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Cysteine proteases: destruction ability versus immunomodulation capacity in immune cells

  • Tina Zavašnik-Bergant und Boris Turk
Veröffentlicht/Copyright: 2. November 2007
Biological Chemistry
Aus der Zeitschrift Band 388 Heft 11

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.


Corresponding author

Published Online: 2007-11-02
Published in Print: 2007-11-01

©2007 by Walter de Gruyter Berlin New York

Artikel in diesem Heft

  1. Proteinase Inhibitors and Biological Control – An Attractive International Symposia Series
  2. Two decades of thyroglobulin type-1 domain research
  3. Cysteine cathepsin non-inhibitory binding partners: modulating intracellular trafficking and function
  4. Cysteine proteases: destruction ability versus immunomodulation capacity in immune cells
  5. ‘Species’ of peptidases
  6. Protease research in the era of systems biology
  7. Human and mouse homo-oligomeric meprin A metalloendopeptidase: substrate and inhibitor specificities
  8. Association of cathepsin E with tumor growth arrest through angiogenesis inhibition and enhanced immune responses
  9. Characterization and comparative 3D modeling of CmPI-II, a novel ‘non-classical’ Kazal-type inhibitor from the marine snail Cenchritis muricatus (Mollusca)
  10. Cellular localization of MAGI-1 caspase cleavage products and their role in apoptosis
  11. Differential methylation kinetics of individual target site strands by T4Dam DNA methyltransferase
  12. Characterisation of zinc-binding domains of peroxisomal RING finger proteins using size exclusion chromatography/inductively coupled plasma-mass spectrometry
  13. Defining the extended substrate specificity of kallikrein 1-related peptidases
  14. Latent MMP-9 is bound to TIMP-1 before secretion
  15. Novel expression of kallikreins, kallikrein-related peptidases and kinin receptors in human pleural mesothelioma
  16. Activity of ulilysin, an archaeal PAPP-A-related gelatinase and IGFBP protease
  17. Clinical chemistry reference database for Wistar rats and C57/BL6 mice
Heruntergeladen am 21.11.2025 von https://www.degruyterbrill.com/document/doi/10.1515/BC.2007.144/html
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