Proteomics of skeletal muscle glycolysis

Glycolysis represents one of the best-understood and most ancient metabolic pathways. In skeletal muscle fibres, energy for contraction is supplied by adenosine triphosphate via anaerobic glycolysis, the phosphocreatine shuttle and oxidative phosphorylation. In this respect, the anaerobic glycolytic pathway supports short duration performances of contractile tissues of high intensity. The catalytic elements associated with glycolysis are altered during development, muscle differentiation, physiological adaptations and many pathological mechanisms, such as muscular dystrophy, diabetes mellitus and age-related muscle weakness. Although gel electrophoresis-based proteomics is afflicted with various biological and technical problems, it is an ideal analytical tool for studying the abundant and mostly soluble enzymes that constitute the glycolytic system. This review critically examines the proteomic findings of recent large-scale studies of glycolytic enzymes and associated components in normal, transforming and degenerating muscle tissues. In the long term, proteins belonging to the glycolytic pathway may be useful as biomarkers of muscle adaptations and pathophysiological mechanisms and can be employed to improve diagnostics and in the identification of novel therapeutic targets in neuromuscular disorders.

Research Highlights
► Glycolytic enzymes are highly abundant cytosolic muscle proteins.
► Mass spectrometry-based proteomics routinely identifies glycolytic enzymes.
► Glycolytic enzymes change drastically during myogenesis and muscle growth.
► Proteomics has shown alterations of glycolytic enzymes in most muscle pathologies.
► Glycolytic enzymes change dramatically during muscle transformation and aging.