A hidden human proteome signature characterizes ...
Document type :
Article dans une revue scientifique: Article original
PMID :
Permalink :
Title :
A hidden human proteome signature characterizes the epithelial mesenchymal transition program
Author(s) :
Vergara, Daniele [Auteur]
Verri, Tiziano [Auteur]
Damato, Marina [Auteur]
Trerotola, Marco [Auteur]
Simeone, Pasquale [Auteur]
Franck, Julien [Auteur]
Protéomique, Réponse Inflammatoire, Spectrométrie de Masse (PRISM) - U1192
FOURNIER, Isabelle [Auteur]
Protéomique, Réponse Inflammatoire, Spectrométrie de Masse (PRISM) - U1192
Salzet, Michel [Auteur]
Protéomique, Réponse Inflammatoire, Spectrométrie de Masse (PRISM) - U1192
Maffia, Michele [Auteur]
Verri, Tiziano [Auteur]
Damato, Marina [Auteur]
Trerotola, Marco [Auteur]
Simeone, Pasquale [Auteur]
Franck, Julien [Auteur]

Protéomique, Réponse Inflammatoire, Spectrométrie de Masse (PRISM) - U1192
FOURNIER, Isabelle [Auteur]

Protéomique, Réponse Inflammatoire, Spectrométrie de Masse (PRISM) - U1192
Salzet, Michel [Auteur]

Protéomique, Réponse Inflammatoire, Spectrométrie de Masse (PRISM) - U1192
Maffia, Michele [Auteur]
Journal title :
Current Pharmaceutical Design
Abbreviated title :
Curr. Pharm. Des.
Publication date :
2020-01-28
ISSN :
1873-4286
Keyword(s) :
proteome
alternative proteins
breast cancer
Epithelial mesenchymal transition
OpenProt database
predicted isoforms
alternative proteins
breast cancer
Epithelial mesenchymal transition
OpenProt database
predicted isoforms
HAL domain(s) :
Sciences du Vivant [q-bio]
English abstract : [en]
BACKGROUND: Molecular changes associated with the initiation of the epithelial to mesenchymal transition (EMT) program involve alterations of large proteome-based networks. The role of protein products mapping to non-coding ...
Show more >BACKGROUND: Molecular changes associated with the initiation of the epithelial to mesenchymal transition (EMT) program involve alterations of large proteome-based networks. The role of protein products mapping to non-coding genomic regions is still unexplored. OBJECTIVE: The goal of this study was the identification of an alternative protein signature in breast cancer cellular models with a distinct expression of EMT markers. METHODS: We profiled MCF-7 and MDA-MB-231 cells using liquid-chromatography mass/spectrometry (LCMS/ MS) and interrogated the OpenProt database to identify novel predicted isoforms and novel predicted proteins from alternative open reading frames (AltProts). RESULTS: Our analysis revealed an AltProt and isoform protein signature capable of classifying the two breast cancer cell lines. Among the most highly expressed alternative proteins, we observed proteins potentially associated with inflammation, metabolism and EMT. CONCLUSION: Here, we present an AltProts signature associated with EMT. Further studies will be needed to define their role in cancer progression.Show less >
Show more >BACKGROUND: Molecular changes associated with the initiation of the epithelial to mesenchymal transition (EMT) program involve alterations of large proteome-based networks. The role of protein products mapping to non-coding genomic regions is still unexplored. OBJECTIVE: The goal of this study was the identification of an alternative protein signature in breast cancer cellular models with a distinct expression of EMT markers. METHODS: We profiled MCF-7 and MDA-MB-231 cells using liquid-chromatography mass/spectrometry (LCMS/ MS) and interrogated the OpenProt database to identify novel predicted isoforms and novel predicted proteins from alternative open reading frames (AltProts). RESULTS: Our analysis revealed an AltProt and isoform protein signature capable of classifying the two breast cancer cell lines. Among the most highly expressed alternative proteins, we observed proteins potentially associated with inflammation, metabolism and EMT. CONCLUSION: Here, we present an AltProts signature associated with EMT. Further studies will be needed to define their role in cancer progression.Show less >
Language :
Anglais
Audience :
Internationale
Popular science :
Non
Administrative institution(s) :
INSERM
Université de Lille
Université de Lille
Submission date :
2022-06-15T13:59:24Z