Monitoring compartment-specific substrate cleavage by cathepsins B, K, L, and S at physiological pH and redox conditions |
| |
| Authors: | Silvia Jordans Saša Jenko-Kokalj Nicole M Kühl Sofia Tedelind Wolfgang Sendt Dieter Brömme Dušan Turk Klaudia Brix |
| |
| Institution: | (1) School of Engineering and Science, Jacobs University Bremen, Campus Ring 6, Research II, 28759 Bremen, Germany;(2) Department of Biochemistry and Molecular Biology, Jožef Stefan Institute, Jamova 39, 1000 Ljubljana, Slovenia;(3) Krankenhaus St. Joseph-Stift Bremen, Schwachhauser Heerstrasse 54, 28209 Bremen, Germany;(4) Department of Oral and Biological Sciences, Faculty of Dentistry, University of British Columbia, 2350 Health Sciences Mall, Vancouver, BC V6T 1Z3, Canada |
| |
| Abstract: | Background Cysteine cathepsins are known to primarily cleave their substrates at reducing and acidic conditions within endo-lysosomes.
Nevertheless, they have also been linked to extracellular proteolysis, that is, in oxidizing and neutral environments. Although
the impact of reducing or oxidizing conditions on proteolytic activity is a key to understand physiological protease functions,
redox conditions have only rarely been considered in routine enzyme activity assays. Therefore we developed an assay to test
for proteolytic processing of a natural substrate by cysteine cathepsins which accounts for redox potentials and pH values
corresponding to the conditions in the extracellular space in comparison to those within endo-lysosomes of mammalian cells. |
| |
| Keywords: | |
| 本文献已被 SpringerLink 等数据库收录！ |
|
