MCP Sign the guestbook
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

Originally published In Press as doi:10.1074/mcp.M500123-MCP200 on June 15, 2005.
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Supplemental Data
Right arrow All Versions of this Article:
M500123-MCP200v1
4/9/1297    most recent
Right arrow Submit a response
Right arrow Alert me when this article is cited
Right arrow Alert me when eLetters are posted
Right arrow Alert me if a correction is posted
Right arrow Citation Map
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow Glossary
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Romijn, E. P.
Right arrow Articles by Heck, A. J. R.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Romijn, E. P.
Right arrow Articles by Heck, A. J. R.
Social Bookmarking
Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?

Molecular & Cellular Proteomics 4:1297-1310, 2005.
© 2005 by The American Society for Biochemistry and Molecular Biology, Inc.

Research

Expression Clustering Reveals Detailed Co-expression Patterns of Functionally Related Proteins during B Cell Differentiation

A Proteomic Study Using a Combination of One-Dimensional Gel Electrophoresis, LC-MS/MS, and Stable Isotope Labeling by Amino Acids in Cell Culture (SILAC)*,S

Edwin P. Romijn{ddagger},§,¶, Chantal Christis||,§, Marnix Wieffer**, Joost W. Gouw{ddagger}, Asier Fullaondo{ddagger},{ddagger}{ddagger}, Peter van der Sluijs**, Ineke Braakman|| and Albert J. R. Heck{ddagger},§§

From the{ddagger} Department of Biomolecular Mass Spectrometry, Bijvoet Center for Biomolecular Research and Utrecht Institute for Pharmaceutical Sciences, Utrecht University, 3584 CA Utrecht, The Netherlands, || Department of Cellular Protein Chemistry, Bijvoet Center for Biomolecular Research, Utrecht University, 3584 CH Utrecht, The Netherlands, ** Department of Cell Biology, University Medical Center Utrecht, 3584 CX Utrecht, The Netherlands, and {ddagger}{ddagger} Genetika, Antropologia Fisikoa eta Animalien Fisiologia Saila, Leioako Campusa, Leioa, 48940 Bizkaia, Spain

B cells play an essential role in the immune response. Upon activation they may differentiate into plasma cells that secrete specific antibodies against potentially pathogenic non-self antigens. To identify the cellular proteins that are important for efficient production of these antibodies we set out to study the B cell differentiation process at the proteome level. We performed an in-depth proteomic study to quantify dynamic relative protein expression patterns of several hundreds of proteins at five consecutive time points after lipopolysaccharide-induced activation of B lymphocytes. The proteome analysis was performed using a combination of stable isotope labeling using [13C6]leucine added to the murine B cell cultures, one-dimensional gel electrophoresis, and LC-MS/MS. In this study we identified 1,001 B cell proteins. We were able to quantify the expression levels of a quarter of all identified proteins (i.e. 234) at each of the five different time points. Nearly all proteins revealed changes in expression patterns. The quantitative dataset was further analyzed using an unbiased clustering method. Based on their expression profiles, we grouped the entire set of 234 quantified proteins into a limited number of 12 distinct clusters. Functionally related proteins showed a strong correlation in their temporal expression profiles. The quality of the quantitative data allowed us to even identify subclusters within functionally related classes of proteins such as in the endoplasmic reticulum proteins that are involved in antibody production.

§§ To whom correspondence should be addressed. Tel.: 0031302536797; Fax: 0031302518219; E-mail: a.j.r.heck{at}chem.uu.nl


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


This article has been cited by other articles:


Home page
 Mol. Cell. ProteomicsHome page
F. Mousson, A. Kolkman, W. W. M. P. Pijnappel, H. Th. M. Timmers, and A. J. R. Heck
Quantitative Proteomics Reveals Regulation of Dynamic Components within TATA-binding Protein (TBP) Transcription Complexes
Mol. Cell. Proteomics, May 1, 2008; 7(5): 845 - 852.
[Abstract] [Full Text] [PDF]

Home page
 Mol. Cell. ProteomicsHome page
A. Pandey, S. Chakraborty, A. Datta, and N. Chakraborty
Proteomics Approach to Identify Dehydration Responsive Nuclear Proteins from Chickpea (Cicer arietinum L.)
Mol. Cell. Proteomics, January 1, 2008; 7(1): 88 - 107.
[Abstract] [Full Text] [PDF]

Home page
 Mol. Cell. ProteomicsHome page
D. Bhushan, A. Pandey, M. K. Choudhary, A. Datta, S. Chakraborty, and N. Chakraborty
Comparative Proteomics Analysis of Differentially Expressed Proteins in Chickpea Extracellular Matrix during Dehydration Stress
Mol. Cell. Proteomics, November 1, 2007; 6(11): 1868 - 1884.
[Abstract] [Full Text] [PDF]

Home page
 BloodHome page
R. D. Unwin, D. L. Smith, D. Blinco, C. L. Wilson, C. J. Miller, C. A. Evans, E. Jaworska, S. A. Baldwin, K. Barnes, A. Pierce, et al.
Quantitative proteomics reveals posttranslational control as a regulatory factor in primary hematopoietic stem cells
Blood, June 15, 2006; 107(12): 4687 - 4694.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 All ASBMB Journals   Journal of Biological Chemistry 
 Journal of Lipid Research   ASBMB Today 
Copyright © 2005 by the American Society for Biochemistry and Molecular Biology.