Characterization of Legumain Degradome Confirms Narrow Cleavage Specificity

Legumain or asparagine endopeptidase is a unique cysteine endopeptidase with a distinctive specificity for the hydrolysis of peptide bonds after asparagine and to a lesser extent after aspartate. It is ubiquitously expressed in various tissues and besides its involvement in immune response and other...

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Main Authors: Robert Vidmar, Matej Vizovišek, Dušan Turk, Boris Turk, Marko Fonović
Format: Article
Language:English
Published: Slovenian Chemical Society 2019-02-01
Series:Acta Chimica Slovenica
Subjects:
Online Access:https://journals.matheo.si/index.php/ACSi/article/view/4632
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author Robert Vidmar
Matej Vizovišek
Dušan Turk
Boris Turk
Marko Fonović
author_facet Robert Vidmar
Matej Vizovišek
Dušan Turk
Boris Turk
Marko Fonović
author_sort Robert Vidmar
collection DOAJ
description Legumain or asparagine endopeptidase is a unique cysteine endopeptidase with a distinctive specificity for the hydrolysis of peptide bonds after asparagine and to a lesser extent after aspartate. It is ubiquitously expressed in various tissues and besides its involvement in immune response and other physiological processes, it was also shown to play a role in pathological states such as inflammation and cancer. In order to improve our understanding of legumain substrate recognition we have performed proteomic profiling of legumain specificity on native proteins derived from MDA-MB-231 cells using two different N-terminal labelling methodologies (FPPS and ISIL). Our data revealed narrow cleavage specificity for P1 position combined with clear cleavage preference for unstructured secondary regions in the substrate proteins. No extended cleavage specificity on native proteins was observed. Moreover, a limited number of identified cleavages on individual substrates suggest its primary role in precision proteolysis and regulatory proteolytic events.
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spelling doaj.art-4b4c36c181f3416a98231308981496642022-12-21T18:57:39ZengSlovenian Chemical SocietyActa Chimica Slovenica1318-02071580-31552019-02-01661505710.17344/acsi.2018.4632657Characterization of Legumain Degradome Confirms Narrow Cleavage SpecificityRobert VidmarMatej VizovišekDušan TurkBoris TurkMarko FonovićLegumain or asparagine endopeptidase is a unique cysteine endopeptidase with a distinctive specificity for the hydrolysis of peptide bonds after asparagine and to a lesser extent after aspartate. It is ubiquitously expressed in various tissues and besides its involvement in immune response and other physiological processes, it was also shown to play a role in pathological states such as inflammation and cancer. In order to improve our understanding of legumain substrate recognition we have performed proteomic profiling of legumain specificity on native proteins derived from MDA-MB-231 cells using two different N-terminal labelling methodologies (FPPS and ISIL). Our data revealed narrow cleavage specificity for P1 position combined with clear cleavage preference for unstructured secondary regions in the substrate proteins. No extended cleavage specificity on native proteins was observed. Moreover, a limited number of identified cleavages on individual substrates suggest its primary role in precision proteolysis and regulatory proteolytic events.https://journals.matheo.si/index.php/ACSi/article/view/4632proteolysisproteasesdegradomecleavage specificitylegumain
spellingShingle Robert Vidmar
Matej Vizovišek
Dušan Turk
Boris Turk
Marko Fonović
Characterization of Legumain Degradome Confirms Narrow Cleavage Specificity
Acta Chimica Slovenica
proteolysis
proteases
degradome
cleavage specificity
legumain
title Characterization of Legumain Degradome Confirms Narrow Cleavage Specificity
title_full Characterization of Legumain Degradome Confirms Narrow Cleavage Specificity
title_fullStr Characterization of Legumain Degradome Confirms Narrow Cleavage Specificity
title_full_unstemmed Characterization of Legumain Degradome Confirms Narrow Cleavage Specificity
title_short Characterization of Legumain Degradome Confirms Narrow Cleavage Specificity
title_sort characterization of legumain degradome confirms narrow cleavage specificity
topic proteolysis
proteases
degradome
cleavage specificity
legumain
url https://journals.matheo.si/index.php/ACSi/article/view/4632
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