Lipopolysaccharide-inactivating activity of neutrophils is due to lactoferrin
| Autor: | Karen M. Pabst, Michael J. Pabst, Yoshitomi Aida, Demin Wang |
|---|---|
| Rok vydání: | 1995 |
| Předmět: |
Lipopolysaccharides
Lysis biology Lipopolysaccharide Superoxide Lactoferrin Neutrophils Iron Immunology Cell Biology biology.organism_classification Peripheral blood mononuclear cell Immunoglobulin G Monocytes Microbiology Culture Media chemistry.chemical_compound chemistry Limulus Time course biology.protein Immunology and Allergy Humans lipids (amino acids peptides and proteins) |
| Zdroj: | Journal of leukocyte biology. 57(6) |
| ISSN: | 0741-5400 |
| Popis: | Neutrophils can inactivate lipopolysaccharide (LPS), thereby blocking the ability of LPS to prime fresh neutrophils for enhanced fMLP-triggered release of superoxide. Here we show that inactivation of LPS by neutrophils was primarily due to lactoferrin. A time course for inactivating LPS showed that neutrophils (5 million/ml) took 30 min to inactivate 10 ng/ml LPS. Mononuclear cells could not inactivate LPS under the same conditions. Experiments with radioactive LPS showed that inactivated LPS remained in the medium and was not taken up or destroyed by the neutrophils during inactivation. Inactivated IPS still gelled Limulus lysate and primed monocytes. Cell-free medium from neutrophil suspensions also inactivated LPS. A single LPS-inactivating factor was purified from medium by heparin-agarose chromatography. SDS-PAGE showed a single band at 80 kDa, which was identified as lactoferrin by immunoblotting. Antilactoferrin immunoglobulin G removed the LPS-inactivating activity from purified lactoferrin and cell-free medium. Surprisingly, even purified neutrophil lactoferrin required 30 min to inactivate LPS, indicating inherently slow binding of lactoferrin to LPS J. Leukoc. Biol. 57: 865–874; 1995. |
| Databáze: | OpenAIRE |
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