The type II transmembrane serine protease Matriptase-2 – identification, structural features, enzymology, expression pattern and potential roles
Ramsay, Andrew J., Reid, Janet C., Velasco, Gloria, Quigley, James P., & Hooper, John D. (2008) The type II transmembrane serine protease Matriptase-2 – identification, structural features, enzymology, expression pattern and potential roles. Frontiers in Bioscience, 13(1), pp. 569-579.
Matriptase-2 (also known as TMPRSS6) is a recently identified member of the type II transmembrane serine protease 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. Although the physiological function of matriptase-2 is not known, its high mRNA expression in liver and data from a limited number of studies indicating association with several cancers, it is likely that this enzyme will have important cell surface associated roles. Here we overview the identification of matriptase-2, summarise its structural features, biochemistry, expression pattern and disease associations and speculate on its potential functions.
Impact and interest:
Citation counts are sourced monthly from and citation databases.
These databases contain citations from different subsets of available publications and different time periods and thus the citation count from each is usually different. Some works are not in either database and no count is displayed. Scopus includes citations from articles published in 1996 onwards, and Web of Science® generally from 1980 onwards.
Citations counts from theindexing service can be viewed at the linked Google Scholar™ search.
Full-text downloads displays the total number of times this work’s files (e.g., a PDF) have been downloaded from QUT ePrints as well as the number of downloads in the previous 365 days. The count includes downloads for all files if a work has more than one.
|Item Type:||Journal Article|
|Additional Information:||Author contact details: firstname.lastname@example.org|
|Subjects:||Australian and New Zealand Standard Research Classification > BIOLOGICAL SCIENCES (060000)
Australian and New Zealand Standard Research Classification > BIOLOGICAL SCIENCES (060000) > BIOCHEMISTRY AND CELL BIOLOGY (060100)
|Divisions:||Past > QUT Faculties & Divisions > Faculty of Science and Technology|
|Copyright Owner:||Copyright 2008 Frontiers in Bioscience Publications|
|Copyright Statement:||Posted with the permission of the copyright owner for your personal use only. No further distribution is permitted without permission of the copyright owner.|
|Deposited On:||28 Jun 2007|
|Last Modified:||29 Feb 2012 13:47|
Repository Staff Only: item control page