HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text Full Text (PDF) Supplemental Data All Versions of this Article: M800172-MCP200v1 8/4/624    most recent Submit a response Alert me when this article is cited Alert me when eLetters are posted Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Request Permissions Glossary Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Schiess, R. Articles by Aebersold, R. Search for Related Content PubMed PubMed Citation Articles by Schiess, R. Articles by Aebersold, R. Social Bookmarking                      What's this?

Molecular & Cellular Proteomics 8:624-638, 2009.
© 2009 by The American Society for Biochemistry and Molecular Biology, Inc.

---

Research

Analysis of Cell Surface Proteome Changes via Label-free, Quantitative Mass Spectrometry^*,S

Ralph Schiess^,,¶, Lukas N. Mueller^,¶, Alexander Schmidt^,¶, Markus Mueller^||, Bernd Wollscheid^,**, and Ruedi Aebersold^,¶,,¶¶

From the Institute of Molecular Systems Biology, Eidgenössische Technische Hochschule (ETH) Zurich, 8093 Zurich, Switzerland, Ph.D. Program in Molecular Life Science and ^¶¶ Faculty of Science, University of Zurich, 8057 Zurich, Switzerland, ^¶ Competence Center for Systems Physiology and Metabolic Disease, 8093 Zurich, Switzerland, ^|| Swiss Institute of Bioinformatics, 1211 Geneva, Switzerland, ^** National Center for Competence in Research (NCCR) Neuro Center for Proteomics, ETH and University of Zurich, 8093 Zurich, Switzerland, and Institute for Systems Biology, Seattle, Washington 98103

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.

CiteULike    Complore    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this?

This article has been cited by other articles:

				R. L. Gundry, K. Raginski, Y. Tarasova, I. Tchernyshyov, D. Bausch-Fluck, S. T. Elliott, K. R. Boheler, J. E. Van Eyk, and B. Wollscheid The Mouse C2C12 Myoblast Cell Surface N-Linked Glycoproteome: IDENTIFICATION, GLYCOSITE OCCUPANCY, AND MEMBRANE ORIENTATION Mol. Cell. Proteomics, November 1, 2009; 8(11): 2555 - 2569. [Abstract] [Full Text] [PDF]