A. P. Surette, R. S. Liwski, P. Svenningsson, and D. M. Waisman, “S100A10 regulates plasminogen-dependent macrophage invasion,” Blood, vol. 116, no. 7, pp. 1136–1146, 2010. View at Publisher · View at Google Scholar · View at Scopus
  7. V. A. Ploplis, E. L. French, P. Carmeliet, D. Collen, and E. F. Plow, “Plasminogen deficiency differentially affects recruitment of inflammatory cell populations in mice,” Blood, vol. 91, no. 6, pp. 2005–2009, 1998. View at Google Scholar · View at Scopus
  8. T. A. Wynn and L. Barron, “Macrophages: master regulators of inflammation and fibrosis,” Seminars in Liver Disease, vol. 30, no. 3, pp. 245–257, 2010. View at Publisher · View at Google Scholar · View at Scopus
  9. Y. Gong, E. Hart, A. Shchurin, and J. Hoover-Plow, “Inflammatory macrophage migration requires MMP-9 activation by plasminogen in mice,” Journal of Clinical Investigation, vol. 118, no. 9, pp. 3012–3024, 2008. View at Publisher · View at Google Scholar · View at Scopus
  10. J. M. Shipley, R. L. Wesselschmidt, D. K. Kobayashi, T. J. Ley, and S. D. Shapiro, “Metalloelastase is required for macrophage-mediated proteolysis and matrix invasion in mice,” Proceedings of the National Academy of Sciences of the United States of America, vol. 93, no. 9, pp. 3942–3946, 1996. View at Publisher · View at Google Scholar · View at Scopus
  11. S. Akilesh, D. J. Shaffer, and D. Roopenian, “Customized molecular phenotyping by quantitative gene expression and pattern recognition analysis,” Genome Research, vol. 13, no. 7, pp. 1719–1727, 2003. View at Publisher · View at Google Scholar · View at Scopus
  12. J. Vandesompele, K. De Preter, F. Pattyn et al., “Accurate normalization of real-time quantitative RT-PCR data by geometric averaging of multiple internal control genes,” Genome biology, vol. 3, no. 7, RESEARCH0034, 2002. View at Google Scholar · View at Scopus
  13. M. W. Pfaffl, “A new mathematical model for relative quantification in real-time RT-PCR,” Nucleic acids research, vol. 29, no. 9, article e45, 2001. View at Google Scholar · View at Scopus
  14. S. A. Bustin, “Absolute quantification of mrna using real-time reverse transcription polymerase chain reaction assays,” Journal of Molecular Endocrinology, vol. 25, no. 2, pp. 169–193, 2000. View at Google Scholar · View at Scopus
  15. B. Reel, G. B. Sala-Newby, W.-C. Huang, and A. C. Newby, “Diverse patterns of cyclooxygenase-independent metalloproteinase gene regulation in human monocytes,” British Journal of Pharmacology, vol. 163, no. 8, pp. 1679–1690, 2011. View at Publisher · View at Google Scholar
  16. A. Bar-Or, R. K. Nuttall, M. Duddy et al., “Analyses of all matrix metalloproteinase members in leukocytes emphasize monocytes as major inflammatory mediators in multiple sclerosis,” Brain, vol. 126, no. 12, pp. 2738–2749, 2003. View at Publisher · View at Google Scholar · View at Scopus
  17. J. J. Gao, V. Diesl, T. Wittmann et al., “Bacterial LPS and CpG DNA differentially induce gene expression profiles in mouse macrophages,” Journal of Endotoxin Research, vol. 9, no. 4, pp. 237–243, 2003. View at Publisher · View at Google Scholar · View at Scopus
  18. A. Hyc, A. Osiecka-Iwan, J. Niderla-Bielinska, and S. Moskalewski, “Influence of LPS, TNF, TGF-β1 and IL-4 on the expression of MMPs, TIMPs and selected cytokines in rat synovial membranes incubated in vitro,” International Journal of Molecular Medicine, vol. 27, no. 1, pp. 127–137, 2011. View at Publisher · View at Google Scholar
  19. M. P. Vincenti, “The matrix metalloproteinase (MMP) and tissue inhibitor of metalloproteinase (TIMP) genes. Transcriptional and posttranscriptional regulation, signal transduction and cell-type-specific expression,” Methods in Molecular Biology, vol. 151, pp. 121–148, 2001. View at Google Scholar · View at Scopus
  20. R. M. B. Teles, R. B. Teles, T. P. Amadeu et al., “High matrix metalloproteinase production correlates with immune activation and leukocyte migration in leprosy reactional lesions,” Infection and Immunity, vol. 78, no. 3, pp. 1012–1021, 2010. View at Publisher · View at Google Scholar · View at Scopus
  21. I. Shima, S. Katsuda, Y. Ueda, N. Takahashi, and H. Sasaki, “Expression of matrix metalloproteinases in wound healing after glaucoma filtration surgery in rabbits,” Ophthalmic Research, vol. 39, no. 6, pp. 315–324, 2007. View at Publisher · View at Google Scholar · View at Scopus
  22. J. Pugin, M. C. Widmer, S. Kossodo, C. M. Liang, H. L. Preas, and A. F. Suffredini, “Human neutrophils secrete gelatinase B in vitro and in vivo in response to endotoxin and proinflammatory mediators,” American Journal of Respiratory Cell and Molecular Biology, vol. 20, no. 3, pp. 458–464, 1999. View at Google Scholar · View at Scopus
  23. T. Klein and R. Bischoff, “Physiology and pathophysiology of matrix metalloproteases,” Amino Acids, vol. 41, no. 2, pp. 271–290, 2011. View at Publisher · View at Google Scholar · View at Scopus
  24. A. C. Newby, “Metalloproteinase expression in monocytes and macrophages and its relationship to atherosclerotic plaque instability,” Arteriosclerosis, Thrombosis, and Vascular Biology, vol. 28, no. 12, pp. 2108–2114, 2008. View at Publisher · View at Google Scholar · View at Scopus
  25. U. Benbow and C. E. Brinckerhoff, “The AP-1 site and MMP gene regulation: what is all the fuss about?” Matrix Biology, vol. 15, no. 8-9, pp. 519–526, 1997. View at Publisher · View at Google Scholar · View at Scopus
  26. E. O. Costelloe, K. J. Stacey, T. M. Antalis, and D. A. Hume, “Regulation of the plasminogen activator inhibitor-2 (PAI-2) gene in murine macrophages. Demonstration of a novel pattern of responsiveness to bacterial endotoxin,” Journal of Leukocyte Biology, vol. 66, no. 1, pp. 172–182, 1999. View at Google Scholar · View at Scopus
  27. P. H. Hart, G. F. Vitti, D. R. Burgess, D. K. Singleton, and J. A. Hamilton, “Human monocytes can produce tissue-type plasminogen activator,” Journal of Experimental Medicine, vol. 169, no. 4, pp. 1509–1514, 1989. View at Google Scholar · View at Scopus
  28. A. Hald, B. Rønø, M. C. Melander, M. Ding, S. Holck, and L. R. Lund, “MMP9 is protective against lethal inflammatory mass lesions in the mouse colon,” DMM Disease Models and Mechanisms, vol. 4, no. 2, pp. 212–227, 2011. View at Publisher · View at Google Scholar
  29. N. Hattori, S. Mochizuki, K. Kishi et al., “MMP-13 plays a role in keratinocyte migration, angiogenesis, and contraction in mouse skin wound healing,” American Journal of Pathology, vol. 175, no. 2, pp. 533–546, 2009. View at Publisher · View at Google Scholar · View at Scopus
  30. S. Tanaka, T. Furukawa, and S. A. Plotkin, “Human cytomegalovirus stimulates host cell RNA synthesis,” Journal of Virology, vol. 15, no. 2, pp. 297–304, 1975. View at Google Scholar · View at Scopus