Protective role of phospholipid oxidation products in endotoxin-induced tissue damage

Nature

Volumn 419, Issue 6902, 2002, Pages 77-81

  Bochkov, Valery N ^a   Kadl, Alexandra ^a   Huber, Joakim ^a   Gruber, Florian ^a   Binder, Bernd R ^a   Leitinger, Norbert ^a  

^a UNIVERSITY OF VIENNA   (Austria)

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIA; ENZYMES; OXIDATION; PHOSPHOLIPIDS; POLYSACCHARIDES; TISSUE;

NEUTROPHILS;

BIOCHEMISTRY;

CD14 ANTIGEN; ENDOTOXIN; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; INTERLEUKIN 1BETA; LIPOPOLYSACCHARIDE; LIPOPOLYSACCHARIDE BINDING PROTEIN; MITOGEN ACTIVATED PROTEIN KINASE; PHOSPHOLIPID; REACTIVE OXYGEN METABOLITE; TOLL LIKE RECEPTOR 4; TUMOR NECROSIS FACTOR ALPHA;

MEDICINE;

ARTICLE; CONTROLLED STUDY; FEEDBACK SYSTEM; GENE EXPRESSION; HUMAN; HUMAN CELL; LIPID OXIDATION; PATHOGENESIS; PRIORITY JOURNAL; PROTEIN INTERACTION; SIGNAL TRANSDUCTION; TISSUE INJURY;

ACUTE-PHASE PROTEINS; ANIMALS; ANTIGENS, CD14; CARRIER PROTEINS; CELL ADHESION MOLECULES; CELL LINE; ENDOTHELIUM, VASCULAR; ENZYME-LINKED IMMUNOSORBENT ASSAY; FEMALE; GRAM-NEGATIVE BACTERIA; HUMANS; IMMUNITY, NATURAL; INFLAMMATION; INTERLEUKIN-1; LIPOPOLYSACCHARIDES; MEMBRANE GLYCOPROTEINS; MICE; MITOGEN-ACTIVATED PROTEIN KINASES; NF-KAPPA B; OXIDATION-REDUCTION; P38 MITOGEN-ACTIVATED PROTEIN KINASES; PERITONEUM; PHOSPHOLIPIDS; RNA, MESSENGER; SHOCK, SEPTIC; SIGNAL TRANSDUCTION; SKIN; TUMOR NECROSIS FACTOR-ALPHA;

BACTERIA (MICROORGANISMS); NEGIBACTERIA;

EID: 0037026527     PISSN: 00280836     EISSN: None     Source Type: Journal    
DOI: 10.1038/nature01023     Document Type: Article

References (26)

1. Toll-like receptors and innate immunity
2. Toll-like receptors in the induction of the innate immune response
3. Toll-like receptor-4 mediates lipopolysaccharide-induced signal transduction
4. Tir4: Central component of the sole mammalian LPS sensor
5. Inside the neutrophil phagosome: Oxidants, myeloperoxidase, and bacterial killing
6. Defects in leukocyte-mediated initiation of lipid peroxidation in plasma as studied in myeloperoxidase deficient subjects: Systematic identification of multiple endogenous diffusible substrates for myeloperoxidase in plasma
7. Atherosclerosis
8. Structurally similar oxidized phospholipids differentially regulate endothelial binding of monocytes and neutrophils
9. Structurally identification by mass spectrometry of oxidized phospholipids in minimally oxidized low density lipoprotein that induce monocyte/endothelial interactions and evidence for their presence in vivo
10. ++/NFAT
11. Lactoferrin inhibits the endotoxin interaction with CD14 by competition with the lipopolysaccharide-binding protein
12. In vitro inactivation of bacterial endotoxin by human lipoproteins and apolipoproteins
13. Plasma CD14 decreases monocyte responses to LPS by transferring cell-bound LPS to plasma lipoproteins
14. LipopoLysaccharide-binding protein and soluble CD14 transfer lipopolysaccharide to phospholipid bilayers: Preferential interaction with particular classes of lipid
15. Molecular mapping and detoxification of the lipid A binding site by synthetic peptides
16. E5531, a pure endotoxin antagonist of high potency
17. Lipid A-like molecules that antagonize the effects of endotoxins on human monocytes
18. Salmonella-type heptaacylated lipid A is inactive and acts as an antagonist of lipopolysaccharide action on human line cells
19. Soluble CD14 participates in the response of cells to lipopolysaccharide
20. Lipopolysaccharide binding protein participation in cellular activation by LPS
21. Soluble CD 14 mediates efflux of phospholipids from cells
22. Lipopolysaccharide binding protein and soluble CD 14 catalyze exchange of phospholipids
23. Possible new role for NF-κB in the resolution of inflammation
24. Helicobacter pylori and Porphyromonas gingivalis lipopolysaccharides are poorly transferred to recombinant soluble CD14
25. Cutting edge: Cationic antimicrobial peptides block the binding of lipopolysaccharide (LPS) to LPS binding protein
26. Measurement of cutaneous inflammation: Estimation of neutrophil content with an enzyme marker