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Published ahead of print on August 21, 2008, doi:10.1165/rcmb.2008-0015RC

Am. J. Respir. Cell Mol. Biol., Volume 39, Number 6, December 2008, 631-637

A more recent version of this article appeared on December 1, 2008
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Submitted on January 9, 2008
Revised on August 20, 2008

{alpha}1-antitrypsin Inhibits the Activity of the Matriptase Catalytic Domain in vitro

Sabina Janciauskiene1*, Izabela Nita1, Devipriya Subramaniyam1, Qian Li2, Jack R Lancaster, Jr.3, and Sadis Matalon3

1 Department of Clinical Sciences, The Wallenberg Laboratory, Lund University, Malmo University Hospital, Malmo, Sweden, 2 Department of Anesthesiology, University of Alabama at Birmingham, School of Medicine, Birmingham, Alabama, USA, 3 Department of Anesthesiology, University of Alabama at Birmingham, School of Medicine, Birmingham, Alabama, USA; Department of Physiology and Biophysics, University of Alabama at Birmingham, School of Medicine, Birmingham, Alabama, USA; Environmental Health Sciences, University of Alabama at Birmingham, School of Medicine, Birmingham, Alabama, USA

* To whom correspondence should be addressed. E-mail: Sabina.Janciauskiene{at}med.lu.se.

Matriptase is a type II transmembrane protease which is characterized by an N-terminal transmembrane and multiple extracellular domains, in addition to the conserved extracellular serine protease catalytic domain. The expression pattern of matriptase suggests that this protease may play broad roles in the biology of surface lining epithelial cells. In this study we report that {alpha}1-antitrypsin (AAT), an endogenous inhibitor of serine proteases, inhibits the catalytic domain of human recombinant matriptase in vitro. Co-incubation of {alpha}1-antitrypsin with matriptase (at a molar ratio 1:2) resulted in the formation of heat stable complexes, clearly seen in sodium dodecyl sulfate (SDS) electrophoresis and Western blots. AAT was found to be a slow, tight-binding inhibitor of the catalytic domain of matriptase with a second order reaction rate constant of 0.31 x103 M-1s-1. Notably, the oxidised form of AAT, which lacks serine protease inhibitor activity, failed to generate matriptase complexes and to inhibit matriptase activity. Since matriptase is involved in a number of physiological processes including activation of epithelial sodium channels, our findings offer considerable new insights into new regulatory function of AAT in vivo.




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