Neutrophil elastase cleaves epithelial cadherin in acutely injured lung epithelium.

ABSTRACT:

Background

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 po

SUBMITTER: Boxio R 

PROVIDER: S-EPMC5067913 | biostudies-literature | 2016 Oct

REPOSITORIES: biostudies-literature