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Activated human neutrophils rapidly break down nitric oxide
Author(s) -
McBride Alan G,
Brown Guy C
Publication year - 1997
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(97)01284-2
Subject(s) - peroxynitrite , respiratory burst , nitric oxide , superoxide , chemistry , superoxide dismutase , n formylmethionine leucyl phenylalanine , biochemistry , chemotaxis , reactive oxygen species , neutrophile , nadph oxidase , phorbol , protein kinase c , in vitro , oxidative stress , receptor , signal transduction , enzyme , organic chemistry
Isolated human neutrophils produced no detectable (<10 nM) nitric oxide (NO) before or after activation with phorbol 12‐myristate 13‐acetate (PMA) or a chemotactic peptide, N ‐formyl‐ l ‐methionyl‐ l ‐leucyl‐ l ‐phenylalanine. Physiological levels of NO (1 μM) added before or after neutrophil activation had no effect on their respiratory burst oxygen consumption. Neutrophils activated with PMA caused very rapid breakdown of exogenously added NO. NO breakdown rates recorded at 250 nM NO were 0.09±0.02 and 3.77±0.23 nmol NO/min/10 6 cells ( n =3) before and after activation respectively and addition of copper‐zinc superoxide dismutase during activation significantly decreased this rate (1.06±0.09 nmol NO/min/10 6 cells ( n =3)), suggesting that superoxide (O − 2 ) production was mainly responsible for the NO breakdown. These results suggest that activation of human neutrophils in vivo will dramatically decrease surrounding NO levels, potentially causing vasoconstriction, platelet aggregation and adhesion and peroxynitrite (ONOO − ) formation.