About this Journal Submit a Manuscript Table of Contents
International Journal of Peptides
Volume 2011 (2011), Article ID 594723, 7 pages
http://dx.doi.org/10.1155/2011/594723
Review Article

Structural and Functional Consequences Induced by Post-Translational Modifications in α-Defensins

1School of Biosciences and Biotechnologies, University of Camerino, Gentile III da Varano Street, 62032 Camerino, Italy
2Department of Chemistry, University of Siena, 53100 Siena, Italy
3Research Center, Novartis Vaccines and Diagnostics, Fiorentina 1 Street, 53100 Siena, Italy
4Department of Evolutionary Biology, University of Siena, 53100 Siena, Italy

Received 3 April 2011; Accepted 22 May 2011

Academic Editor: Peter Bergman

Copyright © 2011 Enrico Balducci 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. R. I. Lehrer, A. K. Lichtenstein, and T. Ganz, “Defensins: antimicrobial and cytotoxic peptides of mammalian cells,” Annual Review of Immunology, vol. 11, pp. 105–128, 1993. View at Scopus
  2. F. G. Oppenheim, T. Xu, F. M. McMillian et al., “Histatins, a novel family of histidine-rich proteins in human parotid secretion. Isolation, characterization, primary structure, and fungistatic effects on Candida albicans,” Journal of Biological Chemistry, vol. 263, no. 16, pp. 7472–7477, 1988. View at Scopus
  3. B. Schittek, R. Hipfel, B. Sauer et al., “Dermcidin: a novel human antibiotic peptide secreted by sweat glands,” Nature Immunology, vol. 2, no. 12, pp. 1133–1137, 2001. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  4. S. V. Peña, D. A. Hanson, B. A. Carr, T. J. Goralski, and A. M. Krensky, “Processing, subcellular localization, and function of 519 (granulysin), a human late T cell activation molecule with homology to small, lytic, granule proteins,” Journal of Immunology, vol. 158, no. 6, pp. 2680–2688, 1997. View at Scopus
  5. K. W. Bensch, M. Raida, H. J. Magert, P. Schulz-Knappe, and W. G. Forssmann, “hBD-1: a novel β-defensin from human plasma,” FEBS Letters, vol. 368, no. 2, pp. 331–335, 1995. View at Publisher · View at Google Scholar · View at Scopus
  6. J. Harder, J. Bartels, E. Christophers, and J. M. Schröder, “Isolation and characterization of human β-defensin-3, a novel human inducible peptide antibiotic,” Journal of Biological Chemistry, vol. 276, no. 8, pp. 5707–5713, 2001. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  7. J. Harder, J. Bartels, E. Christophers, and J. M. Schroder, “A peptide antibiotic from human skin,” Nature, vol. 387, no. 6636, p. 861, 1997. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  8. L. Eckmann, “Defence molecules in intestinal innate immunity against bacterial infections,” Current Opinion in Gastroenterology, vol. 21, no. 2, pp. 147–151, 2005. View at Publisher · View at Google Scholar
  9. R. I. Lehrer and T. Ganz, “Cathelicidins: a family of endogenous antimicrobial peptides,” Current Opinion in Hematology, vol. 9, no. 1, pp. 18–22, 2002. View at Publisher · View at Google Scholar
  10. G. Paone, L. A. Stevens, R. L. Levine et al., “ADP-ribosyltransferase-specific modification of human neutrophil peptide-1,” Journal of Biological Chemistry, vol. 281, no. 25, pp. 17054–17060, 2006. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  11. K. Ueda and O. Hayaishi, “ADP-ribosylation,” Annual Review of Biochemistry, vol. 54, pp. 73–100, 1985.
  12. K. A. Wreggett, “Bacterial toxins and the role of ADP-ribosylation,” Journal of Receptor Research, vol. 6, no. 2, pp. 95–126, 1986. View at Scopus
  13. S. S. Lahiri, “Bacterial toxins—an overview,” Journal of Natural Toxins, vol. 9, no. 4, pp. 381–408, 2000. View at Scopus
  14. M. J. Pallen, A. C. Lam, N. J. Loman, and A. McBride, “An abundance of bacterial ADP-ribosyltransferases—Implications for the origin of exotoxins and their human homologues,” Trends in Microbiology, vol. 9, no. 7, pp. 302–308, 2001. View at Publisher · View at Google Scholar · View at Scopus
  15. I. J. Okazaki, H. J. Kim, and J. Moss, “Cloning and characterization of a novel membrane-associated lymphocyte NAD:arginine ADP-ribosyltransferase,” Journal of Biological Chemistry, vol. 271, no. 36, pp. 22052–22057, 1996. View at Publisher · View at Google Scholar · View at Scopus
  16. I. J. Okazaki and J. Moss, “Characterization of glycosylphosphatidylinositiol-anchored, secreted, and intracellular vertebrate mono-ADP-ribosyltransferases,” Annual Review of Nutrition, vol. 19, pp. 485–509, 1999. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  17. A. G. Ladurner, “Inactivating chromosomes: a macro domain that minimizes transcription,” Molecular Cell, vol. 12, no. 1, pp. 1–2, 2003. View at Publisher · View at Google Scholar · View at Scopus
  18. E. Balducci, K. Horiba, J. Usuki, M. Park, V. J. Ferrans, and J. Moss, “Selective expression of RT6 superfamily in human bronchial epithelial cells,” American Journal of Respiratory Cell and Molecular Biology, vol. 21, no. 3, pp. 337–346, 1999. View at Scopus
  19. J. Ashitani, H. Mukae, M. Nakazato et al., “Elevated concentrations of defensins in bronchoalveolar lavage fluid in diffuse panbronchiolitis,” European Respiratory Journal, vol. 11, no. 1, pp. 104–111, 1998. View at Publisher · View at Google Scholar · View at Scopus
  20. H. Steiner, D. Hultmark, and A. Engstrom, “Sequence and specificity of two antibacterial proteins involved in insect immunity,” Nature, vol. 292, no. 5820, pp. 246–248, 1981. View at Scopus
  21. W. Meyer-Glauner, E. Bernard, D. Armstrong, and B. Merrifield, “The antifungal activity of carrier peptides, L-arginyl-X-L-phenylalanine, containing amino acid antagonists or atypical non-biogenic D-amino acids in the central position,” Zentralblatt fur Bakteriologie Mikrobiologie und Hygiene A, vol. 252, no. 2, pp. 274–278, 1982.
  22. Z. Oren, J. Hong, and Y. Shai, “A repertoire of novel antibacterial diastereomeric peptides with selective cytolytic activity,” Journal of Biological Chemistry, vol. 272, no. 23, pp. 14643–14649, 1997. View at Publisher · View at Google Scholar · View at Scopus
  23. G. Paone, A. Wada, L. A. Stevens et al., “ADP ribosylation of human neutrophil peptide-1 regulates its biological properties,” Proceedings of the National Academy of Sciences of the United States of America, vol. 99, no. 12, pp. 8231–8235, 2002. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  24. G. Zou, E. De Leeuw, C. Li et al., “Toward understanding the cationicity of defensins: arg and Lys versus their noncoded analogs,” Journal of Biological Chemistry, vol. 282, no. 27, pp. 19653–19665, 2007. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  25. E. de Leeuw, M. Rajabi, G. Zou, M. Pazgier, and W. Lu, “Selective arginines are important for the antibacterial activity and host cell interaction of human α-defensin 5,” FEBS Letters, vol. 583, no. 15, pp. 2507–2512, 2009. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  26. K. Rikova, A. Guo, Q. Zeng et al., “Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer,” Cell, vol. 131, no. 6, pp. 1190–1203, 2007. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  27. S. V. Kharadia and D. J. Graves, “Relationship of phosphorylation and ADP-ribosylation using a synthetic peptide as a model substrate,” Journal of Biological Chemistry, vol. 262, no. 36, pp. 17379–17383, 1987. View at Scopus
  28. L. A. Stevens, R. L. Levine, B. R. Gochuico, and J. Moss, “ADP-ribosylation of human defensin HNP-1 results in the replacement of the modified arginine with the noncoded amino acid ornithine,” Proceedings of the National Academy of Sciences of the United States of America, vol. 106, no. 47, pp. 19796–19800, 2009. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  29. J. Moss, S. C. Tsai, R. Adamik, H. C. Chen, and S. J. Stanley, “Purification and characterization of ADP-ribosylarginine hydrolase from Turkey erythrocytes,” Biochemistry, vol. 27, no. 15, pp. 5819–5823, 1988. View at Scopus
  30. A. Zolkiewska and J. Moss, “Processing of ADP-ribosylated integrin α7 in skeletal muscle myotubes,” Journal of Biological Chemistry, vol. 270, no. 16, pp. 9227–9233, 1995. View at Publisher · View at Google Scholar · View at Scopus
  31. D. M. E. Bowdish, D. J. Davidson, and R. E. W. Hancock, “A re-evaluation of the role of host defence peptides in mammalian immunity,” Current Protein and Peptide Science, vol. 6, no. 1, pp. 35–51, 2005. View at Publisher · View at Google Scholar · View at Scopus
  32. H. Osago, M. Terashima, N. Hara, K. Yamada, and M. Tsuchiya, “A new detection method for arginine-specific ADP-ribosylation of protein—a combinational use of anti-ADP-ribosylarginine antibody and ADP-ribosylarginine hydrolase,” Journal of Biochemical and Biophysical Methods, vol. 70, no. 6, pp. 1014–1019, 2008. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  33. P. M. Moyle and T. W. Muir, “Method for the synthesis of mono-ADP-ribose conjugated peptides,” Journal of the American Chemical Society, vol. 132, no. 45, pp. 15878–15880, 2010. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  34. G. J. Van Der Heden Van Noort, M. G. Van Der Horst, H. S. Overkleeft, G. A. Van Der Marel, and D. V. Filippov, “Synthesis of mono-ADP-ribosylated oligopeptides using ribosylated amino acid building blocks,” Journal of the American Chemical Society, vol. 132, no. 14, pp. 5236–5240, 2010. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus