title: Matriptase: potent proteolysis on the cell surface.
abstract: Matriptase is a type II transmembrane serine protease expressed in most human epithelia, where it is coexpressed with its cognate transmembrane inhibitor, hepatocyte growth factor activator inhibitor (HAI)-1. Activation of the matriptase zymogen requires sequential N-terminal cleavage, activation site autocleavage, and transient association with HAI-1. Matriptase has an essential physiological role in profilaggrin processing, corneocyte maturation, and lipid matrix formation associated with terminal differentiation of the oral epithelium and the epidermis, and is also critical for hair follicle growth. Matriptase and HAI expression are frequently dysregulated in human cancer, and matriptase expression that is unopposed by HAI-1 potently promotes carcinogenesis and metastatic dissemination in animal models.
authors.affiliation: Proteases and Tissue Remodeling Unit, Oral and Pharyngeal Cancer Branch, National Institute of Dental and Craniofacial Research, National Institutes of Health, Bethesda, MD 20892, USA. thomas.bugge@nih.gov
authors.forename: Karin
authors.initials: K
authors.lastname: List
authors.forename: Thomas H
authors.initials: TH
authors.lastname: Bugge
authors.forename: Roman
authors.initials: R
authors.lastname: Szabo
mesh_terms: D000818:Animals; D002462:Cell Membrane / Q000378:metabolism*; D004789:Enzyme Activation; D004847:Epithelial Cells / Q000473:pathology; D006801:Humans; D009369:Neoplasms / Q000201:enzymology; D011499:Protein Processing, Post-Translational; D012697:Serine Endopeptidases / Q000378:metabolism*
chemical_list: D012697:Serine Endopeptidases; C485595:matriptase