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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
31
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pubmed:dateCreated |
2003-7-28
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pubmed:abstractText |
The human cathelicidin, hCAP-18, is expressed both in neutrophils and in epithelial cells. hCAP-18 is processed to the antimicrobial peptide LL-37 by proteinase 3 in neutrophils. hCAP-18 is highly expressed in the epididymis with a subsequent high concentration in seminal plasma where the protein is present in its unprocessed and antimicrobially inactive form. We report here that hCAP-18 in seminal plasma is processed to generate a 38-amino acid antimicrobial peptide ALL-38 by the prostate-derived protease gastricsin when incubated at a pH corresponding to the vaginal pH. In accordance with this, seminal plasma derived hCAP-18 was found in its processed form in the vagina following sexual intercourse. The antimicrobial activity of ALL-38 against a variety of microorganisms tested is equal to that of LL-37. This enzymatic activation of a proantimicrobial substance in seminal plasma following exposure to the vaginal milieu represents a novel mechanism to prevent infection following sexual intercourse.
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pubmed:commentsCorrections |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Anti-Bacterial Agents,
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/Pepsin A,
http://linkedlifedata.com/resource/pubmed/chemical/Pepstatins,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Fragments,
http://linkedlifedata.com/resource/pubmed/chemical/Protease Inhibitors,
http://linkedlifedata.com/resource/pubmed/chemical/cathelicidin antimicrobial peptide,
http://linkedlifedata.com/resource/pubmed/chemical/gastricsin,
http://linkedlifedata.com/resource/pubmed/chemical/pepsinostreptin,
http://linkedlifedata.com/resource/pubmed/chemical/pepstatin
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
0021-9258
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
278
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
28540-6
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pubmed:dateRevised |
2010-11-18
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pubmed:meshHeading |
pubmed-meshheading:12759353-Amino Acid Sequence,
pubmed-meshheading:12759353-Anti-Bacterial Agents,
pubmed-meshheading:12759353-Antimicrobial Cationic Peptides,
pubmed-meshheading:12759353-Bacillus megaterium,
pubmed-meshheading:12759353-Body Fluids,
pubmed-meshheading:12759353-Cathelicidins,
pubmed-meshheading:12759353-Chemical Precipitation,
pubmed-meshheading:12759353-Coitus,
pubmed-meshheading:12759353-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:12759353-Escherichia coli,
pubmed-meshheading:12759353-Female,
pubmed-meshheading:12759353-Humans,
pubmed-meshheading:12759353-Hydrogen-Ion Concentration,
pubmed-meshheading:12759353-Male,
pubmed-meshheading:12759353-Molecular Sequence Data,
pubmed-meshheading:12759353-Pepsin A,
pubmed-meshheading:12759353-Pepstatins,
pubmed-meshheading:12759353-Peptide Fragments,
pubmed-meshheading:12759353-Protease Inhibitors,
pubmed-meshheading:12759353-Semen,
pubmed-meshheading:12759353-Staphylococcus aureus,
pubmed-meshheading:12759353-Vagina
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pubmed:year |
2003
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pubmed:articleTitle |
Processing of seminal plasma hCAP-18 to ALL-38 by gastricsin: a novel mechanism of generating antimicrobial peptides in vagina.
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pubmed:affiliation |
Granulocyte Research Laboratory, the Department of Hematology, Copenhagen University Hospital, Rigshospitalet, DK-2100 Copenhagen, Denmark. sorensen@ucla.edu
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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