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: M600345-MCP200v1 6/4/728    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 Fraterman, S. Articles by Rubinstein, N. A. Search for Related Content PubMed PubMed Citation Articles by Fraterman, S. Articles by Rubinstein, N. A. Social Bookmarking                      What's this?

Molecular & Cellular Proteomics 6:728-737, 2007.
© 2007 by The American Society for Biochemistry and Molecular Biology, Inc.

---

Research

Quantitative Proteomics Profiling of Sarcomere Associated Proteins in Limb and Extraocular Muscle Allotypes^*,S

Sven Fraterman^,,¶,||, Ulrike Zeiger^**,¶, Tejvir S. Khurana^**,¶, Matthias Wilm and Neal A. Rubinstein^,¶

From the Gene Expression Unit, European Molecular Biology Laboratory, 69117 Heidelberg, Germany and Department of Cell and Developmental Biology, ^** Department of Physiology, and ^¶ Pennsylvania Muscle Institute, School of Medicine, University of Pennsylvania, Philadelphia, Pennsylvania 19104

The sarcomere is the major structural and functional unit of striated muscle. Approximately 65 different proteins have been associated with the sarcomere, and their exact composition defines the speed, endurance, and biology of each individual muscle. Past analyses relied heavily on electrophoretic and immunohistochemical techniques, which only allow the analysis of a small fraction of proteins at a time. Here we introduce a quantitative label-free, shotgun proteomics approach to differentially quantitate sarcomeric proteins from microgram quantities of muscle tissue in a fast and reliable manner by liquid chromatography and mass spectrometry. The high sequence similarity of some sarcomeric proteins poses a problem for shotgun proteomics because of limitations in subsequent database search algorithms in the exclusive assignment of peptides to specific isoforms. Therefore multiple sequence alignments were generated to improve the identification of isoform specific peptides. This methodology was used to compare the sarcomeric proteome of the extraocular muscle allotype to limb muscle. Extraocular muscles are a unique group of highly specialized muscles with distinct biochemical, physiological, and pathological properties. We were able to quantitate 40 sarcomeric proteins; although the basic sarcomeric proteins in extraocular muscle are similar to those in limb muscle, key proteins stabilizing the connection of the Z-bands to thin filaments and the costamere are augmented in extraocular muscle and may represent an adaptation to the eccentric contractions known to normally occur during eye movements. Furthermore, a number of changes are seen that closely relate to the unique nature of extraocular muscle.

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

This article has been cited by other articles:

				C. Thoma, S. Fraterman, M. Gentzel, M. Wilm, and M. W. Hentze Translation initiation by the c-myc mRNA internal ribosome entry sequence and the poly(A) tail RNA, August 1, 2008; 14(8): 1579 - 1589. [Abstract] [Full Text] [PDF]