ACTIVITY-BASED PROBES TO UTILIZE THE PROTEOLYTIC ACTIVITY OF CATHEPSIN G IN BIOLOGICAL SAMPLES
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Date
2021-02-25
Authors
Burster, Timo
Gärtner, Fabian
Knippschild, Uwe
Zhanapiya, Anuar
Journal Title
Journal ISSN
Volume Title
Publisher
Frontiers in Chemistry
Abstract
Neutrophils, migrating to the site of infection, are able to release serine proteases after being
activated. These serine proteases comprise cathepsin G (CatG), neutrophil elastase
protease 3 (PR3), and neutrophil serine protease 4 (NSP4). A disadvantage of the
uncontrolled proteolytic activity of proteases is the outcome of various human diseases,
including cardiovascular diseases, thrombosis, and autoimmune diseases. Activity-based
probes (ABPs) are used to determine the proteolytic activity of proteases, containing a set of
three essential elements: Warhead, recognition sequence, and the reporter tag for
detection of the covalent enzyme activity–based probe complex. Here, we summarize
the latest findings of ABP-mediated detection of proteases in both locations intracellularly
and on the cell surface of cells, thereby focusing on CatG. Particularly, application of ABPs
in regular flow cytometry, imaging flow cytometry, and mass cytometry by time-of-flight
(CyTOF) approaches is advantageous when distinguishing between immune cell subsets.
ABPs can be included in a vast panel of markers to detect proteolytic activity and determine
whether proteases are properly regulated during medication. The use of ABPs as a
detection tool opens the possibility to interfere with uncontrolled proteolytic activity of
proteases by employing protease inhibitors.
Description
Keywords
Type of access: Open Access, activity-based probes, cathepsin G, flow cytometry, CyTOF/mass cytometry, immune cells, serine proteases
Citation
Burster, T., Gärtner, F., Knippschild, U., & Zhanapiya, A. (2021). Activity-Based Probes to Utilize the Proteolytic Activity of Cathepsin G in Biological Samples. Frontiers in Chemistry, 9. https://doi.org/10.3389/fchem.2021.628295