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Biological Chemistry

Editor-in-Chief: Brüne, Bernhard

Editorial Board Member: Buchner, Johannes / Lei, Ming / Ludwig, Stephan / Sies, Helmut / Turk, Boris / Wittinghofer, Alfred

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1437-4315
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Specificity of human cathepsin S determined by processing of peptide substrates and MHC class II-associated invariant chain

Thomas Rückrich
  • Interfacultary Institute for Biochemistry, University of Tübingen, Medical and Natural Sciences Research Centre, Ob dem Himmelreich 7, D-72074 Tübingen, Germany and Department of Medicine II, University of Tübingen, Otfried-Müller-Str. 10, D-72076 Tübingen, Germany
/ Jens Brandenburg
  • Interfacultary Institute for Biochemistry, University of Tübingen, Medical and Natural Sciences Research Centre, Ob dem Himmelreich 7, D-72074 Tübingen, Germany
/ Alexander Cansier
  • Interfacultary Institute for Biochemistry, University of Tübingen, Medical and Natural Sciences Research Centre, Ob dem Himmelreich 7, D-72074 Tübingen, Germany and Present address: Panatecs GmbH, Ob dem Himmelreich 7, D-72074 Tübingen, Germany
/ Margret Müller
  • Institute for Cell Biology, Department of Immunology, University of Tübingen, Auf der Morgenstelle 15, D-72076 Tübingen, Germany
/ Stefan Stevanović
  • Institute for Cell Biology, Department of Immunology, University of Tübingen, Auf der Morgenstelle 15, D-72076 Tübingen, Germany
/ Klaus Schilling
  • Institute of Biochemistry I, Friedrich-Schiller-University, Nonnenplan 2, D-07743 Jena, Germany
/ Bernd Wiederanders
  • Institute of Biochemistry I, Friedrich-Schiller-University, Nonnenplan 2, D-07743 Jena, Germany
/ Alexander Beck
  • Department of Medicine IV, University of Tübingen, Otfried-Müller-Str. 10, D-72076 Tübingen, Germany
/ Arthur Melms
  • Department of General Neurology, Hertie Institute for Clinical Brain Research, Tübingen University Hospital, Otfried-Müller-Str. 27, D-72076 Tübingen, Germany
/ Michael Reich
  • Department of Medicine II, University of Tübingen, Otfried-Müller-Str. 10, D-72076 Tübingen, Germany
/ Christoph Driessen
  • Department of Medicine II, University of Tübingen, Otfried-Müller-Str. 10, D-72076 Tübingen, Germany
/ Hubert Kalbacher
  • Interfacultary Institute for Biochemistry, University of Tübingen, Medical and Natural Sciences Research Centre, Ob dem Himmelreich 7, D-72074 Tübingen, Germany
Published Online: 2006-11-02 | DOI: https://doi.org/10.1515/BC.2006.188

Abstract

Cathepsin S (CatS) is a lysosomal cysteine protease of the papain family, the members of which possess relatively broad substrate specificities. It has distinct roles in major histocompatibility complex (MHC) class II-associated peptide loading and in antigen processing in both the MHC class I and class II pathways. It may therefore represent a target for interference with antigen presentation, which could be of value in the therapy of (auto)immune diseases. To obtain more detailed information on the specificity of CatS, we mapped its cleavage site preferences at subsites S3–S1′ by in vitro processing of a peptide library. Only five amino acid residues at the substrate's P2 position allowed for cleavage by CatS under time-limited conditions. Preferences for groups of amino acid residues were also observed at positions P3, P1 and P1′. Based on these results, we developed highly CatS-sensitive peptides. After processing of MHC class II-associated invariant chain (Ii), a natural protein substrate of CatS, we identified CatS cleavage sites in Ii of which a majority matched the amino acid residue preference data obtained with peptides. These observed cleavage sites in Ii might be of relevance for its in vivo processing by CatS.

Keywords: antigen processing; cathepsin S; electrospray mass spectrometry; invariant chain; MHC class II; substrate specificity

References

About the article

Corresponding author


Received: March 14, 2006

Accepted: July 4, 2006

Published Online: 2006-11-02

Published in Print: 2006-10-01


Citation Information: Biological Chemistry, ISSN (Online) 1437-4315, ISSN (Print) 1431-6730, DOI: https://doi.org/10.1515/BC.2006.188. Export Citation

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