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BioMed Research International
Volume 2014, Article ID 309718, 9 pages
Review Article

Cysteine Cathepsin Activity Regulation by Glycosaminoglycans

1Faculty of Chemistry and Chemical Technology, University of Ljubljana, Večna pot 113, SI-1000 Ljubljana, Slovenia
2Department of Biochemistry, Molecular and Structural Biology, Jozef Stefan Institute, Jamova Cesta 39, SI-1000 Ljubljana, Slovenia
3Centre of Excellence for Integrated Approaches in Chemistry and Biology of Proteins, Jamova Cesta 39, SI-1000 Ljubljana, Slovenia

Received 16 May 2014; Accepted 2 July 2014; Published 21 December 2014

Academic Editor: George Tzanakakis

Copyright © 2014 Marko Novinec et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.


Cysteine cathepsins are a group of enzymes normally found in the endolysosomes where they are primarily involved in intracellular protein turnover but also have a critical role in MHC II-mediated antigen processing and presentation. However, in a number of pathologies cysteine cathepsins were found to be heavily upregulated and secreted into extracellular milieu, where they were found to degrade a number of extracellular proteins. A major role in modulating cathepsin activities play glycosaminoglycans, which were found not only to facilitate their autocatalytic activation including at neutral pH, but also to critically modulate their activities such as in the case of the collagenolytic activity of cathepsin K. The interaction between cathepsins and glycosaminoglycans will be discussed in more detail.