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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 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 Citation Map 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. Related Collections Red Cells Plenary Papers Cytoskeleton Social Bookmarking                   What's this?  Previous Article  |  Table of Contents  |  Next Article  PLENARY PAPERS In-depth analysis of the membrane and cytosolic proteome of red blood cells Erica M. Pasini, Morten Kirkegaard, Peter Mortensen, Hans U. Lutz, Alan W. Thomas, and Matthias Mann From the Biomedical Primate Research Centre, Lange Kleiweg, Rijswijk, The Netherlands; Institute of Biochemistry, Swiss Federal Institute of Technology, ETH-Hönggerberg, Zurich, Switzerland; Center for Experimental Bioinformatics, University of Southern Denmark, Odense, Denmark; and Max-Planck Institute for Biochemistry, Amklopferspitz, Martinsreid, Germany. In addition to transporting oxygen and carbon dioxide to and from the tissues, a range of other functions are attributed to red blood cells (RBCs) of vertebrates. 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 use 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 subcellular 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, or ester-linked complexes. Our data reveal unexpected complexity of the RBC proteome, provide a wealth of data on its composition, shed light on several open issues in RBC biology, and form 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: M. Desmarets, C. M. Cadwell, K. R. Peterson, R. Neades, and J. C. Zimring Minor histocompatibility antigens on transfused leukoreduced units of red blood cells induce bone marrow transplant rejection in a mouse model Blood, September 10, 2009; 114(11): 2315 - 2322. [Abstract] [Full Text] [PDF] R. Chandramohanadas, P. H. Davis, D. P. Beiting, M. B. Harbut, C. Darling, G. Velmourougane, M. Y. Lee, P. A. Greer, D. S. Roos, and D. C. Greenbaum Apicomplexan Parasites Co-Opt Host Calpains to Facilitate Their Escape from Infected Cells Science, May 8, 2009; 324(5928): 794 - 797. [Abstract] [Full Text] [PDF] Z. Wang, K. Park, F. 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