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.
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|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:||07 Apr 2015 01:44|
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