Titre
Profiling treatment-specific post-translational modifications in a complex proteome with subtractive substrate phage display
Type
article
Institution
UNIL/CHUV/Unisanté + institutions partenaires
Périodique
Auteur(s)
Tenzer, A.
Auteure/Auteur
Hofstetter, B.
Auteure/Auteur
Sauser, C.
Auteure/Auteur
Bodis, S.
Auteure/Auteur
Schubiger, A. P.
Auteure/Auteur
Bonny, C.
Auteure/Auteur
Pruschy, M.
Auteure/Auteur
Liens vers les personnes
Liens vers les unités
ISSN
1615-9853
Statut éditorial
Publié
Date de publication
2004-09
Volume
4
Numéro
9
Première page
2796
Dernière page/numéro d’article
804
Notes
Journal Article
Research Support, Non-U.S. Gov't --- Old month value: Sep
Research Support, Non-U.S. Gov't --- Old month value: Sep
Résumé
Proteolytic activation of zymogens or controlled degradation of inhibitory factors is part of a major regulatory system on the post-translational level to regulate treatment induced cellular stress responses. The identification of differential activity based substrates is thus of high interest to prioritize and validate candidate targets for drug discovery. Here we present a novel subtractive substrate phage display screening method for the selection of treatment induced post-translational peptide modifications in complex proteomes. We investigated this approach with tumor cells in response to a protease activating anticancer treatment modality using subtractive and iterative screening of cellular extracts derived from control and treated cells. Specific phage were identified that served as substrates for proteolytic activities in response to treatment related activity changes and could be distinguished from substrates for unspecific proteolytic background activities. Novel, selected peptide substrates were investigated in vitro and in vivo and showed high substrate specificity and functional biological significance.
Sujets
PID Serval
serval:BIB_F95E06391CAD
PMID
Date de création
2008-01-25T13:16:00.498Z
Date de création dans IRIS
2025-05-21T05:24:18Z