A mass spectrometric-derived cell surface protein atlas
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 availab...
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Published in | PloS one Vol. 10; no. 3; p. e0121314 |
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Main Authors | , , , , , , , , , , , , , , , , , , , |
Format | Journal Article |
Language | English |
Published |
United States
Public Library of Science
20.04.2015
Public Library of Science (PLoS) |
Subjects | |
Online Access | Get full text |
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Summary: | 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. |
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Bibliography: | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 Current Address: Novartis Institute of Biomedical Research, Novartis, Basel, Switzerland Competing Interests: The authors have declared that no competing interests exist. Current Address: Institute of Molecular Life Sciences, University of Zurich, Zurich, Switzerland Current Address: College of Life Sciences, University of Dundee, Dundee, United Kingdom Current Address: James Thoracic Center, James Cancer Center, The Ohio State University Medical Center, Columbus, Ohio, United States of America Conceived and designed the experiments: DBF BW KRB PZ RA. Performed the experiments: DBF AH TB APF FC AJ HM RLG CY RS AS PM AH. Analyzed the data: DBF UO. Contributed reagents/materials/analysis tools: AS APF FC TB BW. Wrote the paper: DBF BW. Supervised experiments: JVE JPB. Current Address: Department of Microbiology and Immunology, Stanford School of Medicine, Stanford, California, United States of America Current Address: Proteomics Core Facility, Biozentrum, University of Basel, Basel, Switzerland Current Address: ProteoMediX AG, Schlieren, Switzerland Current Address: Cedars-Sinai, Clinical Biosystem Research Institute, Los Angeles, California, United States of America Current Address: European Molecular Biology Laboratory, Heidelberg, Germany |
ISSN: | 1932-6203 1932-6203 |
DOI: | 10.1371/journal.pone.0121314 |