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Proteomic analysis of detergent-resistant membrane rafts

  1. Author:
    Blonder, J.
    Hale, M. L.
    Lucas, D. A.
    Schaefer, C. F.
    Yu, L. R.
    Conrads, T. R.
    Issaq, H. J.
    Stiles, B. G.
    Veenstra, T. D.

  2. Author Address

    NCI, SAIC Frederick, Lab Proteom & Analyt Technol, Frederick, MD 21702 USA. USA, Med Res Inst Infect Dis, Dept Immunol & Mol Biol, Toxinol Div, Frederick, MD USA. NCI, Ctr Bioinformat, Bethesda, MD 20892 USA. Veenstra, TD, NCI, SAIC Frederick, Lab Proteom & Analyt Technol, Frederick, MD 21702 USA
    1. Year: 2004
  2. Journal: Electrophoresis
    1. 25
    2. 9
    3. Pages: 1307-1318
  4. Type of Article: Article
  1. Abstract:

    A combined, detergent- and organic solvent-based proteomic method for the analysis of detergent-resistant membrane rafts (DRMR) is described. These specialized domains of the plasma membrane contain a distinctive and dynamic protein and/or lipid complement, which can be isolated from most mammalian cells. Lipid rafts are predominantly involved in signal transduction and adapted to mediate and produce different cellular responses. To facilitate a better understanding of their biology and role, DRMR were isolated from Vero cells as a Triton X-100 insoluble fraction. After detergent removal, sonication in 60% buffered methanol was used to extract, solubilize and tryptically digest the resulting protein complement. The peptide digestate was analyzed by microcapillary reversed-phase liquid chromatography-tandem mass spectrometry. Gas-phase fractionation in the mass-to-charge range was employed to broaden the selection of precursor ions and increase the number of identifications in an effort to detect less abundant proteins. A total of 380 proteins were identified including all known lipid raft markers. A total of 91 (24%) proteins were classified as integral alpha-helical membrane proteins, of which 51 (56%) were predicted to have multiple transmembrane domains

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