IMR Press / FBL / Volume 13 / Issue 2 / DOI: 10.2741/2702

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.


The type II transmembrane serine protease Matriptase-2 – identification, structural features, enzymology, expression pattern and potential roles

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1 Institute of Health and Biomedical Innovation, Queensland University of Technology, Kelvin Grove, Queensland 4059, Australia
2 Departamento de Bioquimica y Biologia Molecular, Instituto Universitario de Oncologia, Universidad de Oviedo, 33006 Oviedo, Spain
3 Department of Cell Biology, The Scripps Research Institute, La Jolla, California 92037, USA
Front. Biosci. (Landmark Ed) 2008, 13(2), 569–579;
Published: 1 January 2008

Matriptase-2 (also known as TMPRSS6) is a recently identified member of the type II transmembrane serine protease (TTSP) family. Structurally this enzyme contains a short cytoplasmic amino terminal tail, a transmembrane region, a stem region containing two CUB domains and three LDL receptor class A domains, and at the carboxy terminal a trypsin-like serine protease domain. The matriptase-2 gene and encoded protein are highly conserved in mammals. Biochemically matriptase-2 has substrate specificity similar to the structurally related protein matriptase (also known as MT-SP1). Although the patho-physiological functions of matriptase-2 are not known, its high mRNA expression in liver and several cancers indicate that this enzyme, similar to other TTSPs, will likely have important cell surface associated roles in normal and disease states. Here we overview the identification of matriptase-2, summarise its structural features, biochemistry, expression pattern and disease associations and discuss its potential functions.

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