title: Antimicrobial peptides in the first line defence of human colon mucosa.
abstract: 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.
authors.affiliation: Department of Medical Biochemistry and Biophysics, Karolinska Institutet, SE-171 77 Stockholm, Sweden.
authors.forename: Maria
authors.initials: M
authors.lastname: Tollin
authors.forename: Peter
authors.initials: P
authors.lastname: Bergman
authors.forename: Torgny
authors.initials: T
authors.lastname: Svenberg
authors.forename: Hans
authors.initials: H
authors.lastname: Jörnvall
authors.forename: Gudmundur Hrafn
authors.initials: GH
authors.lastname: Gudmundsson
authors.forename: Birgitta
authors.initials: B
authors.lastname: Agerberth
mesh_terms: D000890:Anti-Infective Agents / Q000494:pharmacology*; D023181:Antimicrobial Cationic Peptides / Q000494:pharmacology; D001419:Bacteria / Q000276:immunology; D001798:Blood Proteins / Q000737:chemistry; D015139:Blotting, Southern; D015153:Blotting, Western; D054804:Cathelicidins; D002851:Chromatography, High Pressure Liquid; D003106:Colon / Q000473:pathology*; D023082:Defensins / Q000737:chemistry; D004591:Electrophoresis, Polyacrylamide Gel; D047091:Eosinophil Granule Proteins; D006657:Histones / Q000737:chemistry; D006801:Humans; D013058:Mass Spectrometry; D009092:Mucous Membrane / Q000473:pathology*; D010455:Peptides / Q000737:chemistry / Q000494:pharmacology; D010741:Phospholipases A / Q000737:chemistry; D017434:Protein Structure, Tertiary; D012333:RNA, Messenger / Q000378:metabolism; D020133:Reverse Transcriptase Polymerase Chain Reaction; D012260:Ribonucleases / Q000737:chemistry; D012269:Ribosomal Proteins / Q000737:chemistry; D013997:Time Factors; D023084:alpha-Defensins / Q000737:chemistry; D023083:beta-Defensins / Q000737:chemistry
chemical_list: D000890:Anti-Infective Agents; D023181:Antimicrobial Cationic Peptides; D001798:Blood Proteins; D054804:Cathelicidins; C406407:DEFB1 protein, human; D023082:Defensins; D047091:Eosinophil Granule Proteins; D006657:Histones; D010455:Peptides; D012333:RNA, Messenger; D012269:Ribosomal Proteins; D023084:alpha-Defensins; D023083:beta-Defensins; C406413:human neutrophil peptide 1; C040469:ribosomal protein S30; D012260:Ribonucleases; D010741:Phospholipases A