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Database (Oxford). 2015 Jun 14;2015:bav056. doi: 10.1093/database/bav056. Print 2015.

Inconsistencies in the red blood cell membrane proteome analysis: generation of a database for research and diagnostic applications.

Author information

1
MTA-SE Molecular Biophysics Research Group, Hungarian Academy of Sciences, Tűzoltó u. 37-47, H-1094 Budapest, Hungary, Department of Biophysics and Radiation Biology, Semmelweis University, Tűzoltó u. 37-47, H-1094 Budapest, Hungary, Department of Clinical Pharmacology and Toxicology, University Hospital Zurich, Raemistrasse 100, CH-8091 Zurich, Switzerland, Institute of Enzymology, Research Centre for Natural Sciences, Hungarian Academy of Sciences, Magyar tudósok körútja 2, H-1117 Budapest, Hungary and Functional Genomics Center Zurich, University of Zurich, ETH Zurich, Winterthurerstrasse 190, CH-8057 Zurich, Switzerland MTA-SE Molecular Biophysics Research Group, Hungarian Academy of Sciences, Tűzoltó u. 37-47, H-1094 Budapest, Hungary, Department of Biophysics and Radiation Biology, Semmelweis University, Tűzoltó u. 37-47, H-1094 Budapest, Hungary, Department of Clinical Pharmacology and Toxicology, University Hospital Zurich, Raemistrasse 100, CH-8091 Zurich, Switzerland, Institute of Enzymology, Research Centre for Natural Sciences, Hungarian Academy of Sciences, Magyar tudósok körútja 2, H-1117 Budapest, Hungary and Functional Genomics Center Zurich, University of Zurich, ETH Zurich, Winterthurerstrasse 190, CH-8057 Zurich, Switzerland hegedus@hegelab.org.
2
MTA-SE Molecular Biophysics Research Group, Hungarian Academy of Sciences, Tűzoltó u. 37-47, H-1094 Budapest, Hungary, Department of Biophysics and Radiation Biology, Semmelweis University, Tűzoltó u. 37-47, H-1094 Budapest, Hungary, Department of Clinical Pharmacology and Toxicology, University Hospital Zurich, Raemistrasse 100, CH-8091 Zurich, Switzerland, Institute of Enzymology, Research Centre for Natural Sciences, Hungarian Academy of Sciences, Magyar tudósok körútja 2, H-1117 Budapest, Hungary and Functional Genomics Center Zurich, University of Zurich, ETH Zurich, Winterthurerstrasse 190, CH-8057 Zurich, Switzerland.
3
MTA-SE Molecular Biophysics Research Group, Hungarian Academy of Sciences, Tűzoltó u. 37-47, H-1094 Budapest, Hungary, Department of Biophysics and Radiation Biology, Semmelweis University, Tűzoltó u. 37-47, H-1094 Budapest, Hungary, Department of Clinical Pharmacology and Toxicology, University Hospital Zurich, Raemistrasse 100, CH-8091 Zurich, Switzerland, Institute of Enzymology, Research Centre for Natural Sciences, Hungarian Academy of Sciences, Magyar tudósok körútja 2, H-1117 Budapest, Hungary and Functional Genomics Center Zurich, University of Zurich, ETH Zurich, Winterthurerstrasse 190, CH-8057 Zurich, Switzerland MTA-SE Molecular Biophysics Research Group, Hungarian Academy of Sciences, Tűzoltó u. 37-47, H-1094 Budapest, Hungary, Department of Biophysics and Radiation Biology, Semmelweis University, Tűzoltó u. 37-47, H-1094 Budapest, Hungary, Department of Clinical Pharmacology and Toxicology, University Hospital Zurich, Raemistrasse 100, CH-8091 Zurich, Switzerland, Institute of Enzymology, Research Centre for Natural Sciences, Hungarian Academy of Sciences, Magyar tudósok körútja 2, H-1117 Budapest, Hungary and Functional Genomics Center Zurich, University of Zurich, ETH Zurich, Winterthurerstrasse 190, CH-8057 Zurich, Switzerland.
4
MTA-SE Molecular Biophysics Research Group, Hungarian Academy of Sciences, Tűzoltó u. 37-47, H-1094 Budapest, Hungary, Department of Biophysics and Radiation Biology, Semmelweis University, Tűzoltó u. 37-47, H-1094 Budapest, Hungary, Department of Clinical Pharmacology and Toxicology, University Hospital Zurich, Raemistrasse 100, CH-8091 Zurich, Switzerland, Institute of Enzymology, Research Centre for Natural Sciences, Hungarian Academy of Sciences, Magyar tudósok körútja 2, H-1117 Budapest, Hungary and Functional Genomics Center Zurich, University of Zurich, ETH Zurich, Winterthurerstrasse 190, CH-8057 Zurich, Switzerland hegedus@hegelab.org bstieger@kpt.uzh.ch.

Abstract

Based on recent results, the determination of the easily accessible red blood cell (RBC) membrane proteins may provide new diagnostic possibilities for assessing mutations, polymorphisms or regulatory alterations in diseases. However, the analysis of the current mass spectrometry-based proteomics datasets and other major databases indicates inconsistencies-the results show large scattering and only a limited overlap for the identified RBC membrane proteins. Here, we applied membrane-specific proteomics studies in human RBC, compared these results with the data in the literature, and generated a comprehensive and expandable database using all available data sources. The integrated web database now refers to proteomic, genetic and medical databases as well, and contains an unexpected large number of validated membrane proteins previously thought to be specific for other tissues and/or related to major human diseases. Since the determination of protein expression in RBC provides a method to indicate pathological alterations, our database should facilitate the development of RBC membrane biomarker platforms and provide a unique resource to aid related further research and diagnostics.

PMID:
26078478
PMCID:
PMC4480073
DOI:
10.1093/database/bav056
[Indexed for MEDLINE]
Free PMC Article

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