Comparative Proteomics for Studying Muscular Dystrophy: Intrinsic Biological and Analytical Issues Associated with the Systematic Utilization of Tissue Specimens
Ashling Holland and Kay Ohlendieck*
Muscle Biology Laboratory, Department of Biology, Maynooth University, National University of Ireland, Maynooth, Co. Kildare, Ireland
- *Corresponding Author:
- Kay Ohlendieck
Professor & Chair, Department of Biology
Maynooth University, National University of Ireland
Maynooth, Co. Kildare, Ireland
Tel: (353) (1) 708-3842
Fax :(353) (1) 708-3845
E-mail: [email protected]
Received Date: September 12, 2014; Accepted Date: October 10, 2014; Published Date: October 14, 2014
Citation: Holland A, Ohlendieck K (2014) Comparative Proteomics for Studying Muscular Dystrophy: Intrinsic Biological and Analytical Issues Associated with the Systematic Utilization of Tissue Specimens. J Proteomics Bioinform S10:002. doi: 10.4172/jpb.S10-002
Copyright: © 2014 Holland A, et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
Over the past decade, mass spectrometry-based proteomics has been instrumental for the detailed elucidation of pathobiochemical mechanisms involved in major neuromuscular diseases. Although the identification of musclederived proteins in biofluids is the main focus of diagnostic biomarker research, the large-scale proteomic analysis of pathological muscle tissue is of central importance for furthering our general understanding of the dysregulation that underlies complex muscle diseases. Here, we discuss intrinsic biological issues and bioanalytical difficulties that are generally associated with comparative muscle tissue proteomics. The systematic utilization of cellular mixtures or whole tissue specimens as starting material for studying neuromuscular pathology is seriously complicated by the cellular heterogeneity and physiological plasticity of contractile tissues. The comprehensive biochemical analysis of the skeletal muscle proteome is often hampered by the wide dynamic expression range of proteins, the greatly differing physicochemical properties of dissimilar muscle protein species and the potential cross-contamination of samples by highly abundant proteins. Thus, neither gel electrophoretic methodology nor liquid chromatography, is capable of appropriately separating all constituents of the skeletal muscle proteome. However, the application of advanced extraction strategies, the usage of subcellular fractionation protocols to reduce sample complexity and the affinity purification of distinct protein fractions prior to mass spectrometric analysis promises to overcome some of the inherent problems associated with muscle tissue proteomics.