Neutrophil elastase cleaves epithelial cadherin in acutely injured lung epithelium.
Fiche publication
Date publication
octobre 2016
Journal
Respiratory research
Auteurs
Membres identifiés du Cancéropôle Est :
Dr NAWROCKI-RABY Béatrice
Tous les auteurs :
Boxio R, Wartelle J, Nawrocki-Raby B, Lagrange B, Malleret L, Hirche T, Taggart C, Pacheco Y, Devouassoux G, Bentaher A
Lien Pubmed
Résumé
In acutely injured lungs, massively recruited polymorphonuclear neutrophils (PMNs) secrete abnormally neutrophil elastase (NE). Active NE creates a localized proteolytic environment where various host molecules are degraded leading to impairment of tissue homeostasis. Among the hallmarks of neutrophil-rich pathologies is a disrupted epithelium characterized by the loss of cell-cell adhesion and integrity. Epithelial-cadherin (E-cad) represents one of the most important intercellular junction proteins. E-cad exhibits various functions including its role in maintenance of tissue integrity. While much interest has focused on the expression and role of E-cad in different physio- and physiopathological states, proteolytic degradation of this structural molecule and ensuing potential consequences on host lung tissue injury are not completely understood.
Mots clés
E-cadherin, Epithelium disruption, Lung inflammation and injury, Neutrophil elastase
Référence
Respir. Res.. 2016 10 17;17(1):129