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Peroxyl radicals from tumor promoter organic hydroperoxides induced by human myeloperoxidase and human neutrophils

Conference · · FASEB Journal (Federation of American Societies for Experimental Biology); (United States)
OSTI ID:6006362
; ;  [1]
  1. National Inst. of Health, Research Triangle Park, NC (United States) Univ. of North Carolina, Chapel Hill (United States)

The decomposition of tumor promotor organic hydroperoxides as catalyzed by human myeloperoxidase (MPO) and human neutrophils (PMN) was investigated by electron paramagnetic resonance. Peroxyl, alkoxyl and carbon-centered free radicals were successfully trapped by spin trap 5,5-dimethyl-1-pyrroline N-oxide (DMPO) for both MPO and PMN systems. The classical peroxidase mechanism is proposed to describe the formation of peroxyl radicals. The authors propose that the tert-butyl peroxyl radical reacts to form tert-butyl alkoxyl radical. {beta}-Scission of tert-butyl alkoxyl radical leads to the formation of methyl radical. In the case of ethyl hydroperoxide, ethyloxyl was not detected with DMPO; rather, {alpha}-hydroxyethyl was trapped by another spin trap, tert-nitrosopropane. The authors propose that ethyloxyl radical rapidly undergoes internal hydrogen atom transfer resulting in the formation of {alpha}-hydroxyethyl radical. The addition of azide (MPO inhibitor) and rabbit antisera IgG fraction for human MPO resulted in the inhibition of free radical formation in both MPO/ and PMN/ organic hydroperoxide systems. The results imply that the MPO of PMN form oxygen-centered free radicals from organic hydroperoxides inside these cells.

OSTI ID:
6006362
Report Number(s):
CONF-9104107--
Journal Information:
FASEB Journal (Federation of American Societies for Experimental Biology); (United States), Journal Name: FASEB Journal (Federation of American Societies for Experimental Biology); (United States) Vol. 4:3; ISSN FAJOE; ISSN 0892-6638
Country of Publication:
United States
Language:
English