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Biological Chemistry

Editor-in-Chief: Brüne, Bernhard

Editorial Board: Buchner, Johannes / Lei, Ming / Ludwig, Stephan / Thomas, Douglas D. / Turk, Boris / Wittinghofer, Alfred


IMPACT FACTOR 2018: 3.014
5-year IMPACT FACTOR: 3.162

CiteScore 2018: 3.09

SCImago Journal Rank (SJR) 2018: 1.482
Source Normalized Impact per Paper (SNIP) 2018: 0.820

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1437-4315
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First identification of a phosphorylcholine-substituted protein from Caenorhabditis elegans: isolation and characterization of the aspartyl protease ASP-6

Günter Lochnit
  • Institute of Biochemistry, Faculty of Medicine, Justus-Liebig-University, Friedrichstrasse 24, D-35392 Giessen, Germany
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/ Julia Grabitzki
  • Institute of Biochemistry, Faculty of Medicine, Justus-Liebig-University, Friedrichstrasse 24, D-35392 Giessen, Germany
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/ Björn Henkel
  • Institute of Biochemistry, Faculty of Medicine, Justus-Liebig-University, Friedrichstrasse 24, D-35392 Giessen, Germany
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/ Nektarios Tavernarakis
  • Institute of Molecular Biology and Biotechnology, Foundation for Research and Technology, Vassilika Vouton, P.O. Box 1385, GR-71110 Heraklion, Crete, Greece
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/ Rudolf Geyer
  • Institute of Biochemistry, Faculty of Medicine, Justus-Liebig-University, Friedrichstrasse 24, D-35392 Giessen, Germany
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Published Online: 2006-11-02 | DOI: https://doi.org/10.1515/BC.2006.186

Abstract

Caenorhabditis elegans is a widely accepted model system for parasitic nematodes, drug screening and developmental studies. Similar to parasitic worms, C. elegans expresses glycosphingolipids and glycoproteins carrying, in part, phosphorylcholine (PCho) substitutions, which might play important roles in nematode development, fertility and, at least in the case of parasites, survival within the host. With the exception of a major secretory/excretory product from Acanthocheilonema viteae (ES-62), no protein carrying this epitope has been studied in detail yet. Here we report on the identification, characterization and localization of the aspartyl protease ASP-6 of C. elegans, which is excreted by the nematode in a PCho-substituted form. Within the worm, most prominent expression of the protein is observed in the intestine, while muscle and epithelial cells express asp-6 to a lesser extent. In animals harboring an ASP-6::GFP fusion protein, diffuse fluorescence throughout the body cavity of adult worms indicates that the chimeric protein is secreted.

Keywords: mass spectrometry; nematodes; posttranslational modification; protease

About the article

Corresponding author


Received: February 27, 2006

Accepted: June 13, 2006

Published Online: 2006-11-02

Published in Print: 2006-10-01


Citation Information: Biological Chemistry, Volume 387, Issue 10/11, Pages 1487–1493, ISSN (Online) 1437-4315, ISSN (Print) 1431-6730, DOI: https://doi.org/10.1515/BC.2006.186.

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