Lipid mediator-induced expression of bactericidal/ permeability-increasing protein (BPI) in human mucosal epithelia

Détails

ID Serval
serval:BIB_A5CE68CF68E1
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Institution
Titre
Lipid mediator-induced expression of bactericidal/ permeability-increasing protein (BPI) in human mucosal epithelia
Périodique
Proceedings of the National Academy of Sciences of the United States of America
Auteur⸱e⸱s
Canny  G., Levy  O., Furuta  G. T., Narravula-Alipati  S., Sisson  R. B., Serhan  C. N., Colgan  S. P.
ISSN
0027-8424
Statut éditorial
Publié
Date de publication
03/2002
Peer-reviewed
Oui
Volume
99
Numéro
6
Pages
3902-7
Notes
Journal Article
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, P.H.S. --- Old month value: Mar 19
Résumé
Epithelial cells which line mucosal surfaces are the first line of defense against bacterial invasion and infection. Recent studies have also indicated that epithelial cells contribute significantly to the orchestration of ongoing inflammatory processes. Here, we demonstrate that human epithelial cells express bactericidal/permeability-increasing protein (BPI), an antibacterial and endotoxin-neutralizing molecule previously associated with neutrophils. Moreover, we demonstrate that such BPI expression is transcriptionally regulated by analogs of endogenously occurring anti-inflammatory eicosanoids (aspirin-triggered lipoxins, ATLa). Initial studies to verify microarray analysis revealed that epithelial cells of wide origin (oral, pulmonary, and gastrointestinal mucosa) express BPI and each is similarly regulated by aspirin-triggered lipoxins. Studies aimed at localization of BPI revealed that such expression occurs on the cell surface of cultured epithelial cell lines and dominantly localizes to epithelia in human mucosal tissue. Functional studies employing a BPI-neutralizing anti-serum revealed that surface BPI blocks endotoxin-mediated signaling in epithelia and kills Salmonella typhimurium. These studies identify a previously unappreciated "molecular shield" for protection of mucosal surfaces against Gram-negative bacteria and their endotoxin.
Mots-clé
Anti-Bacterial Agents/*metabolism/pharmacology Anti-Inflammatory Agents/metabolism/pharmacology Antimicrobial Cationic Peptides Blood Proteins/biosynthesis/genetics/*metabolism/pharmacology Caco-2 Cells Cell Line Cell Membrane/drug effects/metabolism Epithelial Cells/cytology/drug effects/metabolism Gene Expression Regulation/*drug effects Humans Inflammation/metabolism/microbiology/pathology Lipids/*pharmacology Lipopolysaccharides/antagonists & inhibitors/metabolism/pharmacology *Membrane Proteins Mucous Membrane/cytology/*drug effects/*metabolism Protein Transport Salmonella typhimurium/physiology
Pubmed
Web of science
Open Access
Oui
Création de la notice
18/01/2008 12:11
Dernière modification de la notice
20/08/2019 15:10
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