Abstract
In skeletal muscle fibers, the excitation–contraction–relaxation cycle is a highly evolved process that is mediated by the contractile proteins – myosin and actin – and the regulatory elements – troponin and tropomyosin. Contractile fibers exhibit enormous complexity and heterogeneity on the molecular level, which is reflected by the diversity of protein isoforms that constitute the actomyosin apparatus. The main components of the contractile apparatus exist in high abundance and are relatively soluble, making them ideal candidates for a systematic analysis by liquid chromatography or gel electrophoresis-based proteomics. This review discusses the proteomic profiling of contractile components in adapting, degenerating and aging skeletal muscle tissues. The proteomic identification of altered contractile proteins may be useful for the establishment of biomarker signatures that can be applied in the examination of the physiological adaptability, cellular plasticity and pathological susceptibility of the neuromuscular system.
Acknowledgements
The authors wish to thank their colleagues in the Department of Biology and the Mass Spectrometry Suite of NUI Maynooth for their continued support of our Muscle Proteomics Project.
Financial & competing interests disclosure
This study was supported by grants from the Irish Higher Education Authority (BioAT Programme of PRTLI5) and Muscular Dystrophy Ireland. The authors have no other relevant affiliations or financial involvement with any organization or entity with a financial interest in or financial conflict with the subject matter or materials discussed in the manuscript apart from those disclosed.
No writing assistance was utilized in the production of this manuscript.