Qualitative improvement and quantitative assessment of N-terminomics

Proteomics
Vilém GuryčaPaul Cutler

Abstract

Proteolysis represents one of the most tightly controlled physiological processes, as proteases create events that will typically commit pathways in an irreversible manner. Despite their implication in nearly all biological systems, our understanding of the role of proteases in disease pathology is often limited. Several approaches to studying proteolytic activity as it relates to biology, pathophysiology, and drug therapy have been published, including the recently described terminal amine isotopic labeling of substrates (TAILS) strategy by Kleifeld and colleagues. Here, we investigate TAILS as a methodology based on targeted enrichment and mass spectrometric detection of endogenous N-terminal peptides from clinically relevant biological samples and its potential to provide quantitative information on proteolysis and elucidation of the protease cleavage sites. While optimizing the most current protocol, by switching to a streamlined one-tube format and simplifying the reagents' removal steps, we demonstrate the advantages over previously published methods and provide solutions to some of the technical challenges presented in the Kleifeld publication. We also identify some of the current and unresolved limitations. We use human...Continue Reading

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Citations

Feb 16, 2013·Journal of Proteome Research·Bas van de WaterbeemdAd P J M de Jong
May 30, 2015·International Journal of Mass Spectrometry·Zhiyu LiDavid E Clemmer
Aug 15, 2014·Proteomics·Erica M Hartmann, Jean Armengaud
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Aug 7, 2018·Journal of Proteome Research·Cristal Reyna ThompsonPatricia A Champion
Jun 5, 2015·ACS Chemical Biology·Giada MarinoChristopher M Overall

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