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Bioinformatics & Proteomics Open Access Journal Research Article 9 min read

A Short History of Skeletal Muscle Proteomics

Zulezwan ABM* and Burniston JG*
* Corresponding author
ISSN: 2642-6129  10.23880/bpoj-16000110  Received: September 21, 2017  Published: November 01, 2017
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Keywords
&lt p&gt Skeletal Muscle Proteomics 2DGE MALDI-TOF LC-ESI-MS/MS&lt /p&gt
Abstract

<p>Proteomics is the study of proteins using high-throughput techniques and relies on a combination of genomics, mass spectrometry and protein biochemistry. The human genome contains of approximately 20,000 genes that are transcribed into mRNA and then can be translated in to proteins Researchers can test hypotheses regarding individual mRNA or proteins using techniques such as Northern blots (for mRNA expression) or Western blots (for protein abundance). This ‘reductionist’ approach, where biology is reduced to individual questions, has been the mainstay of biological research. However, data arising from hypothesis-led studies clearly indicates that biology is not organised or controlled by isolated events Rather, biological systems are organised as complex networks and multiple interactions occur to bring about physiological changes. Therefore, more comprehensive (eg ‘-omic’) analysis techniques are required in order to advance our understanding of biological systems. The proteome is cell-specific and dynamic, responding on a minute-by-minute basis to changes in cell environment. Consequently, the proteome reflects the particular stage of development and current environmental condition the cell finds itself experiencing with regard exercise proteomics, report proteomic studies have mostly focused on striated muscle responses to endurance training, which are associated with health benefits underpinned by improvements in aerobic capacity. Over the past decade, researchers have studied the ability of proteomics analysis on skeletal muscle and the development of techniques. In this review we will point out some of the studies related that contributed to skeletal muscle proteomics</p>

Introduction

In theory, proteomics techniques should be able to characterise and measure the relative abundance of each myofibrillar protein species (ie encompassing isoforms, splice-variants and post-translational states) simultaneously [1]. This more comprehensive analysis circumvents the need to reduce the description of muscle to its relative proportion of 3 fibre types Burniston and Hoffman (2011) [2].

Bioinformatics & Proteomics Open Access Journal

Proteomic Techniques

The use of 2DGE offers robust comparative analysis of protein species, which represent different post- translational states of a protein [33]. However, 2DGE requires a significant level of skill is laborious and has a number of technical limitations, including difficulties in resolving proteins at the extremes of the mass and pH scales, and a limited dynamic range. Therefore, there is currently a drive to move away from 2DGE and develop simpler (SDS-PAGE) or more automated HPLC workflows. In muscle proteomics, the time efficiency of orthogonal SDS-PAGE and HPLC separations has been investigated [34]. The combination of SDS-PAGE with HPLC coupled directly to electrospray ionisation (ESI) tandem mass spectrometry (MS/MS), known as GeLC-MS/MS is of particular utility in skeletal muscle protein identification [35]. Several studies have applied the GeLC-MS/MS technique in proteomic research [36] used GeLC-MS/MS and reported combination of proteomic and transcriptomic analyses. In 2008, Hojlund and colleagues catalogued almost 1,000 proteins in the human skeletal muscle proteome using GeLC-MS/MS and Norheim, et al. [37] used this method for identification of proteins secreted by skeletal muscle cells in vitro. Burniston & Hoffman, (2011)[2] pioneered the application of proteomic techniques to investigate cardiac and skeletal muscle responses to endurance exercise. Further to standard proteomic techniques using 2DGE [20], they have developed specific methods for analysing muscle proteins [2, 8, 38] using sub-fractionation and solution-based protein separations (ie 1D HPLC). The current researches further develops this workflow by specifically investigating the myofibrillar sub-proteome using liquid chromatography separation of proteins with real-time tandem mass spectrometry and create a more robust analysis platform for measuring differences in the abundance of dozens of important myofibrillar proteins based on quantitative label-free mass spectrometry techniques.

Conclusions

More than a decade of research exploring the proteomic analysis of skeletal muscle has provided very promising results; only the future will determine more advance proteomic techniques will successfully use by all researchers.

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@article{zulezwan2017,
  title   = {A Short History of Skeletal Muscle Proteomics},
  author  = {Zulezwan ABM* and Burniston JG},
  journal = {Bioinformatics & Proteomics Open Access Journal},
  year    = {2017},
  volume  = {1},
  number  = {2},
  doi     = {10.23880/bpoj-16000110}
}
Zulezwan ABM* and Burniston JG (2017). A Short History of Skeletal Muscle Proteomics. Bioinformatics & Proteomics Open Access Journal, 1(2). https://doi.org/10.23880/bpoj-16000110
TY  - JOUR
TI  - A Short History of Skeletal Muscle Proteomics
AU  - Zulezwan ABM* and Burniston JG
JO  - Bioinformatics & Proteomics Open Access Journal
PY  - 2017
VL  - 1
IS  - 2
DO  - 10.23880/bpoj-16000110
ER  -