Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
2003-7-15
pubmed:abstractText
Antimicrobial peptides and proteins are effector molecules in the protection of epithelial surfaces. We have evaluated the presence of antimicrobial peptides/proteins that can participate in human colonic defence against microbes. A peptide/protein extract of normal human colon mucosa was found to be active against Gram-positive bacteria, Gram-negative bacteria, and fungi. Four polypeptides with antimicrobial activity were isolated from this material and they were identified by N-terminal amino acid sequence analysis as ubiquicidin, histone H2B, eosinophil cationic protein, and phospholipase A(2) (PLA(2)). Using immunodetection and mass spectrometry, LL-37, HNP1-3, and HBD-1 were also identified. Combined, these results indicate that the colon mucosa is protected by a complex mixture of polypeptides, able to kill invading microbes and working in synergy as a barrier against bacterial invasion.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Anti-Infective Agents, http://linkedlifedata.com/resource/pubmed/chemical/Antimicrobial Cationic Peptides, http://linkedlifedata.com/resource/pubmed/chemical/Blood Proteins, http://linkedlifedata.com/resource/pubmed/chemical/CAP18 lipopolysaccharide-binding..., http://linkedlifedata.com/resource/pubmed/chemical/Cathelicidins, http://linkedlifedata.com/resource/pubmed/chemical/DEFB1 protein, human, http://linkedlifedata.com/resource/pubmed/chemical/Defensins, http://linkedlifedata.com/resource/pubmed/chemical/Eosinophil Granule Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Histones, http://linkedlifedata.com/resource/pubmed/chemical/Peptides, http://linkedlifedata.com/resource/pubmed/chemical/Phospholipases A, http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger, http://linkedlifedata.com/resource/pubmed/chemical/Ribonucleases, http://linkedlifedata.com/resource/pubmed/chemical/Ribosomal Proteins, http://linkedlifedata.com/resource/pubmed/chemical/alpha-Defensins, http://linkedlifedata.com/resource/pubmed/chemical/beta-Defensins, http://linkedlifedata.com/resource/pubmed/chemical/cathelicidin antimicrobial peptide, http://linkedlifedata.com/resource/pubmed/chemical/human neutrophil peptide 1, http://linkedlifedata.com/resource/pubmed/chemical/ribosomal protein S30
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0196-9781
pubmed:author
pubmed:issnType
Print
pubmed:volume
24
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
523-30
pubmed:dateRevised
2010-11-18
pubmed:meshHeading
pubmed-meshheading:12860195-Anti-Infective Agents, pubmed-meshheading:12860195-Antimicrobial Cationic Peptides, pubmed-meshheading:12860195-Bacteria, pubmed-meshheading:12860195-Blood Proteins, pubmed-meshheading:12860195-Blotting, Southern, pubmed-meshheading:12860195-Blotting, Western, pubmed-meshheading:12860195-Cathelicidins, pubmed-meshheading:12860195-Chromatography, High Pressure Liquid, pubmed-meshheading:12860195-Colon, pubmed-meshheading:12860195-Defensins, pubmed-meshheading:12860195-Electrophoresis, Polyacrylamide Gel, pubmed-meshheading:12860195-Eosinophil Granule Proteins, pubmed-meshheading:12860195-Histones, pubmed-meshheading:12860195-Humans, pubmed-meshheading:12860195-Mass Spectrometry, pubmed-meshheading:12860195-Mucous Membrane, pubmed-meshheading:12860195-Peptides, pubmed-meshheading:12860195-Phospholipases A, pubmed-meshheading:12860195-Protein Structure, Tertiary, pubmed-meshheading:12860195-RNA, Messenger, pubmed-meshheading:12860195-Reverse Transcriptase Polymerase Chain Reaction, pubmed-meshheading:12860195-Ribonucleases, pubmed-meshheading:12860195-Ribosomal Proteins, pubmed-meshheading:12860195-Time Factors, pubmed-meshheading:12860195-alpha-Defensins, pubmed-meshheading:12860195-beta-Defensins
pubmed:year
2003
pubmed:articleTitle
Antimicrobial peptides in the first line defence of human colon mucosa.
pubmed:affiliation
Department of Medical Biochemistry and Biophysics, Karolinska Institutet, SE-171 77 Stockholm, Sweden.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't