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.
Export Options
About this article
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 |
- Author Guidelines
- Graphical Abstracts
- Fabricating and Stating False Information
- Research Misconduct
- Post Publication Discussions and Corrections
- Publishing Ethics and Rectitude
- Increase Visibility of Your Article
- Archiving Policies
- Peer Review Workflow
- Order Your Article Before Print
- Promote Your Article
- Manuscript Transfer Facility
- Editorial Policies
- Allegations from Whistleblowers
Related Articles
-
Tailored Angiogenesis Inhibition in Cancer Therapy: Respecting the Heart to Improve the Net Outcome
Current Signal Transduction Therapy New Perspectives in Glioma Immunotherapy
Current Pharmaceutical Design Quality Assessment of Diagnostic Methods Employed for Suspected Lung Cancer
Current Respiratory Medicine Reviews Oxidative Stress in Tumor Angiogenesis - Therapeutic Targets
Current Pharmaceutical Design Nuclear Export as a Novel Therapeutic Target: The CRM1 Connection
Current Cancer Drug Targets Patent Selections
Recent Patents on Inflammation & Allergy Drug Discovery Nano-Tetrandrine Efficiently Inhibits the Proliferation and Induces the Apoptosis of Hep2 Cells through a Mitochondrial Signaling Pathway
Current Signal Transduction Therapy Predicting Cancer-Related MiRNAs Using Expression Profiles in Tumor Tissue
Current Pharmaceutical Biotechnology Impact of Epigenetic Dietary Components on Cancer through Histone Modifications
Current Medicinal Chemistry Neurokinin-1 Receptor Antagonists in Lung Cancer Therapy
Letters in Drug Design & Discovery Jaridonin, a Novel Ent-Kaurene Diterpenoid from Isodon rubescens, Inducing Apoptosis via Production of Reactive Oxygen Species in Esophageal Cancer Cells
Current Cancer Drug Targets TGFb and its Smad Connection to Cancer
Current Genomics Methylation Profile of miR-9-1 and miR-9-1/-9-3 as Potential Biomarkers of Diabetic Retinopathy
Current Diabetes Reviews Anti-Cancer Drug Design Using Natural and Synthetic Pharmacophores
Current Organic Chemistry The Cross-talk between Tristetraprolin and Cytokines in Cancer
Anti-Cancer Agents in Medicinal Chemistry Targeting JAK3 Tyrosine Kinase-Linked Signal Transduction Pathways with Rationally-Designed Inhibitors
Anti-Cancer Agents in Medicinal Chemistry MicroRNAs (miRNAs) as Biomarker(s) for Prognosis and Diagnosis of Gastrointestinal (GI) Cancers
Current Pharmaceutical Design Viral Carcinogenesis of Oral Region and Recent Trends in Treatment
Recent Patents on Biomarkers The ATP-driven Hsp60 Machinery: Biological and Clinical Implications
Current Immunology Reviews (Discontinued) Dual Nuclear/Fluorescence Imaging Potantial of Zinc(II) Phthalocyanine in MIA PaCa-2 Cell Line
Current Radiopharmaceuticals