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Blood, 1 August 2006, Vol. 108, No. 3, pp. 791-801. Prepublished online as a Blood First Edition Paper on April 18, 2006; DOI 10.1182/blood-2005-11-007799. This Article Full Text (PDF) Supplemental Tables All Versions of this Article: blood-2005-11-007799v1 108/3/791    most recent Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Rights and Permissions Citing Articles Citing Articles via HighWire Citing Articles via CrossRef Citing Articles via Google Scholar Google Scholar Articles by Pasini, E. M Articles by Mann, M. Search for Related Content PubMed PubMed Citation Articles by Pasini, E. M Articles by Mann, M. Social Bookmarking                   What's this?  Previous Article  |  Next Article  Submitted November 17, 2005 Accepted March 13, 2006 In-depth analysis of the membrane and cytosolic proteome of red blood cells Erica M Pasini, Morten Kirkegaard, Peter Mortensen, Hans U Lutz, Alan Thomas, and Matthias Mann* Biomedical Primate Research Centre, Rijswijk, The Netherlands Center for Experimental Bioinformatics,University of Southern Denmark and Max-Planck Institute Institute of Biochemistry, Swiss Federal Institute of Technology, Zuerich, Switzerland Max-Planck Institute for Biochemistry * Corresponding author; email: mmann{at}biochem.mpg.de. As well as transport of oxygen and carbon dioxide to and from the tissues, red blood cells (RBCs) of vertebrates have a range of other functions attributed to them. Diseases compromising RBC performance in any of these functions warrant in depth study. Furthermore the human RBC is a vital host cell for the malaria parasite. Much has been learned from classical biochemical approaches about RBC composition, and membrane organization. Here, we employ mass spectrometry (MS) based proteomics to characterize the normal RBC protein profile. The aim of this study was to obtain the most complete and informative human RBC proteome possible by combining high accuracy, high sensitivity protein identification technology (quadrupole time of flight and Fourier Transform MS) with selected biochemical procedures for sample preparation. A total of 340 membrane proteins and 252 soluble proteins were identified, validated and categorized in terms of sub-cellular localization, protein family and function. Splice isoforms of proteins were identified and polypeptides that migrated with anomalously high or low apparent molecular weights could be grouped into either ubiquitinylated, partially degraded and ester-linked complexes. Our data reveals unexpected complexity of the RBC proteome, provide a wealth of data on its composition, sheds light on several open issues in RBC biology and is a departure point for comprehensive understanding of RBC functions. CiteULike    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this? This article has been cited by other articles: E. M. Pasini, M. Kirkegaard, D. Salerno, P. Mortensen, M. Mann, and A. W. Thomas Deep Coverage Mouse Red Blood Cell Proteome: A First Comparison with the Human Red Blood Cell Mol. Cell. Proteomics, July 1, 2008; 7(7): 1317 - 1330. [Abstract] [Full Text] [PDF] A. A. Khan, T. Hanada, M. Mohseni, J.-J. Jeong, L. Zeng, M. Gaetani, D. Li, B. C. Reed, D. W. Speicher, and A. H. Chishti Dematin and Adducin Provide a Novel Link between the Spectrin Cytoskeleton and Human Erythrocyte Membrane by Directly Interacting with Glucose Transporter-1 J. Biol. Chem., May 23, 2008; 283(21): 14600 - 14609. [Abstract] [Full Text] [PDF] E. 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