Aiping M Zhao

Publication Detail

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Matriptase-3 is a novel phylogenetically preserved membrane-anchored serine protease with broad serpin reactivity.

Roman Szabo; Sarah Netzel-Arnett; John P Hobson; Toni M Antalis; Thomas H Bugge (Profiled Author: Toni Antalis)

Proteases and Tissue Remodeling Unit, Oral and Pharyngeal Cancer Branch, National Institute of Dental and Craniofacial Research, National Institutes of Health, 30 Convent Drive, Bethesda, MD 20892, USA.
The Biochemical journal 2005;390(Pt 1):231-42.

We report in the present study the bioinformatic identification, molecular cloning and biological characterization of matriptase-3, a novel membrane-anchored serine protease that is phylogenetically preserved in fish, birds, rodents, canines and primates. The gene encoding matriptase-3 is located on syntenic regions of human chromosome 3q13.2, mouse chromosome 16B5, rat chromosome 11q21 and chicken chromosome 1. Bioinformatic analysis combined with cDNA cloning predicts a functional TTSP (type II transmembrane serine protease) with 31% amino acid identity with both matriptase/MT-SP1 and matriptase-2. This novel protease is composed of a short N-terminal cytoplasmic region followed by a transmembrane domain, a stem region with one SEA, two CUB and three LDLRa (low-density lipoprotein receptor domain class A) domains and a C-terminal catalytic serine protease domain. Transcript analysis revealed restricted, species-conserved expression of matriptase-3, with the highest mRNA levels in brain, skin, reproductive and oropharyngeal tissues. The full-length matriptase-3 cDNA directed the expression of a 90 kDa N-glycosylated protein that localized to the cell surface, as assessed by cell-surface biotin labelling. The purified activated matriptase-3 serine protease domain expressed in insect cells hydrolysed synthetic peptide substrates, with a strong preference for Arg at position P(1), and showed proteolytic activity towards several macromolecular substrates, including gelatin, casein and albumin. Interestingly, activated matriptase-3 formed stable inhibitor complexes with an array of serpins, including plasminogen activator inhibitor-1, protein C inhibitor, alpha1-proteinase inhibitor, alpha2-antiplasmin and antithrombin III. Our study identifies matriptase-3 as a novel biologically active TTSP of the matriptase subfamily having a unique expression pattern and post-translational regulation.

2 Originating Grant

• 1.

  Antalis, Toni M

  New Function for the Serpin PAI-2 as a Regular of pRb

  1 August 2003 - 31 May 2009

  NATIONAL CANCER INSTITUTE

• 2.

  Antalis, Toni M

  NEW FUNCTION SERPIN PAI 2 AS A REGULAR OF RB

  1 July 2002 - 30 June 2010

  NATIONAL CANCER INSTITUTE

Scientific Context

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