Characterization of the human skeletal muscle proteome by one-dimensional gel electrophoresis and HPLC-ESI-MS/MS

Kurt Højlund, Zhengping Yi, Hyonson Hwang, Benjamin Bowen, Natalie Lefort, Charles R. Flynn, Paul Langlais, Susan T. Weintraub, Lawrence J. Mandarino

    Research output: Contribution to journalArticle

    83 Citations (Scopus)

    Abstract

    Changes in protein abundance in skeletal muscle are central to a large number of metabolic and other disorders, including, and perhaps most commonly, insulin resistance. Proteomics analysis of human muscle is an important approach for gaining insight into the biochemical basis for normal and pathophysiological conditions. However, to date, the number of proteins identified by this approach has been limited, with 107 different proteins being the maximum reported so far. Using a combination of one-dimensional gel electrophoresis and high performance liquid chromatography electrospray ionization tandem mass spectrometry, we identified 954 different proteins in human vastus lateralis muscle obtained from three healthy, nonobese subjects. In addition to a large number of isoforms of contractile proteins, we detected all proteins involved in the major pathways of glucose and lipid metabolism in skeletal muscle. Mitochondrial proteins accounted for 22% of all proteins identified, including 55 subunits of the respiratory complexes I-V. Moreover, a number of enzymes involved in endocrine and metabolic signaling pathways as well as calcium homeostasis were identified. These results provide the most comprehensive characterization of the human skeletal muscle proteome to date. These data hold promise for future global assessment of quantitative changes in the muscle proteome of patients affected by disorders involving skeletal muscle.

    Original languageEnglish (US)
    Pages (from-to)257-267
    Number of pages11
    JournalMolecular and Cellular Proteomics
    Volume7
    Issue number2
    DOIs
    StatePublished - Feb 2008

    Fingerprint

    Proteome
    Electrophoresis
    Muscle
    Skeletal Muscle
    Gels
    High Pressure Liquid Chromatography
    Proteins
    Muscles
    Electron Transport Complex I
    Contractile Proteins
    Electrospray Ionization Mass Spectrometry
    Mitochondrial Proteins
    Quadriceps Muscle
    Electrospray ionization
    Tandem Mass Spectrometry
    Metabolic Networks and Pathways
    Lipid Metabolism
    Proteomics
    High performance liquid chromatography
    Insulin Resistance

    ASJC Scopus subject areas

    • Biochemistry

    Cite this

    Characterization of the human skeletal muscle proteome by one-dimensional gel electrophoresis and HPLC-ESI-MS/MS. / Højlund, Kurt; Yi, Zhengping; Hwang, Hyonson; Bowen, Benjamin; Lefort, Natalie; Flynn, Charles R.; Langlais, Paul; Weintraub, Susan T.; Mandarino, Lawrence J.

    In: Molecular and Cellular Proteomics, Vol. 7, No. 2, 02.2008, p. 257-267.

    Research output: Contribution to journalArticle

    Højlund, K, Yi, Z, Hwang, H, Bowen, B, Lefort, N, Flynn, CR, Langlais, P, Weintraub, ST & Mandarino, LJ 2008, 'Characterization of the human skeletal muscle proteome by one-dimensional gel electrophoresis and HPLC-ESI-MS/MS', Molecular and Cellular Proteomics, vol. 7, no. 2, pp. 257-267. https://doi.org/10.1074/mcp.M700304-MCP200
    Højlund, Kurt ; Yi, Zhengping ; Hwang, Hyonson ; Bowen, Benjamin ; Lefort, Natalie ; Flynn, Charles R. ; Langlais, Paul ; Weintraub, Susan T. ; Mandarino, Lawrence J. / Characterization of the human skeletal muscle proteome by one-dimensional gel electrophoresis and HPLC-ESI-MS/MS. In: Molecular and Cellular Proteomics. 2008 ; Vol. 7, No. 2. pp. 257-267.
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