Table of Contents
International Journal of Molecular Imaging
Volume 2016, Article ID 5768312, 11 pages
http://dx.doi.org/10.1155/2016/5768312
Research Article

Understanding Lung Deposition of Alpha-1 Antitrypsin in Acute Experimental Mouse Lung Injury Model Using Fluorescence Microscopy

1Pharmacokinetics, Dynamics and Metabolism, Pfizer Inc., Andover, MA, USA
2Drug Safety R&D, Pfizer Inc., Andover, MA, USA
3Clinical R&D, Pfizer Inc., Cambridge, MA, USA
4Molecular Imaging Laboratory, Pfizer Inc., Andover, MA, USA
5Rare Disease RU, Pfizer Inc., Cambridge, MA, USA

Received 6 June 2016; Revised 26 September 2016; Accepted 26 October 2016

Academic Editor: Helmut Sinzinger

Copyright © 2016 Mengmeng Wang 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. M. Brantly, T. Nukiwa, and R. G. Crystal, “Molecular basis of alpha-1-antitrypsin deficiency,” The American Journal of Medicine, vol. 84, no. 6, pp. 13–31, 1988. View at Publisher · View at Google Scholar · View at Scopus
  2. Z. Li, S. Alam, J. Wang, C. S. Sandstrom, S. Janciauskiene, and R. Mahadeva, “Oxidized α1-antitrypsin stimulates the release of monocyte chemotactic protein-1 from lung epithelial cells: potential role in emphysema,” American Journal of Physiology—Lung Cellular and Molecular Physiology, vol. 297, no. 2, pp. L388–L400, 2009. View at Publisher · View at Google Scholar · View at Scopus
  3. K.-S. Kwon, M. Song, and M.-H. Yu, “Purification and characterization of α1-antitrypsin secreted by recombinant yeast Saccharomyces diastaticus,” Journal of Biotechnology, vol. 42, no. 3, pp. 191–195, 1995. View at Publisher · View at Google Scholar · View at Scopus
  4. A. Modrykamien and J. K. Stoller, “Alpha-1 antitrypsin (AAT) deficiency—what are the treatment options?” Expert Opinion on Pharmacotherapy, vol. 10, no. 16, pp. 2653–2661, 2009. View at Publisher · View at Google Scholar · View at Scopus
  5. D. L. DeMeo and E. K. Silverman, “α1-Antitrypsin deficiency. 2: genetic aspects of α1-antitrypsin deficiency: phenotypes and genetic modifiers of emphysema risk,” Thorax, vol. 59, no. 3, pp. 259–264, 2004. View at Publisher · View at Google Scholar · View at Scopus
  6. D. A. Lomas, D. L. Evans, J. T. Finch, and R. W. Carrell, “The mechanism of Z α1-antitrypsin accumulation in the liver,” Nature, vol. 357, no. 6379, pp. 605–607, 1992. View at Publisher · View at Google Scholar · View at Scopus
  7. S. Eriksson, J. Carlson, and R. Velez, “Risk of cirrhosis and primary liver cancer in alpha1-antitrypsin deficiency,” The New England Journal of Medicine, vol. 314, no. 12, pp. 736–739, 1986. View at Publisher · View at Google Scholar · View at Scopus
  8. T. Cabezon, M. De Wilde, P. Herion, R. Loriau, and A. Bollen, “Expression of human alpha 1-antitrypsin cDNA in the yeast Saccharomyces cerevisiae,” Proceedings of the National Academy of Sciences of the United States of America, vol. 81, no. 21, pp. 6594–6598, 1984. View at Publisher · View at Google Scholar · View at Scopus
  9. J. E. Gadek, H. G. Klein, P. V. Holland, and R. G. Crystal, “Replacement therapy of alpha 1-antitrypsin deficiency. Reversal of protease-antiprotease imbalance within the alveolar structures of PiZ subjects,” The Journal of Clinical Investigation, vol. 68, no. 5, pp. 1158–1165, 1981. View at Publisher · View at Google Scholar · View at Scopus
  10. R. B. Schlesinger, “Comparative deposition of inhaled aerosols in experimental animals and humans: a review,” Journal of Toxicology and Environmental Health, vol. 15, no. 2, pp. 197–214, 1985. View at Publisher · View at Google Scholar · View at Scopus
  11. P. E. Morrow, “Factors determining hygroscopic aerosol deposition in airways,” Physiological Reviews, vol. 66, no. 2, pp. 330–376, 1986. View at Google Scholar · View at Scopus
  12. R. C. Hubbard, M. A. Casolaro, M. Mitchell et al., “Fate of aerosolized recombinant DNA-produced α1-antitrypsin: use of the epithelial surface of the lower respiratory tract to administer proteins of therapeutic importance,” Proceedings of the National Academy of Sciences of the United States of America, vol. 86, no. 2, pp. 680–684, 1989. View at Publisher · View at Google Scholar · View at Scopus
  13. S. Kossodo, J. Zhang, K. Groves et al., “Noninvasive in vivo quantification of neutrophil elastase activity in acute experimental mouse lung injury,” International Journal of Molecular Imaging, vol. 2011, Article ID 581406, 11 pages, 2011. View at Publisher · View at Google Scholar
  14. R. Corteling, D. Wyss, and A. Trifilieff, “In vivo models of lung neutrophil activation. Comparison of mice and hamsters,” BMC Pharmacology, vol. 2, article 1, 2002. View at Publisher · View at Google Scholar · View at Scopus
  15. L.-Y. Chen, W. W. Pan, M. Chen et al., “Synergistic induction of inflammation by bacterial products lipopolysaccharide and fMLP: an important microbial pathogenic mechanism,” The Journal of Immunology, vol. 182, no. 4, pp. 2518–2524, 2009. View at Publisher · View at Google Scholar · View at Scopus
  16. G. Matute-Bello, C. W. Frevert, and T. R. Martin, “Animal models of acute lung injury,” American Journal of Physiology—Lung Cellular and Molecular Physiology, vol. 295, no. 3, pp. L379–L399, 2008. View at Publisher · View at Google Scholar · View at Scopus
  17. M. R. Zalutsky and A. S. Narula, “A method for the radiohalogenation of proteins resulting in decreased thyroid uptake of radioiodine,” International Journal of Radiation Applications and Instrumentation Part A, vol. 38, no. 12, pp. 1051–1055, 1987. View at Publisher · View at Google Scholar · View at Scopus
  18. M. D. Wewers, M. A. Casolaro, S. E. Sellers et al., “Replacement therapy for alpha 1-antitrypsin deficiency associated with emphysema,” The New England Journal of Medicine, vol. 316, no. 17, pp. 1055–1062, 1987. View at Publisher · View at Google Scholar · View at Scopus
  19. K. E. Driscoll, D. L. Costa, G. Hatch et al., “Intratracheal instillation as an exposure technique for the evaluation of respiratory tract toxicity: uses and limitations,” Toxicological Sciences, vol. 55, no. 1, pp. 24–35, 2000. View at Publisher · View at Google Scholar · View at Scopus
  20. D. Jonigk, M. Al-Omari, L. Maegel et al., “Anti-inflammatory and immunomodulatory properties of α1-antitrypsin without inhibition of elastase,” Proceedings of the National Academy of Sciences of the United States of America, vol. 110, no. 37, pp. 15007–15012, 2013. View at Publisher · View at Google Scholar · View at Scopus
  21. G. Oberdorster, H. Oldiges, and B. Zimmermann, “Lung deposition and clearance of cadmium in rats exposed by inhalation or by intratracheal instillation,” Zentralblatt fur Bakteriologie 1 Abt Originale B, Hygiene, Krankenhaushygiene, Betriebshygiene, praventive Medizin, vol. 170, no. 1-2, pp. 35–43, 1980. View at Google Scholar
  22. J. D. Brain, D. E. Knudson, S. P. Sorokin, and M. A. Davis, “Pulmonary distribution of particles given by intratracheal instillation or by aerosol inhalation,” Environmental Research, vol. 11, no. 1, pp. 13–33, 1976. View at Publisher · View at Google Scholar · View at Scopus