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: M500216-MCP200v1 4/12/1968    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 Nunomura, K. Articles by Isobe, T. Search for Related Content PubMed PubMed Citation Articles by Nunomura, K. Articles by Isobe, T. Social Bookmarking                      What's this?

Molecular & Cellular Proteomics 4:1968-1976, 2005.
© 2005 by The American Society for Biochemistry and Molecular Biology, Inc.

---

Research

Cell Surface Labeling and Mass Spectrometry Reveal Diversity of Cell Surface Markers and Signaling Molecules Expressed in Undifferentiated Mouse Embryonic Stem Cells ^*,S

Kazuto Nunomura, Kohji Nagano, Chiharu Itagaki, Masato Taoka, Nobuko Okamura^,¶, Yoshio Yamauchi, Sumio Sugano^||, Nobuhiro Takahashi^**, Tomonori Izumi and Toshiaki Isobe^,,

From the Division of Proteomics Research, Institute of Medical Science and the ^|| Department of Medical Genome Sciences, Graduate School of Frontier Sciences, University of Tokyo, 4-6-1 Shirokanedai, Minato-ku, Tokyo 108-8639, the ^¶ Life Science Division, Nihon Millipore K. K., Minato-ku, Tokyo 108-0073, the ^** Department of Applied Biological Science, Tokyo University of Agriculture and Technology, 3-5-8 Saiwai-cho, Fuchu-shi, Tokyo 183-8509, and the Department of Chemistry, Graduate School of Science, Tokyo Metropolitan University, Hachioji-shi, Tokyo 192-0397, Japan

Although interactions between cell surface proteins and extracellular ligands are key to initiating embryonic stem cell differentiation to specific cell lineages, the plasma membrane protein components of these cells are largely unknown. We describe here a group of proteins expressed on the surface of the undifferentiated mouse embryonic stem cell line D3. These proteins were identified using a combination of cell surface labeling with biotin, subcellular fractionation of plasma membranes, and mass spectrometry-based protein identification technology. From 965 unique peptides carrying biotin labels, we assigned 324 proteins including 235 proteins that have putative signal sequences and/or transmembrane segments. Receptors, transporters, and cell adhesion molecules were the major classes of proteins identified. Besides known cell surface markers of embryonic stem cells, such as alkaline phosphatase, the analysis identified 59 clusters of differentiation-related molecules and more than 80 components of multiple cell signaling pathways that are characteristic of a number of different cell lineages. We identified receptors for leukemia-inhibitory factor, interleukin 6, and bone morphogenetic protein, which play critical roles in the maintenance of undifferentiated mouse embryonic stem cells. We also identified receptors for growth factors/cytokines, such as fibroblast growth factor, platelet-derived growth factor, ephrin, Hedgehog, and Wnt, which transduce signals for cell differentiation and embryonic development. Finally we identified a variety of integrins, cell adhesion molecules, and matrix metalloproteases. These results suggest that D3 cells express diverse cell surface proteins that function to maintain pluripotency, enabling cells to respond to various external signals that initiate differentiation into a variety of cell types.

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]

				S. Fujiyama-Nakamura, H. Yoshikawa, K. Homma, T. Hayano, T. Tsujimura-Takahashi, K. Izumikawa, H. Ishikawa, N. Miyazawa, M. Yanagida, Y. Miura, et al. Parvulin (Par14), a Peptidyl-Prolyl cis-trans Isomerase, Is a Novel rRNA Processing Factor That Evolved in the Metazoan Lineage Mol. Cell. Proteomics, July 1, 2009; 8(7): 1552 - 1565. [Abstract] [Full Text] [PDF]

				Y. Liu, B. K. Law, and H. Luesch Apratoxin A Reversibly Inhibits the Secretory Pathway by Preventing Cotranslational Translocation Mol. Pharmacol., July 1, 2009; 76(1): 91 - 104. [Abstract] [Full Text] [PDF]

				T. Vaisar Thematic Review Series: Proteomics. Proteomic analysis of lipid-protein complexes J. Lipid Res., May 1, 2009; 50(5): 781 - 786. [Abstract] [Full Text] [PDF]

				A. Sidibe, X. Yin, E. Tarelli, Q. Xiao, A. Zampetaki, Q. Xu, and M. Mayr Integrated Membrane Protein Analysis of Mature and Embryonic Stem Cell-derived Smooth Muscle Cells Using a Novel Combination of CyDye/Biotin Labeling Mol. Cell. Proteomics, October 1, 2007; 6(10): 1788 - 1797. [Abstract] [Full Text] [PDF]