Key result
Proteomic analysis of human skeletal muscle identifies 89 protein spots as gene expression products.
This proteomic analysis provides a baseline map of human skeletal muscle proteins to support future studies on physiological and pathological mechanisms.
Offers no immediate clinical implications; leaves open its role in guiding future research on muscle physiology and pathology.
Proteins from bioptates and autoptates of human skeletal muscle m. vastus lateralis were separated by O'Farrell two-dimensional gel electrophoresis (2DE). MALDI-TOF MS and MS/MS enabled identification of 89 protein spots as expression products of 55 genes. A modification of the O'Farrell's method including non-equilibrium electrophoresis in a pH gradient allowed detection--among major sarcomeric, mitochondrial, and cytosolic proteins--of several proteins, such as PDZ- and LIM domain-containing ones (pI > 8.70), fragments of known proteins, and a stable complex of heavy and light ferritin chains. The data underlie further studies of human skeletal muscle proteins in terms of molecular mechanisms of some physiological and pathological processes.
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Kovalyova et al. (2009) studied this question. Proteomic analysis (2DE and MALDI-TOF MS) was evaluated on Identification of protein spots. Proteomic analysis of human skeletal muscle using 2DE and MALDI-TOF MS identified 89 protein spots as expression products of 55 genes.
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