IMR Press / FBL / Volume 12 / Issue 13 / DOI: 10.2741/2448

Frontiers in Bioscience-Landmark (FBL) is published by IMR Press from Volume 26 Issue 5 (2021). Previous articles were published by another publisher on a subscription basis, and they are hosted by IMR Press on as a courtesy and upon agreement with Frontiers in Bioscience.

Matriptase-dependent cell surface proteolysis in epithelial development and pathogenesis
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1 Proteases and Tissue Remodeling Unit, National Institute of Dental and Craniofacial Research, National Institutes of Health, Bethesda, MD, USA
Front. Biosci. (Landmark Ed) 2007, 12(13), 5060–5070;
Published: 1 September 2007

Matriptase is an epithelial type II transmembrane serine protease with a complex modular structure and sophisticated activation mechanism. Reduced matriptase activity in mice or humans is associated with incomplete terminal differentiation of epidermis, epidermal appendages, oral epithelium, and, likely, other epithelial structures. Preliminary evidence indicates that matriptase is part of a serine protease zymogen activation cascade that regulates epithelial cell proliferation and fate. Matriptase activity must be tightly controlled in epithelial tissues by transcriptional and posttranslational mechanisms, as matriptase dysregulation can cause embryonic demise as well as malignant transformation.

Cell Surface Proteolysis
Epithelial Development
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