Activity-Based Probes to Utilize the Proteolytic Activity of Cathepsin G in Biological Samples
Burster T. Gärtner F. Knippschild U. Zhanapiya A.
25 February 2021Frontiers Media S.A.
Frontiers in Chemistry
2021#9
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. © Copyright
activity-based probes , cathepsin G , CyTOF/mass cytometry , flow cytometry , immune cells , serine proteases
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Department of Biology, School of Sciences and Humanities, Nazarbayev University, Nur-Sultan, Kazakhstan
Department of General and Visceral Surgery, Surgery Center, Ulm University Hospital, Ulm, Germany
Department of Biology
Department of General and Visceral Surgery
10 лет помогаем публиковать статьи Международный издатель
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