Pathobiochemical Changes in Diabetic Skeletal Muscle as Revealed by Mass-Spectrometry-Based Proteomics

Figure 2

Overview of changes in diabetic skeletal muscle as revealed by mass-spectrometry-based proteomics. Shown is a diagram of a skeletal muscle fibre outlining sarcolemmal proteins involved in insulin signaling and glucose uptake, as well as major cellular mechanisms affected in diabetic muscle tissues. Listed are established diabetes-related impairments of insulin receptor (IR) phosphorylation and abnormal signaling and transporter recruitment involving IRS1, p85, p110, Akt, PI-3-kinase, and glucose transporter isoform GLUT4. Proteomic profiling of muscle tissues from patients and established animal models of type 2 diabetes have revealed changes in components downstream from these plasmalemmal signaling cascades, including proteins involved in mitochondrial metabolism, glycolysis, contractile apparatus, detoxification mechanisms, cellular stress response, glucose metabolism, fatty acid utilization, nucleotide metabolism, and amino acid metabolism.