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Protein & Peptide Letters

Editor-in-Chief

ISSN (Print): 0929-8665
ISSN (Online): 1875-5305

Substrate Specificity of Rat DESC4, a Type II Transmembrane Serine Protease

Author(s): Maik Behrens, Friedrich Buck and Wolfgang Meyerhof

Volume 16, Issue 1, 2009

Page: [1 - 6] Pages: 6

DOI: 10.2174/092986609787049466

Price: $65

Abstract

Type II transmembrane serine proteases (TTSPs) are involved in important physiological processes, such as pro-hormone processing, cellular signaling, host immune defense, and cancer development. The diversity of functions is reflected by the multidomain architecture of these proteases, which are composed of a variety of functional domains in addition to the catalytic domain. Recently, we identified rat DESC4, a member of the HAT/DESC1-like subfamily of TTSPs. Intriguingly, DESC4 gene expression is confined to few tissues including gustatory papillae. In the current publication we present the purification of the catalytic domain of recombinant rat DESC4. Subsequently, the catalytic domain was subjected to a refolding procedure. During refolding we observed endogenous catalytic activity leading to smaller fragments, which were analyzed by peptide sequencing. The identified cleavage-sites are typical for trypsin-like serine proteases. For further analyses a homology-based model of the DESC4 catalytic domain was generated enabling us to investigate protease-substrate interaction in more detail.

Keywords: Type II transmembrane serine protease, proteolysis, recombinant protein expression, HAT/DESC1-like proteases

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