Dataset Information

A mass spectrometric-derived cell surface protein atlas.

ABSTRACT: Cell surface proteins are major targets of biomedical research due to their utility as cellular markers and their extracellular accessibility for pharmacological intervention. However, information about the cell surface protein repertoire (the surfaceome) of individual cells is only sparsely available. Here, we applied the Cell Surface Capture (CSC) technology to 41 human and 31 mouse cell types to generate a mass-spectrometry derived Cell Surface Protein Atlas (CSPA) providing cellular surfaceome snapshots at high resolution. The CSPA is presented in form of an easy-to-navigate interactive database, a downloadable data matrix and with tools for targeted surfaceome rediscovery (http://wlab.ethz.ch/cspa). The cellular surfaceome snapshots of different cell types, including cancer cells, resulted in a combined dataset of 1492 human and 1296 mouse cell surface glycoproteins, providing experimental evidence for their cell surface expression on different cell types, including 136 G-protein coupled receptors and 75 membrane receptor tyrosine-protein kinases. Integrated analysis of the CSPA reveals that the concerted biological function of individual cell types is mainly guided by quantitative rather than qualitative surfaceome differences. The CSPA will be useful for the evaluation of drug targets, for the improved classification of cell types and for a better understanding of the surfaceome and its concerted biological functions in complex signaling microenvironments.

SUBMITTER: Bausch-Fluck D

PROVIDER: S-EPMC4404347 | biostudies-literature | 2015

REPOSITORIES: biostudies-literature

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A mass spectrometric-derived cell surface protein atlas.

Bausch-Fluck Damaris D Hofmann Andreas A Bock Thomas T Frei Andreas P AP Cerciello Ferdinando F Jacobs Andrea A Moest Hansjoerg H Omasits Ulrich U Gundry Rebekah L RL Yoon Charles C Schiess Ralph R Schmidt Alexander A Mirkowska Paulina P Härtlová Anetta A Van Eyk Jennifer E JE Bourquin Jean-Pierre JP Aebersold Ruedi R Boheler Kenneth R KR Zandstra Peter P Wollscheid Bernd B

PloS one 20150420 3

Cell surface proteins are major targets of biomedical research due to their utility as cellular markers and their extracellular accessibility for pharmacological intervention. However, information about the cell surface protein repertoire (the surfaceome) of individual cells is only sparsely available. Here, we applied the Cell Surface Capture (CSC) technology to 41 human and 31 mouse cell types to generate a mass-spectrometry derived Cell Surface Protein Atlas (CSPA) providing cellular surfaceo ...[more]

PMID: 25894527

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Project description:Supramolecular membrane complexes of low abundance are difficult to study by routine bioanalytical techniques. The plasmalemmal complex consisting of sarcoglycans, dystroglycans, dystrobrevins and syntrophins, which is closely associated with the membrane cytoskeletal protein dystrophin, represents such a high?molecular?mass protein assembly in skeletal muscles. The almost complete loss of the dystrophin isoform Dp427?M and concomitant reduction in the dystrophin?associated glycoprotein complex is the underlying cause of the highly progressive neuromuscular disorder named Duchenne muscular dystrophy. This gives the detailed characterization of the dystrophin complex considerable pathophysiological importance. In order to carry out a comprehensive mass spectrometric identification of the dystrophin?glycoprotein complex, in this study, we used extensive subcellular fractionation and enrichment procedures prior to subproteomic analysis. Mass spectrometry identified high levels of full?length dystrophin isoform Dp427?M, ?/??dystroglycans, ?/?/?/??sarcoglycans, ?1/?1/?2?syntrophins and ?/??dystrobrevins in highly purified sarcolemma vesicles. By contrast, lower levels were detected in transverse tubules and no components of the dystrophin complex were identified in triads. For comparative purposes, the presence of organellar marker proteins was studied in crude surface membrane preparations vs. enriched fractions from the sarcolemma, transverse tubules and triad junctions using gradient gel electrophoresis and on?membrane digestion. This involved the subproteomic assessment of various ion?regulatory proteins and excitation?contraction coupling components. The comparative profiling of skeletal muscle fractions established a relatively restricted subcellular localization of the dystrophin?glycoprotein complex in the muscle fibre periphery by proteomic means and clearly demonstrated the absence of dystrophin from triad junctions by sensitive mass spectrometric analysis.

Dataset Information

A mass spectrometric-derived cell surface protein atlas.

Publications

A mass spectrometric-derived cell surface protein atlas.

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