Drugging the undruggable: activity-based protein profiling offers opportunities for targeting the KLK activome

The vast majority of the human proteome is yet to be functionally characterized thus hindering ongoing investigations on potential drug resistance mechanisms and advanced treatment options. Chemical proteomics is a powerful solution for enzyme profiling and the development of next generation cancer...

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Published in:Cancer biology & therapy Vol. 23; no. 1; pp. 136 - 138
Main Authors: Lee, Kristi Y., Chau, Cindy H., Price, Douglas K., Figg, William D.
Format: Journal Article
Language:English
Published: United States Taylor & Francis 31.12.2022
Taylor & Francis Group
Subjects:
activity-based protein profiling
Humans
kallikrein
Kallikreins - chemistry
Kallikreins - metabolism
Kallikreins - therapeutic use
KLK activome
Male
Prostate cancer
Prostatic Neoplasms - enzymology
Prostatic Neoplasms - metabolism
Prostatic Neoplasms - pathology
Proteomics
Review
Tumor Microenvironment
KLK activome
activity-based protein profiling
proteomics
Prostate cancer
kallikrein
ISSN:1538-4047, 1555-8576, 1555-8576
Online Access:Get full text
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Abstract The vast majority of the human proteome is yet to be functionally characterized thus hindering ongoing investigations on potential drug resistance mechanisms and advanced treatment options. Chemical proteomics is a powerful solution for enzyme profiling and the development of next generation cancer therapeutics previously deemed undruggable by small molecules. Within this field, activity-based protein profiling (ABPP) is a specialized technology capable of discriminating enzyme interactions that occur within complex, biological environments. In a recent publication by Lovell et al, the kallikrein-related peptidase (KLK) family of serine proteases that is highly implicated in the progression of prostate cancer (PCa) was subject to ABPP to elucidate enzymatic activities in the presence of enzalutamide. This is the first report of ABPP in PCa and of activity-based chemical probes selective for individual KLKs. Further, the study reveals androgen receptor-dependent activity among KLK proteins, particularly in mediating the invasion of the bone microenvironment.
AbstractList The vast majority of the human proteome is yet to be functionally characterized thus hindering ongoing investigations on potential drug resistance mechanisms and advanced treatment options. Chemical proteomics is a powerful solution for enzyme profiling and the development of next generation cancer therapeutics previously deemed undruggable by small molecules. Within this field, activity-based protein profiling (ABPP) is a specialized technology capable of discriminating enzyme interactions that occur within complex, biological environments. In a recent publication by Lovell et al, the kallikrein-related peptidase (KLK) family of serine proteases that is highly implicated in the progression of prostate cancer (PCa) was subject to ABPP to elucidate enzymatic activities in the presence of enzalutamide. This is the first report of ABPP in PCa and of activity-based chemical probes selective for individual KLKs. Further, the study reveals androgen receptor-dependent activity among KLK proteins, particularly in mediating the invasion of the bone microenvironment.
The vast majority of the human proteome is yet to be functionally characterized thus hindering ongoing investigations on potential drug resistance mechanisms and advanced treatment options. Chemical proteomics is a powerful solution for enzyme profiling and the development of next generation cancer therapeutics previously deemed undruggable by small molecules. Within this field, activity-based protein profiling (ABPP) is a specialized technology capable of discriminating enzyme interactions that occur within complex, biological environments. In a recent publication by Lovell et al, the kallikrein-related peptidase (KLK) family of serine proteases that is highly implicated in the progression of prostate cancer (PCa) was subject to ABPP to elucidate enzymatic activities in the presence of enzalutamide. This is the first report of ABPP in PCa and of activity-based chemical probes selective for individual KLKs. Further, the study reveals androgen receptor-dependent activity among KLK proteins, particularly in mediating the invasion of the bone microenvironment.The vast majority of the human proteome is yet to be functionally characterized thus hindering ongoing investigations on potential drug resistance mechanisms and advanced treatment options. Chemical proteomics is a powerful solution for enzyme profiling and the development of next generation cancer therapeutics previously deemed undruggable by small molecules. Within this field, activity-based protein profiling (ABPP) is a specialized technology capable of discriminating enzyme interactions that occur within complex, biological environments. In a recent publication by Lovell et al, the kallikrein-related peptidase (KLK) family of serine proteases that is highly implicated in the progression of prostate cancer (PCa) was subject to ABPP to elucidate enzymatic activities in the presence of enzalutamide. This is the first report of ABPP in PCa and of activity-based chemical probes selective for individual KLKs. Further, the study reveals androgen receptor-dependent activity among KLK proteins, particularly in mediating the invasion of the bone microenvironment.
Author Price, Douglas K.
Lee, Kristi Y.
Chau, Cindy H.
Figg, William D.
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  organization: Center for Cancer Research, National Cancer Institute, National Institutes of Health
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10.1021/bc500208y
10.3389/fphar.2018.00353
10.1007/s10585-013-9615-4
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10.1016/j.ejmech.2020.112151
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10.1371/journal.pone.0212968
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Keywords KLK activome
activity-based protein profiling
proteomics
Prostate cancer
kallikrein
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SubjectTerms activity-based protein profiling
Humans
kallikrein
Kallikreins - chemistry
Kallikreins - metabolism
Kallikreins - therapeutic use
KLK activome
Male
Prostate cancer
Prostatic Neoplasms - enzymology
Prostatic Neoplasms - metabolism
Prostatic Neoplasms - pathology
Proteomics
Review
Tumor Microenvironment
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Title Drugging the undruggable: activity-based protein profiling offers opportunities for targeting the KLK activome
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