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
Protein & Peptide Letters
Title: Substrate Specificity of Rat DESC4, a Type II Transmembrane Serine Protease
Volume: 16 Issue: 1
Author(s): Maik Behrens, Friedrich Buck and Wolfgang Meyerhof
Affiliation:
Keywords: Type II transmembrane serine protease, proteolysis, recombinant protein expression, HAT/DESC1-like proteases
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.
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Cite this article as:
Behrens Maik, Buck Friedrich and Meyerhof Wolfgang, Substrate Specificity of Rat DESC4, a Type II Transmembrane Serine Protease, Protein & Peptide Letters 2009; 16 (1) . https://dx.doi.org/10.2174/092986609787049466
DOI https://dx.doi.org/10.2174/092986609787049466 |
Print ISSN 0929-8665 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5305 |
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