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) All Versions of this Article: M400020-MCP200v1 3/11/1065    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 Glossary Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Tannu, N. S. Articles by Raghow, R. Search for Related Content PubMed PubMed Citation Articles by Tannu, N. S. Articles by Raghow, R. Social Bookmarking                      What's this?

Molecular & Cellular Proteomics 3:1065-1082, 2004.
© 2004 by The American Society for Biochemistry and Molecular Biology, Inc.

---

Research

Comparative Proteomes of the Proliferating C₂C₁₂ Myoblasts and Fully Differentiated Myotubes Reveal the Complexity of the Skeletal Muscle Differentiation Program^*,S

Nilesh S. Tannu, Vamshi K. Rao, Ritcha M. Chaudhary^**, Francesco Giorgianni^||, Abdelwahab E. Saeed^¶, Yong Gao^¶ and Rajendra Raghow^,,¶,**,

From the Departments of Biomedical Engineering, Pediatrics, and ^¶ Pharmacology, and ^|| Charles B. Stout Neuroscience Mass Spectrometry Laboratory, University of Tennessee Health Science Center and ^** Department of Veterans Affairs Medical Center, Memphis, TN 38104

When cultured in low serum-containing growth medium, the mouse C₂C₁₂ cells exit cell cycle and undergo a well-defined program of differentiation that culminates in the formation of myosin heavy chain-positive bona fide multinucleated muscle cells. To gain an understanding into this process, we compared total, membrane- and nuclear-enriched proteins, and phospho-proteins from the proliferating C₂C₁₂ cells and the fully differentiated myotubes by the combined methods of two-dimensional PAGE, quantitative PDQuest image analysis, and MS. Quantification of more than 2,000 proteins from C₂C₁₂ myoblasts and myotubes revealed that a vast majority of the abundant proteins appear to be relegated to the essential, housekeeping and structural functions, and their steady state levels remain relatively constant. In contrast, 75 proteins were highly regulated during the phenotypic conversion of rapidly dividing C₂C₁₂ myoblasts into fully differentiated, multi-nucleated, post-mitotic myotubes. We found that differential accumulation of 26 phospho-proteins also occurred during conversion of C₂C₁₂ myoblasts into myotubes. We identified the differentially expressed proteins by MALDI-TOF-MS and LC-ESI-quadrupole ion trap MS/MS. We demonstrate that more than 100 proteins, some shown to be associated with muscle differentiation for the first time, that regulate inter- and intracellular signaling, cell shape, proliferation, apoptosis, and gene expression impinge on the mechanism of skeletal muscle differentiation.

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

This article has been cited by other articles:

				Y. Oikawa, E. Matsuda, T. Nishii, Y. Ishida, and M. Kawaichi Down-regulation of CIBZ, a Novel Substrate of Caspase-3, Induces Apoptosis J. Biol. Chem., May 23, 2008; 283(21): 14242 - 14247. [Abstract] [Full Text] [PDF]

				W. Li, G. Wu, and Y. Wan The dual effects of Cdh1/APC in myogenesis FASEB J, November 1, 2007; 21(13): 3606 - 3617. [Abstract] [Full Text] [PDF]

				T. Kislinger, A. O. Gramolini, Y. Pan, K. Rahman, D. H. MacLennan, and A. Emili Proteome Dynamics during C2C12 Myoblast Differentiation Mol. Cell. Proteomics, July 1, 2005; 4(7): 887 - 901. [Abstract] [Full Text] [PDF]