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by Nitric Oxide in Monocytes/Macrophages Down-Regulates p47phox and Attenuates the Respiratory Burst1
Institute of Cell Biology, University of Kaiserslautern, Kaiserslautern, Germany
NO appears as an important determinant in auto and
paracrine macrophage function. We hypothesized that NO switches
monocyte/macrophage function from a pro- to an anti-inflammatory
phenotype by activating anti-inflammatory properties of the
peroxisome proliferator-activated receptor (PPAR)
. NO-releasing
compounds (100 µM S-nitrosoglutathione or 50 µM
spermine-NONOate) as well as inducible NO synthase induction provoked
activation of PPAR. This was proven by EMSAs, with the notion that
supershift analysis pointed to the involvement of PPAR. PCR analysis
ruled out induction of PPAR mRNA as a result of NO supplementation.
Reporter assays, with a construct containing a triple PPAR response
element in front of a thymidine kinase minimal promoter driving the
luciferase gene, were positive in response to NO delivery. DNA binding
capacity as well as the transactivating capability of PPAR were
attenuated by addition of the antioxidant
N-acetyl-cysteine or in the presence of the NO scavenger
2-phenyl-4,4,5,6-tetramethyl-imidazoline-1-oxyl 3-oxide. Having
established that NO but not lipophilic cyclic GMP analogs activated
PPAR, we verified potential anti-inflammatory consequences. The
oxidative burst of macrophages, evoked by phorbol ester, was attenuated
in association with NO-elicited PPAR activation. A cause-effect
relationship was demonstrated when PPAR response element decoy
oligonucleotides, supplied in front of NO delivery, allowed to regain
an oxidative response. PPAR-mediated down-regulation of p47
phagocyte oxidase, a component of the NAD(P)H oxidase system, was
identified as one molecular mechanism causing inhibition of superoxide
radical formation. We conclude that NO participates in controlling the
pro- vs anti-inflammatory phenotype of macrophages by modulating
PPAR.
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