Source:http://linkedlifedata.com/resource/pubmed/id/12366839
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
1
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| pubmed:dateCreated |
2002-10-7
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| pubmed:abstractText |
Effectors of the innate immune system, the anti-bacterial peptides, have pivotal roles in preventing infection at epithelial surfaces. Here we show that proteinases of the significant human pathogens Pseudomonas aeruginosa, Enterococcus faecalis, Proteus mirabilis and Streptococcus pyogenes, degrade the antibacterial peptide LL-37. Analysis by mass spectrometry of fragments generated by P. aeruginosa elastase in vitro revealed that the initial cleavages occurred at Asn-Leu and Asp-Phe, followed by two breaks at Arg-Ile, thus inactivating the peptide. Proteinases of the other pathogens also degraded LL-37 as determined by SDS-PAGE. Ex vivo, P. aeruginosa elastase induced LL-37 degradation in human wound fluid, leading to enhanced bacterial survival. The degradation was blocked by the metalloproteinase inhibitors GM6001 and 1, 10-phenantroline (both of which inhibited P. aeruginosa elastase, P. mirabilis proteinase, and E. faecalis gelatinase), or the inhibitor E64 (which inhibited S. pyogenes cysteine proteinase). Additional experiments demonstrated that dermatan sulphate and disaccharides of the structure [DeltaUA(2S)-GalNAc(4,6S)], or sucroseoctasulphate, inhibited the degradation of LL-37. The results indicate that proteolytic degradation of LL-37 is a common virulence mechanism and that molecules which block this degradation could have therapeutic potential.
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| pubmed:language |
eng
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| pubmed:journal | |
| pubmed:citationSubset |
IM
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| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Antimicrobial Cationic Peptides,
http://linkedlifedata.com/resource/pubmed/chemical/CAP18 lipopolysaccharide-binding...,
http://linkedlifedata.com/resource/pubmed/chemical/Cathelicidins,
http://linkedlifedata.com/resource/pubmed/chemical/Disaccharides,
http://linkedlifedata.com/resource/pubmed/chemical/Endopeptidases,
http://linkedlifedata.com/resource/pubmed/chemical/Glycosaminoglycans,
http://linkedlifedata.com/resource/pubmed/chemical/Pancreatic Elastase,
http://linkedlifedata.com/resource/pubmed/chemical/Protease Inhibitors,
http://linkedlifedata.com/resource/pubmed/chemical/Sulfur,
http://linkedlifedata.com/resource/pubmed/chemical/cathelicidin antimicrobial peptide
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| pubmed:status |
MEDLINE
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| pubmed:month |
Oct
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| pubmed:issn |
0950-382X
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| pubmed:author | |
| pubmed:issnType |
Print
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| pubmed:volume |
46
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| pubmed:owner |
NLM
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| pubmed:authorsComplete |
Y
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| pubmed:pagination |
157-68
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| pubmed:dateRevised |
2010-11-18
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| pubmed:meshHeading |
pubmed-meshheading:12366839-Amino Acid Sequence,
pubmed-meshheading:12366839-Antimicrobial Cationic Peptides,
pubmed-meshheading:12366839-Bacteria,
pubmed-meshheading:12366839-Bacterial Infections,
pubmed-meshheading:12366839-Cathelicidins,
pubmed-meshheading:12366839-Disaccharides,
pubmed-meshheading:12366839-Endopeptidases,
pubmed-meshheading:12366839-Glycosaminoglycans,
pubmed-meshheading:12366839-Humans,
pubmed-meshheading:12366839-Mass Spectrometry,
pubmed-meshheading:12366839-Microbial Sensitivity Tests,
pubmed-meshheading:12366839-Molecular Sequence Data,
pubmed-meshheading:12366839-Neutrophils,
pubmed-meshheading:12366839-Pancreatic Elastase,
pubmed-meshheading:12366839-Protease Inhibitors,
pubmed-meshheading:12366839-Pseudomonas aeruginosa,
pubmed-meshheading:12366839-Sulfur,
pubmed-meshheading:12366839-Virulence,
pubmed-meshheading:12366839-Wound Infection
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| pubmed:year |
2002
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| pubmed:articleTitle |
Proteinases of common pathogenic bacteria degrade and inactivate the antibacterial peptide LL-37.
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| pubmed:affiliation |
Section for Dermatology, Department of Medical Microbiology, Dermatology and Infection, Biomedical Center, B14, Tornavägen 10, S-22184 Lund, Sweden. artur.schmidtchen@derm.lu.se
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| pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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