Erythrocyte lysis by PMA-triggered neutrophil polymorphonuclears: Evidence for an hypochlorous acid-dependent process

F. Dallegri, A. Ballestrero, G. Frumento, F. Patrone

Research output: Contribution to journalArticle

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Abstract

Human red blood cells (HRBC) were efficiently lysed when incubated with neutrophil poly-morphonuclears (PMN) in the presence of phorbol-myristate-acetate (PMA), as detected by a 4-hr 51Cr release assay. The lysis was virtually absent in the presence of catalase, azide or cyanide and in the absence of chloride ions. These findings indicate the involvement of the myeloperoxidase (MPO)-hydrogen peroxide (H2O2)-chloriDe (Cl(-)) system in the cytolytic process. As the MPO-H2O2-Cl(-) system is capable of generating the powerful oxidant hypochlorous acid (HOCl), cytotoxicity assays were performed in the presence of taurine, glycine, serine and valine to scavenge this potentially lytic agent. Each of these compounds efficiently inhibited the HRBC lysis by PMA-triggered PMN, as well as the lysis caused by HOCl in cell-free system. Thus the results suggest that HOCl, or an agent with similar reactivity, plays a key role in the PMA-dependent PMN-mediated cytotoxicity against HRBC targets.

Original languageEnglish
Pages (from-to)639-645
Number of pages7
JournalImmunology
Volume55
Issue number4
Publication statusPublished - 1985

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Hypochlorous Acid
Tetradecanoylphorbol Acetate
Neutrophils
Erythrocytes
Peroxidase
Chlorides
Azides
Cell-Free System
Taurine
Valine
Cyanides
Oxidants
Catalase
Glycine
Serine
Hydrogen Peroxide
Ions

ASJC Scopus subject areas

  • Immunology

Cite this

Erythrocyte lysis by PMA-triggered neutrophil polymorphonuclears : Evidence for an hypochlorous acid-dependent process. / Dallegri, F.; Ballestrero, A.; Frumento, G.; Patrone, F.

In: Immunology, Vol. 55, No. 4, 1985, p. 639-645.

Research output: Contribution to journalArticle

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AU - Patrone, F.

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AB - Human red blood cells (HRBC) were efficiently lysed when incubated with neutrophil poly-morphonuclears (PMN) in the presence of phorbol-myristate-acetate (PMA), as detected by a 4-hr 51Cr release assay. The lysis was virtually absent in the presence of catalase, azide or cyanide and in the absence of chloride ions. These findings indicate the involvement of the myeloperoxidase (MPO)-hydrogen peroxide (H2O2)-chloriDe (Cl(-)) system in the cytolytic process. As the MPO-H2O2-Cl(-) system is capable of generating the powerful oxidant hypochlorous acid (HOCl), cytotoxicity assays were performed in the presence of taurine, glycine, serine and valine to scavenge this potentially lytic agent. Each of these compounds efficiently inhibited the HRBC lysis by PMA-triggered PMN, as well as the lysis caused by HOCl in cell-free system. Thus the results suggest that HOCl, or an agent with similar reactivity, plays a key role in the PMA-dependent PMN-mediated cytotoxicity against HRBC targets.

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