Advertisement

On the mechanism of human polymorphonuclear leukocyte deactivation of chemotaxis by the synthetic peptide formyl-methiony-leucyl-phenylalanine

  • J. P. Abita
Part of the Inflammation: Mechanisms and Treatment book series (FTIN, volume 4)

Abstract

Polymorphonuclear leukocytes respond chemotactically in vitro to a variety of compounds including denatured proteins1 factors derived from complement2, bacterial products3 and synthetic peptides, the most potent being the peptide formyl-methionyl-leucyl-phenylalanine (f-Met-Leu-Phe)4,5. In addition f-Met-Leu-Phe induces granule enzyme secretion and superoxide production when added with cytochalasin B to rabbit neutrophils in suspension4,6 and aggregates these cells7. There is evidence that all these functions result from the interaction of the peptide with a common membrane receptor4,6–8 which has been demonstrated, by direct binding studies, to exist on the cell surface of rabbit9 and human neutrophils10.

Keywords

Human Neutrophil Cellulose Nitrate Calcium Ionophore A23187 Chemotactic Peptide Lower Filter 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. 1.
    Wilkinson, P. C. (1974) In Chemotaxis and inflammation, p. 54. (Edinburgh: Churchill Livingston)Google Scholar
  2. 2.
    Snyderman, R., Phillips, J. and Mergenhagen, S. E. (1970). Infect. Immun. 1, 521PubMedGoogle Scholar
  3. 3.
    Keller, H. V. and Sorkin, E. (1967). Int. Arch. Allergy, 31, 505CrossRefGoogle Scholar
  4. 4.
    Showell, H.J., Freer, R.J., Zigmond, S.H., Schiffman, E., Aswanikumar, S., Corcoran, B. A. and Becker, E. L. (1976).J. Exp. Med., 143,1154PubMedCrossRefGoogle Scholar
  5. 5.
    Spilberg J., Mandell, B., Mehta, J., Sullivan, T. and Sinckowitz, L. (1978). J. Lab. Clin. Med., 92,297PubMedGoogle Scholar
  6. 6.
    Becker, E. L., Sigman, M. and Oliver, J. M. (1979). Am. J. Pathol, 95, 81PubMedGoogle Scholar
  7. 7.
    O’Flaherty, J.T., Showell, H. J., Kreutzer, D. L., Ward, P. A. and Becker, E. L. (1978). J. Immunol. 120,1326PubMedGoogle Scholar
  8. 8.
    Becker, E. L. (1976) Am. J. Pathol, 85, 385PubMedGoogle Scholar
  9. 9.
    Aswanikumar, S., Corcoran, B., Schiffmann, E., Day, A. R., Freer, R.J., Showell, H. J., Becker, E. L. and Pert, C. (1977). Biochem. Biophys Res. Commun., 74, 810PubMedCrossRefGoogle Scholar
  10. 10.
    Williams, L. T., Snyderman, R., Pike, M. C. and Lefkowitz, R. J. (1977). Proc. Natl. Acad. Sci. (USA) 74,1204CrossRefGoogle Scholar
  11. 11.
    Ward, P. A. and Becker, E. L. (1968). J. Exp. Med., 127, 693PubMedCrossRefGoogle Scholar
  12. 12.
    Spilberg, L, Mandell, B. and Hoffstein, S. (1979). J. Lab. Clin. Med. 94, 361PubMedGoogle Scholar
  13. 13.
    Showell, H. J., Williams, D., Becker, E. L.,Naccache, P. H. and Sha’afi, R. (1979). J. Reticuloendothelial Soc., 25,139Google Scholar
  14. 14.
    Kahn, R. C. (1976). J. Biol. Chem., 70, 261Google Scholar
  15. 15.
    Zigmond, S. H. and Sullivan, S. J. (1979). J. Cell. Biol. 82, 515CrossRefGoogle Scholar
  16. 16.
    Fehr, J. and Dahinden, C. (1979). J. Clin. Invest., 64, 8PubMedCrossRefGoogle Scholar
  17. 17.
    Fernandez, H. N., Henson, P. M., Otani, A. and Hugh, T. E. (1978).J. Immunol., 120,109PubMedGoogle Scholar
  18. 18.
    Chenoweth, D. E. and Hugh, T. E. (1978). Proc. Natl. Acad. Sci (USA) 75, 3943CrossRefGoogle Scholar
  19. 19.
    Wilkinson, P. C. (1979). Immunology, 36, 579PubMedGoogle Scholar

Copyright information

© MTP Press Limited 1980

Authors and Affiliations

  • J. P. Abita
    • 1
  1. 1.France

Personalised recommendations