Analysis of cell surface proteome changes via label-free, quantitative mass spectrometry

Schiess, Ralph and Mueller, Lukas N. and Schmidt, Alexander and Mueller, Markus and Wollscheid, Bernd and Aebersold, Ruedi . (2009) Analysis of cell surface proteome changes via label-free, quantitative mass spectrometry. Molecular and Cellular Proteomics, 8 (4). pp. 624-638.

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Official URL: http://edoc.unibas.ch/45911/

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We present a mass spectrometry-based strategy for the specific detection and quantification of cell surface proteome changes. The method is based on the label-free quantification of peptide patterns acquired by high mass accuracy mass spectrometry using new software tools and the cell surface capturing technology that selectively enriches glycopeptides exposed to the cell exterior. The method was applied to monitor dynamic protein changes in the cell surface glycoproteome of Drosophila melanogaster cells. The results led to the construction of a cell surface glycoprotein atlas consisting of 202 cell surface glycoproteins of D. melanogaster Kc167 cells and indicated relative quantitative changes of cell surface glycoproteins in four different cellular states. Furthermore we specifically investigated cell surface proteome changes upon prolonged insulin stimulation. The data revealed insulin-dependent cell surface glycoprotein dynamics, including insulin receptor internalization, and linked these changes to intracellular signaling networks.
Faculties and Departments:05 Faculty of Science > Departement Biozentrum > Services Biozentrum > Proteomics (Schmidt)
UniBasel Contributors:Schmidt, Alexander
Item Type:Article, refereed
Article Subtype:Research Article
Publisher:American Society for Biochemistry and Molecular Biology
Note:Publication type according to Uni Basel Research Database: Journal article
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Last Modified:29 Nov 2017 08:51
Deposited On:29 Nov 2017 08:51

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