Mass spectrometry‐based proteomics approaches to interrogate skeletal muscle adaptations to exercise

Abstract

Acute exercise and chronic exercise training elicit beneficial whole‐body changes in physiology that ultimately depend on profound alterations to the dynamics of tissue‐specific proteins. Since the work accomplished during exercise owes predominantly to skeletal muscle, it has received the majority of interest from exercise scientists that attempt to unravel adaptive mechanisms accounting for salutary metabolic effects and performance improvements that arise from training. Contemporary scientists are also beginning to use mass spectrometry‐based proteomics, which is emerging as a powerful approach to interrogate the muscle protein signature in a more comprehensive manner. Collectively, these technologies facilitate the analysis of skeletal muscle protein dynamics from several viewpoints, including changes to intracellular proteins (expression proteomics), secreted proteins (secretomics), post‐translational modifications as well as fiber‐, cell‐, and organelle‐specific changes. This review aims to highlight recent literature that has leveraged new workflows and advances in mass spectrometry‐based proteomics to further our understanding of training‐related changes in skeletal muscle. We call attention to untapped areas in skeletal muscle proteomics research relating to exercise training and metabolism, as well as basic points of contention when applying mass spectrometry‐based analyses, particularly in the study of human biology. We further encourage researchers to couple the hypothesis‐generating and descriptive nature of omics data with functional analyses that propel our understanding of the complex adaptive responses in skeletal muscle that occur with acute and chronic exercise.

Deletion of miPEP in adipocytes protects against obesity and insulin resistance by boosting muscle metabolism

“…Thus, similar to adipo-miPEP-KO mice, Ucp1 -deficient mice adapt to cold by activating non-shivering thermogenic mechanisms [ 65 ]. Second, increased shivering leads to alterations in muscle physiology resembling those seen with exercise training [ 66 ]. However, this was not evident from our proteomics analysis.…”

Mass Spectrometry-Based Proteomic Technology and Its Application to Study Skeletal Muscle Cell Biology

“…Figure 5 gives an overview of the extent of proteome-wide adaptations due to changed functional demands or pathophysiological alterations in the skeletal musculature. The skeletal musculature is a highly adaptable organ system [42] that can be affected by changes in lifestyle, physical activity levels, side effects seen in traumatic injury, extensive pharmacotherapy and the natural aging process [38,46]. Acute or chronic myofiber degradation, inflammation and/or myofibrosis are involved in many primary muscleassociated diseases, such as muscular dystrophies [44,256], but also occur in association with various common pathologies, such as cancer, diabetes, obesity, heart disease or sepsis.…”

“…These articles give a comprehensive overview of the many applications of MS-based analyses to improve our molecular and cellular understanding of skeletal muscle protein diversity, modifications and dynamics. Previous reviews have extensively covered the proteomic analysis of human skeletal muscle [20,37], the impact of exercise [38][39][40], disuse-related muscular atrophy [41], skeletal muscle plasticity [42,43], neuromuscular diseases [44,45] and frailty-associated muscle aging [46,47]. Building on these articles, we provide here a general synopsis of skeletal muscle proteomics and its scientific importance for the field of basic and applied myology.…”

Nfe2l1-mediated proteasome function controls muscle energy metabolism in obesity

“…1D). The challenge of skeletal muscle proteomics is the high amount of structural proteins, which limit the identification of proteins with lower abundance 20,21 . Nevertheless, we quantified 3739 proteins in the proteome and 1685 ubiquitylated peptides in the ubiquitome.…”