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Submitted on July 3, 2003
Revised on October 10, 2003
Accepted on October 21, 2003

Expression profiling of lymphocyte plasma membrane proteins

Matthew J. Peirce, Robin Wait, Shajna Begum, Jeremy Saklatvala, and Andrew P. Cope

Cell Signalling, Kennedy Institute of Rheumatology, London W6 8LH

Corresponding Author: m.peirce{at}imperial.ac.uk

The physicochemical properties of plasma membrane proteins of mammalian cells render them refractory to systematic analysis by two-dimensional electrophoresis. We have therefore used in vivo cell surface labelling with a water-soluble biotinylation reagent, followed by cell lysis and membrane purification, prior to affinity capture of biotinylated proteins. Purified membrane proteins were then separated by solution-phase isoelectric focusing and SDS PAGE, and identified by HPLC electrospray/tandem MS. Using this approach, we identified 42 plasma membrane proteins from a murine T cell hybridoma and 46 from unfractionated primary murine splenocytes. These included three unexpected proteins; nicastrin, osteoclast inhibitory lectin (OCIL) and a transmembrane domain-containing hypothetical protein of 11.4kDa. Following stimulation of murine splenocytes with phorbol ester and calcium ionophore we observed differences in expression of CD69, MHC class II molecules, the glucocorticoid-induced TNF receptor family-related gene product (GITR) and surface IgM and IgD that were subsequently confirmed by Western blot or flow cytometric analysis. This approach offers a generic and powerful strategy for investigating differential expression of surface proteins in many cell types under varying environmental and pathophysiological conditions.


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