Matriptase: potent proteolysis on the cell surface.

Karin List; Thomas H Bugge; Roman Szabo

doi:10.2119/2006-00022.list

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PubMed · 16838070

Matriptase: potent proteolysis on the cell surface.

Karin List·Thomas H Bugge·Roman Szabo

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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.

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Animals Cell Membrane Enzyme Activation Epithelial Cells Humans Neoplasms Protein Processing, Post-Translational Serine Endopeptidases Journal Article Research Support, N.I.H., Intramural Research Support, U.S. Gov't, Non-P.H.S.Review

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Karin List, Thomas H Bugge, Roman Szabo. Matriptase: potent proteolysis on the cell surface.. https://doi.org/10.2119/2006-00022.list

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