Angiogenins: a new class of microbicidal proteins involved in innate immunity (original) (raw)

References

  1. Fett, J.W. et al. Isolation and characterization of angiogenin, an angiogenic protein from human carcinoma cells. Biochemistry 24, 5480–5486 (1985).
    Article CAS Google Scholar
  2. Kao, R.Y.T. et al. A small-molecule inhibitor of the ribonucleolytic activity of human angiogenin that possesses antitumor activity. Proc. Natl. Acad. Sci. USA 99, 10066–10071 (2002).
    Article CAS Google Scholar
  3. Rybak, S.M., Fett, J.W., Yao, Q.Z. & Vallee, B.L. Angiogenin mRNA in human tumor and normal cells. Biochem. Biophys. Res. Commun. 146, 1240 (1987).
    Article CAS Google Scholar
  4. Weiner, H.L., Weiner, L.H. & Swain, J.L. Tissue distribution and developmental expression of the messenger RNA encoding angiogenin. Science 237, 280–282 (1987).
    Article CAS Google Scholar
  5. Olson, K.A., Verselis, S.J. & Fett, J.W. Angiogenin is regulated in vivo as an acute phase protein. Biochem. Biophys. Res. Commun. 242, 480–483 (1998).
    Article CAS Google Scholar
  6. Zhang, J. & Rosenberg, H.F. Diversifying selection of the tumor-growth promoter angiogenin in primate evolution. Mol. Biol. Evol. 19, 438–445 (2002).
    Article CAS Google Scholar
  7. Strydom, D.J. The angiogenins. Cell. Mol. Life Sci. 54, 811–824 (1998).
    Article CAS Google Scholar
  8. Nobile, V., Vallee, B.L. & Shapiro, R. Characterization of mouse angiogenin-related protein: implications for functional studies on angiogenin. Proc. Natl. Acad. Sci. USA 93, 4331–4335 (1996).
    Article CAS Google Scholar
  9. Fu, X., Roberts, W.G., Nobile, V., Shapiro, R. & Kamps, M.P. mAngiogenin-3, a target gene of oncoprotein E2a-Pbx1, encodes a new angiogenic member of the angiogenin family. Growth Factors 17, 125–137 (1999).
    Article CAS Google Scholar
  10. Bry, L., Falk, P.G., Midtvedt, T. & Gordon, J.I. A model of host-microbial interactions in an open mammalian ecosystem. Science 273, 1380–1383 (1996).
    Article CAS Google Scholar
  11. Hooper, L.V. et al. Molecular analysis of commensal host-microbial relationships in the intestine. Science 291, 881–884 (2001).
    Article CAS Google Scholar
  12. Emmert-Buck, M.R. et al. Laser capture microdissection. Science 274, 998–1001 (1996).
    Article CAS Google Scholar
  13. Garabedian, E.R., Roberts, L.J., McNevin, M.S. & Gordon, J.I. Examining the role of Paneth cells in the small intestine by lineage ablation in transgenic mice. J. Biol. Chem. 272, 23729–23740 (1997).
    Article CAS Google Scholar
  14. Ayabe, T. et al. Secretion of microbicidal α-defensins by intestinal Paneth cells in response to bacteria. Nat. Immunol. 1, 113–118 (2000).
    Article CAS Google Scholar
  15. Holloway, D.E., Hares, M.C., Shapiro, R., Subramanian, V. & Acharya, K.R. High-level expression of three members of the murine angiogenin family in Escherichia coli and purification of the recombinant proteins. Protein Expr. Purif. 22, 307–317 (2001).
    Article CAS Google Scholar
  16. Rosenberg, H.F. & Domachowske, J.B. Eosinophils, eosinophil ribonucleases, and their role in host defense against respiratory virus pathogens. J. Leukoc. Biol. 70, 691–698 (2001).
    CAS PubMed Google Scholar
  17. Rosenberg, H.F. Recombinant human eosinophil cationic protein. Ribonuclease activity is not essential for cytotoxicity. J. Biol. Chem. 270, 7876–7881 (1995).
    Article CAS Google Scholar
  18. Glaser, P. et al. Comparative genomics of Listeria species. Science 294, 849–852 (2001).
    CAS PubMed Google Scholar
  19. Ghosh, D. et al. Paneth cell trypsin is the processing enzyme for human defensin-5. Nat. Immunol. 3, 583–590 (2002).
    Article CAS Google Scholar
  20. Goldman, M.J. et al. Human β-defensin-1 is a salt-sensitive antibiotic in lung that is inactivated in cystic fibrosis. Cell 88, 553–560 (1997).
    Article CAS Google Scholar
  21. Lehrer, R.I., Lichtenstein, A.K. & Ganz, T. Defensins: antimicrobial and cytotoxic peptides of mammalian cells. Annu. Rev. Immunol. 11, 105–128 (1993).
    Article CAS Google Scholar
  22. Panyutich, A.V., Hiemstra, P.S., van Wetering, S. & Ganz, T. Human neutrophil defensin and serpins form complexes and inactivate each other. Am. J. Respir. Cell. Mol. Biol. 12, 351–357 (1995).
    Article CAS Google Scholar
  23. Panyutich, A.V., Szold, O., Poon, P.H., Tseng, Y. & Ganz, T. Identification of defensin binding to C1 complement. FEBS Lett. 356, 169–173 (1994).
    Article CAS Google Scholar
  24. Saxena, S.K., Rybak, S.M., Davey, R.T. Jr., Youle, R.J. & Ackerman, E.J. Angiogenin is a cytotoxic, tRNA-specific ribonuclease in the RNase A superfamily. J. Biol. Chem. 267, 21982–21986 (1992).
    CAS PubMed Google Scholar
  25. Savage, D.C. Microbial ecology of the gastrointestinal tract. Annu. Rev. Microbiol. 31, 107–133 (1977).
    Article CAS Google Scholar
  26. Putsep, K. et al. Germ-free and colonized mice generate the same products from enteric prodefensins. J. Biol. Chem. 275, 40478–40482 (2000).
    Article CAS Google Scholar
  27. Neish, A.S. et al. Prokaryotic regulation of epithelial responses by inhibition of IκB-α ubiquitination. Science 289, 1560–1563 (2000).
    Article CAS Google Scholar
  28. Guan, K.L. & Dixon, J.E. Eukaryotic proteins expressed in Escherichia coli: an improved thrombin cleavage and purification procedure of fusion proteins with glutathione S-transferase. Anal. Biochem. 192, 262–267 (1991).
    Article CAS Google Scholar
  29. Shapiro, R., Weremowicz, S., Riordan, J.F. & Vallee, B.L. Ribonucleolytic activity of angiogenin: essential histidine, lysine, and arginine residues. Proc. Natl. Acad. Sci. USA 84, 8783–8787 (1987).
    Article CAS Google Scholar

Download references