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Chemo tactic factor inactivation by the myelo peroxidase hydrogen per oxide halide system an inflammatory control mechanism



Chemo tactic factor inactivation by the myelo peroxidase hydrogen per oxide halide system an inflammatory control mechanism



Journal of Clinical Investigation 64(4): 913-920



Polymorphonuclear leukocytes [human] may modulate the acute inflammatory response by secretion of enzymes capable of inactivating mediators of inflammation. Ability of the myeloperoxidase-H2O2-halide system of the neutrophil to inactivate chemoattractants was examined using a radioassay and a morphologic assay of chemotaxis. Incubation of a complement-derived agent, C5a [complement component 5a] or a synthetic formyl-methionyl peptide chemoattractant with the myeloperoxidase system for 15 min at 37.degree. C resulted in essentially complete chemotactic activity loss. Inactivation was dependent on enzymatically active myeloperoxidase, H2O2 or a peroxide-generating enzyme system and a halide cofactor. It was blocked by agents which inhibit peroxidase (azide) or degrade H2O2 (catalase). Inactivation of chemoattractants was time-dependent, reaching maximal levels within 1-5 min, and temperature-dependent with no significant inactivation occurring at 0.degree. C. H2O2 alone had no significant inactivating ability at concentrations as high as 10 mM, whereas in the presence of myeloperoxidase and a halide, 0.1 .mu.M H2O2 showed significant activity and 10 .mu.M H2O2 caused complete inactivation. On a molar basis, order of effectiveness of the halide cofactors was Br- > I- > Cl-, although only Cl- was fully active at physiologic concentrations. Neutrophils stimulated by phagocytosis or by membrane-perturbing agents secrete enzymatic constituents, including myeloperoxidase and metabolic products such as H2O2. The myeloperoxidase system acting at an extracellular site serves as an inflammatory control mechanism by its ability to inactivate neutrophil chemoattractants.

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Accession: 004940895

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