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N-Terminomics Strategies for Protease Substrates Profiling
Mintoo, Mubashir Chakravarty, Amritangshu Tilvawala, Ronak
Mintoo, Mubashir
Chakravarty, Amritangshu
Tilvawala, Ronak
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Abstract
Proteases play a central role in various biochemical pathways catalyzing and regulating key biological events. Proteases catalyze an irreversible post-translational modification called proteolysis by hydrolyzing peptide bonds in proteins. Given the destructive potential of proteolysis, protease activity is tightly regulated. Dysregulation of protease activity has been reported in numerous disease conditions, including cancers, neurodegenerative diseases, inflammatory conditions, cardiovascular diseases, and viral infections. The proteolytic profile of a cell, tissue, or organ is governed by protease activation, activity, and substrate specificity. Thus, identifying protease substrates and proteolytic events under physiological conditions can provide crucial information about how the change in protease regulation can alter the cellular proteolytic landscape. In recent years, mass spectrometry-based techniques called N-terminomics have become instrumental in identifying protease substrates from complex biological mixtures. N-terminomics employs the labeling and enrichment of native and neo-N-termini peptides, generated upon proteolysis followed by mass spectrometry analysis allowing protease substrate profiling directly from biological samples. In this review, we provide a brief overview of N-terminomics techniques, focusing on their strengths, weaknesses, limitations, and providing specific examples where they were successfully employed to identify protease substrates in vivo and under physiological conditions. In addition, we explore the current trends in the protease field and the potential for future developments.
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Date
2021-08-03
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MDPI
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Keywords
Protease substrates, N-terminomics, COFRADIC, TAILS, Subtiligase, CHOPS
Citation
Mintoo, M.; Chakravarty, A.; Tilvawala, R. N-Terminomics Strategies for Protease Substrates Profiling. Molecules 2021, 26, 4699. https://doi.org/10.3390/molecules26154699