Free radical formation from organic hydroperoxides in isolated human polymorphonuclear neutrophils.
We have demonstrated with electron paramagnetic resonance (EPR) that organic hydroperoxides are decomposed to free radicals by both human polymorphonuclear leukocytes (PMNs) and purified myeloperoxidase. When tert-butyl hydroperoxide was incubated with either PMNs or purified myeloperoxidase, peroxyl, alkoxyl, and alkyl radicals were trapped by the spin trap 5,5-dimethyl-1-pyrroline N-oxide (DMPO). In the case of ethyl hydroperoxide, DMPO radical adducts of peroxyl and alkyl (identified as alpha-hydroxyethyl when trapped by tert-nitrosobutane) radicals were detected. Radical adduct formation was inhibited when azide was added to the incubation mixture. Myeloperoxidase-deficient PMNs produced DMPO radical adduct intensities at only about 20-30% of that of normal PMNs. Our studies suggest that myeloperoxidase in PMNs is primarily responsible for the decomposition of organic hydroperoxides to free radicals. The finding of the free radical formation derived from organic hydroperoxides by PMNs may be related to the cytotoxicity of this class of compounds.
Chamulitrat
W
W
National Institute of Environmental Health Sciences, Research Triangle Park, NC 27709.
Cohen
M S
MS
Mason
R P
RP
D000438:Alcohols / Q000097:blood*; D002374:Catalase / Q000097:blood; D004578:Electron Spin Resonance Spectroscopy; D005609:Free Radicals; D006801:Humans; D008958:Models, Molecular; D009504:Neutrophils / Q000378:metabolism*; D009195:Peroxidase / Q000097:blood / Q000172:deficiency; D010545:Peroxides / Q000097:blood*; D016897:Respiratory Burst; D020122:tert-Butylhydroperoxide
D000438:Alcohols; D005609:Free Radicals; D010545:Peroxides; C059688:alkoxyl radical; C025577:ethyl hydroperoxide; C049375:perhydroxyl radical; D020122:tert-Butylhydroperoxide; D002374:Catalase; D009195:Peroxidase