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Lactoferrin works as a new LPS-binding protein in inflammatory activation of macrophages.
- Source :
-
International immunopharmacology [Int Immunopharmacol] 2004 Sep; Vol. 4 (9), pp. 1187-99. - Publication Year :
- 2004
-
Abstract
- Though lactoferrin (LF) is a glycoprotein that is involved in immunomodulation, its action mechanism has not been fully elucidated. Previous studies have suggested that lipopolysaccharide (LPS) activity is inhibited by direct binding between LPS and LF. However, here we show that when LPS and purified LF was mixed, and formed a complex (termed as LF-LPS), it was found to induce production of inflammatory mediators in macrophages to some extent, rather than inhibit LPS activity. Moreover, when macrophages were pretreated with LF-LPS, cells were rendered a tolerant state to LPS challenge. These macrophage-activating effects were mediated by Toll-like receptor 4 (TLR4)-NF-kappaB pathway. Comparative studies with C3H/HeN and C3H/HeJ mice demonstrated the strong dependency of the LF-LPS signal on TLR4. These findings suggest that the immunomodulatory properties of LF could be due, in part, to LPS binding.
- Subjects :
- Animals
Blotting, Western
Cells, Cultured
Electrophoretic Mobility Shift Assay
Immunoassay
Lipopolysaccharides pharmacology
Membrane Glycoproteins drug effects
Membrane Glycoproteins metabolism
Mice
Mice, Inbred C3H
NF-kappa B metabolism
Nitrites analysis
Nitrites metabolism
Receptors, Cell Surface drug effects
Receptors, Cell Surface metabolism
Reverse Transcriptase Polymerase Chain Reaction
Signal Transduction drug effects
Toll-Like Receptor 4
Toll-Like Receptors
Tumor Necrosis Factor-alpha biosynthesis
Acute-Phase Proteins pharmacology
Carrier Proteins pharmacology
Inflammation pathology
Lactoferrin pharmacology
Macrophage Activation drug effects
Membrane Glycoproteins pharmacology
Subjects
Details
- Language :
- English
- ISSN :
- 1567-5769
- Volume :
- 4
- Issue :
- 9
- Database :
- MEDLINE
- Journal :
- International immunopharmacology
- Publication Type :
- Academic Journal
- Accession number :
- 15251114
- Full Text :
- https://doi.org/10.1016/j.intimp.2004.05.009