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Activity-Based Probes to Utilize the Proteolytic Activity of Cathepsin G in Biological Samples
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 p...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Frontiers Media S.A.
2021
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7959752/ https://www.ncbi.nlm.nih.gov/pubmed/33732686 http://dx.doi.org/10.3389/fchem.2021.628295 |
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author | Burster, Timo Gärtner, Fabian Knippschild, Uwe Zhanapiya, Anuar |
author_facet | Burster, Timo Gärtner, Fabian Knippschild, Uwe Zhanapiya, Anuar |
author_sort | Burster, Timo |
collection | PubMed |
description | 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. |
format | Online Article Text |
id | pubmed-7959752 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | Frontiers Media S.A. |
record_format | MEDLINE/PubMed |
spelling | pubmed-79597522021-03-16 Activity-Based Probes to Utilize the Proteolytic Activity of Cathepsin G in Biological Samples Burster, Timo Gärtner, Fabian Knippschild, Uwe Zhanapiya, Anuar Front Chem Chemistry 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. Frontiers Media S.A. 2021-02-25 /pmc/articles/PMC7959752/ /pubmed/33732686 http://dx.doi.org/10.3389/fchem.2021.628295 Text en Copyright © 2021 Burster, Gärtner, Knippschild and Zhanapiya. http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms. |
spellingShingle | Chemistry Burster, Timo Gärtner, Fabian Knippschild, Uwe Zhanapiya, Anuar Activity-Based Probes to Utilize the Proteolytic Activity of Cathepsin G in Biological Samples |
title | Activity-Based Probes to Utilize the Proteolytic Activity of Cathepsin G in Biological Samples |
title_full | Activity-Based Probes to Utilize the Proteolytic Activity of Cathepsin G in Biological Samples |
title_fullStr | Activity-Based Probes to Utilize the Proteolytic Activity of Cathepsin G in Biological Samples |
title_full_unstemmed | Activity-Based Probes to Utilize the Proteolytic Activity of Cathepsin G in Biological Samples |
title_short | Activity-Based Probes to Utilize the Proteolytic Activity of Cathepsin G in Biological Samples |
title_sort | activity-based probes to utilize the proteolytic activity of cathepsin g in biological samples |
topic | Chemistry |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7959752/ https://www.ncbi.nlm.nih.gov/pubmed/33732686 http://dx.doi.org/10.3389/fchem.2021.628295 |
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