Synthetic peptides representing the N-terminal segment of surfactant protein C modulate LPS-stimulated TNF-α production by macrophages
| Autor: | Jesús Pérez-Gil, Ignacio Garcia-Verdugo, Richard Chaby, Jean Kanellopoulos, Elvira Garcia de Paco, Quentin Espinassous, Azucena González-Horta, Monique Synguelakis, Luis Rivas |
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| Rok vydání: | 2009 |
| Předmět: |
Lipopolysaccharides
Lipopolysaccharide Swine CD14 Molecular Sequence Data Immunology Lipopolysaccharide Receptors Inflammation Microbiology Cell Line Mice chemistry.chemical_compound Pulmonary surfactant medicine Animals Amino Acid Sequence Molecular Biology Tumor Necrosis Factor-alpha Chemistry Aqueous two-phase system Pulmonary Surfactants Surfactant protein C Cell Biology Pulmonary Surfactant-Associated Protein C Infectious Diseases Membrane Biochemistry Liposomes Macrophages Peritoneal Intercellular Signaling Peptides and Proteins lipids (amino acids peptides and proteins) Tumor necrosis factor alpha medicine.symptom Peptides |
| Zdroj: | Innate Immunity. 15:53-62 |
| ISSN: | 1753-4267 1753-4259 |
| DOI: | 10.1177/1753425908100500 |
| Popis: | Surfactant protein C (SP-C) consists of a hydrophobic α-helix inserted in pulmonary surfactant membranes, and a more polar N-terminal palmitoylated segment exposed to the aqueous phase. Previously, we showed that SP-C inserted in lipid vesicles interacts with bacterial lipopolysaccharide (LPS) and reduces LPS-elicited responses. As the N-terminal segment of SP-C was the most likely region responsible for these effects, a set of synthetic analogs of this stretch (SPC(1-13)) were studied. Binding studies showed that SPC(1-13)binds LPS to the same extent as porcine SP-C under lipid-free conditions. In the absence of serum, both, palmitoylated and non-palmitoylated analogs enhanced the binding of tritiated LPS to macrophages as well as the LPS-induced production of TNF-α by these cells. These effects were reversed in the presence of serum; the analogs reduced the production of TNF-α in LPS-stimulated macrophages, probably by interfering with the formation of LPS/CD14/LBP complexes as suggested by analysis of the fluorescence emitted by a FITC derivative of Re-LPS. Our data indicate that water-soluble analogs of the N-terminal segment of SP-C can reduce LPS effects in the presence of serum, and thus might help in the design of new derivatives to fight endotoxic shock and pro-inflammatory events. |
| Databáze: | OpenAIRE |
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