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Molecular & Cellular Proteomics 4:1754-1761, 2005.
© 2005 by The American Society for Biochemistry and Molecular Biology, Inc.

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Research

The Human Platelet Membrane Proteome Reveals Several New Potential Membrane Proteins^*,S

Jan Moebius, René Peiman Zahedi, Urs Lewandrowski, Claudia Berger, Ulrich Walter and Albert Sickmann^,¶

From the Protein Mass Spectrometry and Functional Proteomics Group, Rudolf Virchow Center for Experimental Biomedicine, Julius Maximilians University of Wuerzburg, Versbacher Strasse 9, 97078 Wuerzburg, Germany and the Institute for Clinical Biochemistry and Pathobiochemistry, Julius Maximilians University of Wuerzburg, Building D20, Josef-Schneider Strasse 2, 97080 Wuerzburg, Germany

We present the first focused proteome study on human platelet membranes. Due to the removal of highly abundant cytoskeletal proteins a wide spectrum of known platelet membrane proteins and several new and hypothetical proteins were accessible. In contrast to other proteome studies we focused on prefractionation and purification of membranes from human platelets according to published protocols to reduce sample complexity and enrich interesting membrane proteins. Subsequently protein separation by common one-dimensional SDS-PAGE as well as the combined benzyldimethyl-n-hexadecylammonium chloride/SDS separation technique was performed prior to mass spectrometry analysis by nano-LC-ESI-MS/MS. We demonstrate that the application of both separation systems in parallel is required for maximization of protein tagging out of a complex sample. Furthermore the identification of several potential membrane proteins in human platelets yields new potential targets in functional platelet research.

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