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Deja vu in proteomics. A hit parade of repeatedly identified differentially expressed proteins
J Petrak, R Ivanek, O Toman, R Cmejla, J Cmejlova, D Vyoral, J Zivny, CD Vulpe
Language English Country Germany
Grant support
NR8930
MZ0
CEP Register
Digital library NLK
Full text - Article
Source
NLK
Wiley Online Library (archiv)
from 2001-01-01 to 2012-12-31
- MeSH
- Electrophoresis, Gel, Two-Dimensional MeSH
- Financing, Organized MeSH
- Phosphopyruvate Hydratase biosynthesis MeSH
- Transcription, Genetic MeSH
- Glyceraldehyde-3-Phosphate Dehydrogenase (Phosphorylating) metabolism MeSH
- Rats MeSH
- Humans MeSH
- Multigene Family MeSH
- Mice MeSH
- Neoplasm Proteins biosynthesis MeSH
- Peroxiredoxins metabolism MeSH
- HSP27 Heat-Shock Proteins MeSH
- Heat-Shock Proteins biosynthesis MeSH
- Proteomics methods MeSH
- Gene Expression Regulation MeSH
- Gene Expression Profiling MeSH
- Animals MeSH
- Check Tag
- Rats MeSH
- Humans MeSH
- Mice MeSH
- Animals MeSH
After reading many 2-DE-based articles featuring lists of the differentially expressed proteins, one starts experiencing a disturbing deja vu. The same proteins seem to predominate regardless of the experiment, tissue or species. To quantify the occurrence of individual differentially expressed proteins in 2-DE experiment reports, we compiled the identities of differentially expressed proteins identified in human, mouse, and rat tissues published in three recent volumes of Proteomics and calculated the appearance of the most predominant proteins in the dataset. The most frequently identified protein is a highly abundant glycolytic enzyme enolase 1, differentially expressed in nearly every third experiment on both human and rodent tissues. Heat-shock protein 27 (HSP27) and heat-shock protein 60 (HSP60) were differentially expressed in about 30 percent of human and rodent samples, respectively. Considering protein families as units, keratins and peroxiredoxins are the most frequently identified molecules, with at least one member of the group being differentially expressed in about 40 percent of all experiments. We suggest that the frequent identification of these proteins must be considered in the interpretation of any 2-DE studies. We consider if these commonly observed changes represent common cellular stress responses or are a reflection of the technical limitations of 2-DE.
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- $a After reading many 2-DE-based articles featuring lists of the differentially expressed proteins, one starts experiencing a disturbing deja vu. The same proteins seem to predominate regardless of the experiment, tissue or species. To quantify the occurrence of individual differentially expressed proteins in 2-DE experiment reports, we compiled the identities of differentially expressed proteins identified in human, mouse, and rat tissues published in three recent volumes of Proteomics and calculated the appearance of the most predominant proteins in the dataset. The most frequently identified protein is a highly abundant glycolytic enzyme enolase 1, differentially expressed in nearly every third experiment on both human and rodent tissues. Heat-shock protein 27 (HSP27) and heat-shock protein 60 (HSP60) were differentially expressed in about 30 percent of human and rodent samples, respectively. Considering protein families as units, keratins and peroxiredoxins are the most frequently identified molecules, with at least one member of the group being differentially expressed in about 40 percent of all experiments. We suggest that the frequent identification of these proteins must be considered in the interpretation of any 2-DE studies. We consider if these commonly observed changes represent common cellular stress responses or are a reflection of the technical limitations of 2-DE.
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