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rdf:type |
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lifeskim:mentions |
umls-concept:C0007634,
umls-concept:C0015576,
umls-concept:C0017262,
umls-concept:C0023810,
umls-concept:C0030956,
umls-concept:C0175697,
umls-concept:C0185117,
umls-concept:C0279516,
umls-concept:C0332206,
umls-concept:C0671062,
umls-concept:C1167622,
umls-concept:C1367477,
umls-concept:C1413106,
umls-concept:C1456820,
umls-concept:C2697656,
umls-concept:C2911684
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pubmed:issue |
6
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pubmed:dateCreated |
2001-9-6
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pubmed:abstractText |
Mammalian myeloid and epithelial cells express several kinds of antibacterial peptides (alpha-/beta-defensins and cathelicidins) that contribute to the innate host defense by killing invading micro-organisms. In this study we evaluated the LPS-neutralizing activities of cathelicidin peptides human CAP18 (cationic antibacterial proteins of 18 kDa) and guinea pig CAP11 using the CD14(+) murine macrophage cell line RAW264.7 and the murine endotoxin shock model. Flow cytometric analysis revealed that CAP18 and CAP11 inhibited the binding of FITC-conjugated LPS to RAW264.7 cells. Likewise, Northern and Western blot analyses indicated that CAP18 and CAP11 suppressed LPS-induced TNF-alpha mRNA and protein expression by RAW264.7 cells. Interestingly, CAP18 and CAP11 possessed LPS-binding activities, and they strongly suppressed the interaction of LPS with LPS binding protein that mediates the transport of LPS to CD14 to facilitate the activation of CD14(+) cells by LPS. Moreover, when CAP18 and CAP11 were preincubated with RAW264.7 cells, they bound to the cell surface CD14 and inhibited the binding of FITC-LPS to the cells. Furthermore, in the murine endotoxin shock model, CAP18 or CAP11 administration inhibited the binding of LPS to CD14(+) cells (peritoneal macrophages) and suppressed LPS-induced TNF-alpha expression by these cells. Together these observations indicate that cathelicidin peptides CAP18 and CAP11 probably exert protective actions against endotoxin shock by blocking the binding of LPS to CD14(+) cells, thereby suppressing the production of cytokines by these cells via their potent binding activities for LPS and CD14.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
AIM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Acute-Phase Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Anti-Bacterial Agents,
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, CD14,
http://linkedlifedata.com/resource/pubmed/chemical/Antimicrobial Cationic Peptides,
http://linkedlifedata.com/resource/pubmed/chemical/CAP18 lipopolysaccharide-binding...,
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Cathelicidins,
http://linkedlifedata.com/resource/pubmed/chemical/Lipopolysaccharides,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Glycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Prodrugs,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger,
http://linkedlifedata.com/resource/pubmed/chemical/Tumor Necrosis Factor-alpha,
http://linkedlifedata.com/resource/pubmed/chemical/cathelicidin antimicrobial peptide,
http://linkedlifedata.com/resource/pubmed/chemical/lipopolysaccharide-binding protein
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
0022-1767
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
167
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
3329-38
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pubmed:dateRevised |
2010-11-18
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pubmed:meshHeading |
pubmed-meshheading:11544322-Acute-Phase Proteins,
pubmed-meshheading:11544322-Amino Acid Sequence,
pubmed-meshheading:11544322-Animals,
pubmed-meshheading:11544322-Anti-Bacterial Agents,
pubmed-meshheading:11544322-Antigens, CD14,
pubmed-meshheading:11544322-Antimicrobial Cationic Peptides,
pubmed-meshheading:11544322-Carrier Proteins,
pubmed-meshheading:11544322-Cathelicidins,
pubmed-meshheading:11544322-Cell Line,
pubmed-meshheading:11544322-Depression, Chemical,
pubmed-meshheading:11544322-Drug Evaluation, Preclinical,
pubmed-meshheading:11544322-Gene Expression Regulation,
pubmed-meshheading:11544322-Guinea Pigs,
pubmed-meshheading:11544322-Humans,
pubmed-meshheading:11544322-Lipopolysaccharides,
pubmed-meshheading:11544322-Macrophages,
pubmed-meshheading:11544322-Macrophages, Peritoneal,
pubmed-meshheading:11544322-Male,
pubmed-meshheading:11544322-Membrane Glycoproteins,
pubmed-meshheading:11544322-Mice,
pubmed-meshheading:11544322-Mice, Inbred C57BL,
pubmed-meshheading:11544322-Molecular Sequence Data,
pubmed-meshheading:11544322-Prodrugs,
pubmed-meshheading:11544322-Protein Binding,
pubmed-meshheading:11544322-RNA, Messenger,
pubmed-meshheading:11544322-Shock, Septic,
pubmed-meshheading:11544322-Tumor Necrosis Factor-alpha
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pubmed:year |
2001
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pubmed:articleTitle |
Cathelicidin family of antibacterial peptides CAP18 and CAP11 inhibit the expression of TNF-alpha by blocking the binding of LPS to CD14(+) cells.
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pubmed:affiliation |
Department of Biochemistry, Juntendo University School of Medicine, Tokyo, Japan. nagaokai@med.juntendo.ac.jp
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
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