Table 1 List of select biochemical studies that have focused on the proteomic profiling of developing, transforming, pathological and aging skeletal muscle tissues

Skeletal muscle protein complement

Profiling of the skeletal muscle-associated proteome from various species. Shotgun proteomics has catalogued more than 2,000 human skeletal muscle proteins.

[47–50]

Muscle development

Proteomic analysis of myogenesis has identified a large variety of proteins, including metabolic enzymes (enolase, aldehyde dehydrogenase), contractile and structural elements (myosins, actins, tubulin, desmin), stress proteins (peroxiredoxin, superoxide dismutase, heat shock proteins) and components involved in protein synthesis (ribosomal enzymes).

[51–54, 136, 137]

Muscle transitions

Proteomic studies have established distinct changes in marker characteristic of fast-to-slow muscle transformations: fatty acid-binding protein, albumin, myosin heavy chains, myosin light chains, tropomyosins, troponins, creatine kinase and myoglobin.

[62, 63]

Effect of exercise

Proteomic profiling of physical training showed alterations in enolase, albumin, succinate dehydrogenase, myoglobin, aconitase and transferrin.

[60, 61]

Muscle growth

Proteomic analysis of hypertrophy revealed considerable changes in the abundance of contractile proteins (troponins, myosins), metabolic proteins (fatty acid-binding protein, phosphoglucomutase) and various molecular chaperones.

[78–84]

Disuse atrophy

Proteomic profiling of muscle unloading showed drastic changes in structural and contractile proteins (myosins, actins, troponins), stress proteins (various heat shock proteins) and marker enzymes of slow-to-fast transitions (enolase, triosephosphate isomerase, lactate dehydrogenase, isocitrate dehydrogenase).

[57–59, 135]

Dystrophinopathy

Proteomic screening of the x-linked muscular dystrophy (mdx) animal model of Duchenne muscular dystrophy revealed that the deficiency in dystrophin is associated with altered levels of metabolic enzymes (adenylate kinase, carbonic anhydrase, isocitrate dehydrogenase), Ca²⁺-regulatory proteins (regucalcin, calsequestrin) and molecular chaperones (cardiovascular heat shock protein cvHsp).

[64–66]

Muscle aging

Proteomic profiling of aging muscle tissues has shown changes in metabolic markers that are characteristic of a fast-to-slow transition process (various glycolytic enzymes, such as pyruvate kinase and numerous mitochondrial enzymes), as well as changes in adenylate kinase and various molecular chaperones.

[55, 56, 87, 88, 90, 92, 116, 118]