Scavenger Receptors May Regulate Nitric Oxide Production from Macrophages Stimulated by LPS

The effects of scavenger receptor (SR) ligands on nitric oxide (NO) production were investigated using mouse peritoneal macrophages stimulated by LPS. Pretreatment of macrophages with oxidized LDL, heparin, maleylated BSA, or liposomes composed of phosphatidylserine (PS-liposomes) inhibited NO produ...

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Bibliographic Details
Published in:Biochemical and biophysical research communications 1997-08, Vol.237 (3), p.601-605
Main Authors: Matsuno, Ryozo, Aramaki, Yukihiko, Arima, Hidetoshi, Tsuchiya, Seishi
Format: Article
Language:English
Subjects:
Animals
Cells, Cultured
Chloroquine - pharmacology
Heparin - pharmacology
Lipopolysaccharides - pharmacology
Lipoproteins, LDL - pharmacology
Lysosomes - drug effects
Lysosomes - physiology
Macrophages, Peritoneal - drug effects
Macrophages, Peritoneal - physiology
Male
Maleates - pharmacology
Membrane Proteins
Mice
Mice, Inbred C3H
Nitric Oxide - biosynthesis
Nitric Oxide Synthase - biosynthesis
Nitrites - analysis
Phosphatidylserines
Phosphorylation
Phosphotyrosine - metabolism
Receptors, Immunologic - drug effects
Receptors, Immunologic - physiology
Receptors, Lipoprotein
Receptors, Scavenger
Scavenger Receptors, Class B
Serum Albumin, Bovine - pharmacology
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Summary:The effects of scavenger receptor (SR) ligands on nitric oxide (NO) production were investigated using mouse peritoneal macrophages stimulated by LPS. Pretreatment of macrophages with oxidized LDL, heparin, maleylated BSA, or liposomes composed of phosphatidylserine (PS-liposomes) inhibited NO production, but native LDL, acetyl LDL dextran sulfate, did not. Immunoblotting analysis suggests that the inhibitory effects could be a result of the inhibition of inducible NO synthase (iNOS) induction, but not enzyme activity. Further, tyrosine phosphorylation of a 41 kDa protein was also inhibited by OxLDL, heparin, maleylated BSA, and PS-liposomes. Chloroquine did not affect the extent of inhibition of NO production induced by these ligands, suggesting that the binding of these ligands to SR generates a signal(s) which is involved in the inhibition of NO production from macrophages stimulated by LPS. SR, which has an affinity to these ligands, may strictly regulate NO production from macrophages, and this inhibitory effect may be due to the inhibition of LPS-induced tyrosine phosphorylation of 41 kDa protein.
ISSN:0006-291X
1090-2104
DOI:10.1006/bbrc.1997.7195