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Originally published online as doi:10.2353/ajpath.2009.090240 on August 28, 2009

Published online before print August 28, 2009
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(American Journal of Pathology. 2009;175:1453-1463.)
© 2009 American Society for Investigative Pathology
DOI: 10.2353/ajpath.2009.090240

Epithelial Integrity Is Maintained by a Matriptase-Dependent Proteolytic Pathway

Karin List*{dagger}, Peter Kosa*, Roman Szabo*, Alexandra L. Bey*, Chao Becky Wang{dagger}, Alfredo Molinolo* and Thomas H. Bugge*

From the Oral and Pharyngeal Cancer Branch,* National Institute of Dental and Craniofacial Research, National Institutes of Health, Bethesda, Maryland; and the Department of Pharmacology,{dagger} Barbara Ann Karmanos Cancer Institute, Wayne State University School of Medicine, Detroit, Michigan

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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