Skip to main content
Clinical and Experimental Immunology logoLink to Clinical and Experimental Immunology
. 1986 Sep;65(3):664–670.

Interference of target cell catalase with an early step of the neutrophil cytolytic pathway.

F Dallegri, A Ballestrero, G Frumento, F Patrone
PMCID: PMC1542508  PMID: 3022971

Abstract

The hypochlorous acid (HOCL)-dependent lysis of human red blood cells (HRBC) targets by neutrophils, activated with opsonized zymosan particles (OPZ), was increased by inhibiting HRBC catalatic activity with aminotriazole (AT; HRBCAT). The inhibition of HRBC glutathione cycle activity with carmustine (BCNU; HRBCBCNU) had no effect. In addition, the recovery of hydrogen peroxide (H2O2) and HOCL from neutrophils, activated under conditions similar to those used for cytotoxicity assay, was reduced by the presence of HRBC and restored by replacing HRBC with HRBCAT, but not with HRBCBCNU. Linear relationships were found between the increments in the neutrophil-mediated lysis, observed by using HRBCAT instead of HRBC, and the increments in the H2O2 or HOCL recovery, detected by replacing HRBC with HRBCAT. Together these data, coupled with the results obtained by probing neutrophil cytolysis with chemical agents, suggest that the increased cytolytic efficiency displayed by neutrophils against HRBCAT, inhibited in their catalatic activity, is due to an enhanced availability of neutrophil-derived H2O2, with a consequent enhancement in the HOCL production (according to the following reaction: (formula; see text). Thus it appears that HRBC catalase restrains the neutrophil cytolytic activity, by interfering with an early step of the pathway through which neutrophils generate cytotoxins.

Full text

PDF
664

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Aune T. M., Thomas E. L. Accumulation of hypothiocyanite ion during peroxidase-catalyzed oxidation of thiocyanate ion. Eur J Biochem. 1977 Oct 17;80(1):209–214. doi: 10.1111/j.1432-1033.1977.tb11873.x. [DOI] [PubMed] [Google Scholar]
  2. Chance B., Sies H., Boveris A. Hydroperoxide metabolism in mammalian organs. Physiol Rev. 1979 Jul;59(3):527–605. doi: 10.1152/physrev.1979.59.3.527. [DOI] [PubMed] [Google Scholar]
  3. Dallegri F., Ballestrero A., Frumento G., Patrone F. Erythrocyte lysis by PMA-triggered neutrophil polymorphonuclears: evidence for an hypochlorous acid-dependent process. Immunology. 1985 Aug;55(4):639–645. [PMC free article] [PubMed] [Google Scholar]
  4. Dallegri F., Patrone F., Bonvini E., Gahrton G., Holm G., Sacchetti C. Ox erythrocyte cytotoxicity by phorbol myristate acetate-activated human neutrophils. Scand J Immunol. 1983 Feb;17(2):109–114. doi: 10.1111/j.1365-3083.1983.tb00772.x. [DOI] [PubMed] [Google Scholar]
  5. Halliwell B., Gutteridge J. M. Oxygen toxicity, oxygen radicals, transition metals and disease. Biochem J. 1984 Apr 1;219(1):1–14. doi: 10.1042/bj2190001. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. MARGOLIASH E., NOVOGRODSKY A. A study of the inhibition of catalase by 3-amino-1:2:4:-triazole. Biochem J. 1958 Mar;68(3):468–475. doi: 10.1042/bj0680468. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Nathan C. F., Arrick B. A., Murray H. W., DeSantis N. M., Cohn Z. A. Tumor cell anti-oxidant defenses. Inhibition of the glutathione redox cycle enhances macrophage-mediated cytolysis. J Exp Med. 1981 Apr 1;153(4):766–782. doi: 10.1084/jem.153.4.766. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Ruch W., Cooper P. H., Baggiolini M. Assay of H2O2 production by macrophages and neutrophils with homovanillic acid and horse-radish peroxidase. J Immunol Methods. 1983 Oct 28;63(3):347–357. doi: 10.1016/s0022-1759(83)80008-8. [DOI] [PubMed] [Google Scholar]
  9. Test S. T., Weiss S. J. Quantitative and temporal characterization of the extracellular H2O2 pool generated by human neutrophils. J Biol Chem. 1984 Jan 10;259(1):399–405. [PubMed] [Google Scholar]
  10. Thomas E. L., Grisham M. B., Melton D. F., Jefferson M. M. Evidence for a role of taurine in the in vitro oxidative toxicity of neutrophils toward erythrocytes. J Biol Chem. 1985 Mar 25;260(6):3321–3329. [PubMed] [Google Scholar]
  11. Weiss S. J., Klein R., Slivka A., Wei M. Chlorination of taurine by human neutrophils. Evidence for hypochlorous acid generation. J Clin Invest. 1982 Sep;70(3):598–607. doi: 10.1172/JCI110652. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Weiss S. J., Rustagi P. K., LoBuglio A. F. Human granulocyte generation of hydroxyl radical. J Exp Med. 1978 Feb 1;147(2):316–323. doi: 10.1084/jem.147.2.316. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Weiss S. J., Slivka A. Monocyte and granulocyte-mediated tumor cell destruction. A role for the hydrogen peroxide-myeloperoxidase-chloride system. J Clin Invest. 1982 Feb;69(2):255–262. doi: 10.1172/JCI110447. [DOI] [PMC free article] [PubMed] [Google Scholar]

Articles from Clinical and Experimental Immunology are provided here courtesy of British Society for Immunology

RESOURCES