Evidence map›Paper›PMID 40970443›Full record

ArticleProtein science : a publication of the Protein Society2025

Employing complementary fractionation-based N-terminomics approaches enhances the identification of legumain cleavage events in naïve and inflamed colon tissue.

Alexander R Ziegler, Benjamin L Parker, Nichollas E Scott, Laura E Edgington-Mitchell

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Article in Protein science : a publication of the Protein Society, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

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0cells of the map it votes in
3citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

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3 · Its place in the literature

Who cites it

3 citing papers in PubMed.

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4 · The record

Corrections and comments

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5 · Who and what money

Authors and funding

4 authors.

Alexander R ZieglerDepartment of Biochemistry and Pharmacology, Bio21 Molecular Science and Biotechnology Institute, The University of Melbourne, Parkville, Victoria, Australia.
Benjamin L ParkerDepartment of Anatomy and Physiology, Medical Building 181, The University of Melbourne, Parkville, Victoria, Australia.
Nichollas E ScottDepartment of Microbiology and Immunology, Peter Doherty Institute, The University of Melbourne, Parkville, Victoria, Australia.
Laura E Edgington-MitchellDepartment of Biochemistry and Pharmacology, Bio21 Molecular Science and Biotechnology Institute, The University of Melbourne, Parkville, Victoria, Australia.ORCID 0000-0002-6810-6149

Funding

Australian Research Council DP210100362Australian Research Council FT200100270National Health and Medical Research Council 2011119National Health and Medical Research Council 2018980
6 · The paper itself

Abstract

The mammalian lysosomal protease legumain is often dysregulated in pathophysiological conditions including inflammation, neurodegeneration, and cancer, yet its proteolytic targets are poorly defined. To profile protease substrates, degradomics techniques typically employ enrichment strategies to select for sub-stoichiometric and low-abundance peptides generated by proteolytic cleavage. However, recent advancements in degradomics techniques have revealed N-termini enrichment can be circumvented if peptide-based fractionation is employed, enabling simultaneous proteome and N-terminome analysis. Herein, we compare the previously published enrichment-free N-terminomics approach using high-field asymmetric waveform ion mobility spectrometry (FAIMS) to offline basic reverse-phase (bRP) fractionation to assess the complementarity of these fractionation methods for simultaneous proteomic and degradomic analyses. While at the protein level FAIMS and bRP provide access to overlapping proteomic coverage, at the N-terminus level each fractionation technique reveals unique cleavage information. Combining data from the two fractionation approaches revealed 6499 N-terminal peptides with N-terminal TMTpro labeling, allowing the identification of cleavage events modulated in the context of legumain deficiency in naïve murine colons and during dextran sulfate sodium (DSS)-induced colitis. Among these N-termini, we identify 35 putative legumain substrates in naïve and 41 in the DSS-treated colons, supporting a role for legumain in both pro-inflammatory and physiological conditions. Use of an additional negative selection method, High-efficiency Undecanal-based N-Termini EnRichment (HUNTER), further supplements this list of identified legumain substrates. Combined, this study identifies multiple putative substrates of legumain in healthy and inflamed murine colons as well as demonstrates the utility of using complementary fractionation approaches for degradomics studies.

Indexed as

ColitisColonCysteine EndopeptidasesProteomicsAnimalsAsparaginyl EndopeptidaseMiceMice, Inbred C57BLProteolysisProteomeAsparaginyl EndopeptidaseCysteine EndopeptidasesProteomebasic reverse‐phasecolitisFAIMSfractionationHUNTERlegumainN‐terminomicsproteasesubstratesTMTpro

Identifiers

PMID40970443
PMCPMC12447244

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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.