| Apolipoprotein CI enhances the biological response to LPS via the CD14/TLR4 pathway by LPS-binding elements in both its N- and C-terminal helix. | |
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MedLine Citation:
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PMID: 20335569 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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Timely sensing of lipopolysaccharide (LPS) is critical for the host to fight invading Gram-negative bacteria. We recently showed that apolipoprotein CI (apoCI) (apoCI1-57) avidly binds to LPS, involving an LPS-binding motif (apoCI48-54), and thereby enhances the LPS-induced inflammatory response. Our current aim was to further elucidate the structure and function relationship of apoCI with respect to its LPS-modulating characteristics and to unravel the mechanism by which apoCI enhances the biological activity of LPS. We designed and generated N- and C-terminal apoCI-derived peptides containing varying numbers of alternating cationic/hydrophobic motifs. ApoCI1-38, apoCI1-30, and apoCI35-57 were able to bind LPS, whereas apoCI1-23 and apoCI46-57 did not bind LPS. In line with their LPS-binding characteristics, apoCI1-38, apoCI1-30, and apoCI35-57 prolonged the serum residence of 125I-LPS by reducing its association with the liver. Accordingly, both apoCI1-30 and apoCI35-57 enhanced the LPS-induced TNFalpha response in vitro (RAW 264.7 macrophages) and in vivo (C57Bl/6 mice). Additional in vitro studies showed that the stimulating effect of apoCI on the LPS response resembles that of LPS-binding protein (LBP) and depends on CD14/ Toll-like receptor 4 signaling. We conclude that apoCI contains structural elements in both its N-terminal and C-terminal helix to bind LPS and to enhance the proinflammatory response toward LPS via a mechanism similar to LBP. |
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Authors:
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Jimmy F P Berbée; Claudia P Coomans; Marit Westerterp; Johannes A Romijn; Louis M Havekes; Patrick C N Rensen |
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Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't Date: 2010-03-24 |
Journal Detail:
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Title: Journal of lipid research Volume: 51 ISSN: 0022-2275 ISO Abbreviation: J. Lipid Res. Publication Date: 2010 Jul |
Date Detail:
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Created Date: 2010-06-11 Completed Date: 2010-10-18 Revised Date: 2011-08-01 |
Medline Journal Info:
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Nlm Unique ID: 0376606 Medline TA: J Lipid Res Country: United States |
Other Details:
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Languages: eng Pagination: 1943-52 Citation Subset: IM |
Affiliation:
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Department of General Internal Medicine, Endocrinology and Metabolic Diseases, Leiden University Medical Center, 2300 RC Leiden, The Netherlands. J.F.P.Berbee@lumc.nl |
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| MeSH Terms | |
Descriptor/Qualifier:
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Amino Acid Sequence Animals Antigens, CD14 / immunology* Apolipoprotein C-I / chemistry*, genetics, immunology* Cell Line Lipopolysaccharides* / immunology, pharmacology Macrophages / cytology, drug effects, immunology Mice Mice, Inbred C57BL Models, Molecular Molecular Sequence Data Peptides / chemistry, genetics, immunology Protein Binding Protein Structure, Secondary* Sequence Alignment Signal Transduction / immunology* Toll-Like Receptor 4 / immunology* Tumor Necrosis Factor-alpha / immunology |
| Chemical | |
Reg. No./Substance:
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0/Antigens, CD14; 0/Apolipoprotein C-I; 0/Lipopolysaccharides; 0/Peptides; 0/Toll-Like Receptor 4; 0/Tumor Necrosis Factor-alpha |
| Comments/Corrections | |
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