Development of a smart activity-based probe to detect subcellular activity of asparaginyl endopeptidase in living cells

Hong, Jong‐Ah; Choi, Na Young; La, Yeo-Kyoung; Nam, Ho Yeon; Seo, Jiwon; Lee, Jiyoun

doi:10.1039/c7ob01467h

Cited by 11 publications

(7 citation statements)

References 24 publications

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“…Previously, we developed fluorescent probes that can detect mercury ions in organic solvents and the enzyme activity in live cells . While both of these probes contain the same fluorophore, 4‐amino‐1,8‐naphthalimide, by incorporating the specific responsive moiety at the 4‐amino position they demonstrated different specificities and magnitudes of signal enhancement.…”

Section: Acknowledgmentsmentioning

confidence: 97%

A Turn‐On Fluorescent Probe for Live‐Cell Imaging of Biothiols

Hong

Kim

et al. 2018

Bulletin Korean Chem Soc

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Section: Acknowledgmentsmentioning

confidence: 97%

A Turn‐On Fluorescent Probe for Live‐Cell Imaging of Biothiols

Hong

Kim

et al. 2018

Bulletin Korean Chem Soc

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“…Alternatively, qABPs can contain a warhead conjugated with a fluorophore where the emission of fluorescence is increased after the target protease is labeled. This mechanism is due to the photoinduced electron transfer effect (PeT) (Hong et al, 2017). The first qABPs for serine proteases consist of a mixed alkyl aryl phosphonate and are linked to a succinimide derivative of the QSy7 (fluorescent quencher) coupled to the tyramine leaving group.…”

Section: Abps: Diverse Warheads Tags and Applicationsmentioning

confidence: 99%

Activity-Based Probes to Utilize the Proteolytic Activity of Cathepsin G in Biological Samples

et al. 2021

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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.

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“…This probe showed a twofold increase in fluorescence after reaction with the protease and was successfully used in live cell imaging of AEP. Although there is still room for improvement of signal to background ratio, this probe provides an interesting scaffold that could lead to a new generation of qABPs (Hong et al 2017).…”

Section: Fluorophoresmentioning

confidence: 99%

Recent Advances in Activity-Based Protein Profiling of Proteases

Chakrabarty

Kähler

Plassche

et al. 2018

Current Topics in Microbiology and Immunology

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The activity of proteases is tightly regulated, and dysregulation is linked to a variety of human diseases. For this reason, ABPP is a well-suited method to study protease biology and the design of protease probes has pushed the boundaries of ABPP. The development of highly selective protease probes is still a challenging task. After an introduction, the first section of this chapter discusses several strategies to enable detection of a single active protease species. These range from the usage of non-natural amino acids, combination of probes with antibodies, and engineering of the target proteases. A next section describes the different types of detection tags that facilitate the read-out possibilities including various types of imaging methods and mass spectrometry-based target identification. The power of protease ABPP is illustrated by examples for a selected number of proteases. It is expected that some protease probes that have been evaluated in animal models of human disease will find translation into clinical application in the near future.

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Development of a smart activity-based probe to detect subcellular activity of asparaginyl endopeptidase in living cells

Cited by 11 publications

References 24 publications

A Turn‐On Fluorescent Probe for Live‐Cell Imaging of Biothiols

A Turn‐On Fluorescent Probe for Live‐Cell Imaging of Biothiols

Activity-Based Probes to Utilize the Proteolytic Activity of Cathepsin G in Biological Samples

Recent Advances in Activity-Based Protein Profiling of Proteases

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