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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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Volume 388, Issue 11

Issues

Cysteine proteases: destruction ability versus immunomodulation capacity in immune cells

Tina Zavašnik-Bergant
  • 1Department of Biochemistry, Molecular and Structural Biology, Jožef Stefan Institute, SI-1000 Ljubljana, Slovenia
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
/ Boris Turk
  • 2Department of Biochemistry, Molecular and Structural Biology, Jožef Stefan Institute, SI-1000 Ljubljana, Slovenia
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
Published Online: 2007-11-02 | DOI: https://doi.org/10.1515/BC.2007.144

Abstract

Cysteine proteases (cathepsins) play a pivotal role in various physiological processes, as well as in several diseases. In the immune response, maturation of major histocompatibility class II (MHC II) molecules and processing of antigens for further presentation by MHC II is tightly linked to the enzymes of the endosomal/lysosomal system, of which cysteine proteases constitute a major proportion. Furthermore, the process of autophagy provides access for cytosolic antigens to proteolysis by lysosomal cathepsins and subsequent MHC II presentation. Other specific functions of proteolytic enzymes associated with the immune response, such as activation of granzymes by cathepsin C in T-lymphocytes, are introduced and covered in this review.

Keywords: antigen presentation; asparagine endopeptidase; autophagy; cathepsins; cystatins; dipeptidyl peptidase I

About the article

Corresponding author


Published Online: 2007-11-02

Published in Print: 2007-11-01


Citation Information: Biological Chemistry, Volume 388, Issue 11, Pages 1141–1149, ISSN (Online) 14374315, ISSN (Print) 14316730, DOI: https://doi.org/10.1515/BC.2007.144.

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