Epithelial integrity is maintained by a matriptase-dependent proteolytic pathway

K List, P Kosa, R Szabo, AL Bey, CB Wang… - The American journal of …, 2009 - Elsevier
K List, P Kosa, R Szabo, AL Bey, CB Wang, A Molinolo, TH Bugge
The American journal of pathology, 2009Elsevier
A pericellular proteolytic pathway initiated by the transmembrane serine protease matriptase
plays a critical role in the terminal differentiation of epidermal tissues. Matriptase is
constitutively expressed in multiple other epithelia, suggesting a putative role of this
membrane serine protease in general epithelial homeostasis. Here we generated mice with
conditional deletion of the St14 gene, encoding matriptase, and show that matriptase indeed
is essential for the maintenance of multiple types of epithelia in the mouse. Thus, embryonic …
A pericellular proteolytic pathway initiated by the transmembrane serine protease matriptase plays a critical role in the terminal differentiation of epidermal tissues. Matriptase is constitutively expressed in multiple other epithelia, suggesting a putative role of this membrane serine protease in general epithelial homeostasis. Here we generated mice with conditional deletion of the St14 gene, encoding matriptase, and show that matriptase indeed is essential for the maintenance of multiple types of epithelia in the mouse. Thus, embryonic or postnatal ablation of St14 in epithelial tissues of diverse origin and function caused severe organ dysfunction, which was often associated with increased permeability, loss of tight junction function, mislocation of tight junction-associated proteins, and generalized epithelial demise. The study reveals that the homeostasis of multiple simple and stratified epithelia is matriptase-dependent, and provides an important animal model for the exploration of this membrane serine protease in a range of physiological and pathological processes.
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