In-depth analysis of the membrane
Blood, 2006, 108: 791-801. >>NEW<<
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
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.