Quantitative proteomic analysis of the adipocyte plasma membrane

Matthew J Prior, Mark Larance, Robert T Lawrence, Jamie Soul, Sean Humphrey, James Burchfield, Carol Kistler, Jonathon R Davey, Penelope J La-Borde, Michael Buckley, Hiroshi Kanazawa, Robert G Parton, Michael Guilhaus, David E James (Lead / Corresponding author)

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    26 Citations (Scopus)


    The adipocyte is a key regulator of mammalian metabolism. To advance our understanding of this important cell, we have used quantitative proteomics to define the protein composition of the adipocyte plasma membrane (PM) in the presence and absence of insulin. Using this approach, we have identified a high confidence list of 486 PM proteins, 52 of which potentially represent novel cell surface proteins, including a member of the adiponectin receptor family and an unusually high number of hydrolases with no known function. Several novel insulin-responsive proteins including the sodium/hydrogen exchanger, NHE6 and the collagens III and VI were also identified, and we provide evidence of PM-ER association suggestive of a unique functional association between these two organelles in the adipocyte. Together these studies provide a wealth of potential therapeutic targets for the manipulation of adipocyte function and a valuable resource for metabolic research and PM biology.
    Original languageEnglish
    Pages (from-to)4970-4982
    Number of pages13
    JournalJournal of Proteome Research
    Issue number11
    Publication statusPublished - 4 Nov 2011


    • Animals
    • Endoplasmic Reticulum
    • Caveolin 1
    • 3T3-L1 Cells
    • Mice
    • Tandem Mass Spectrometry
    • Membrane Proteins
    • Cell Fractionation
    • Adipocytes
    • Calnexin
    • Proteomics
    • Cell Membrane
    • Syntaxin 16
    • Sodium-Hydrogen Antiporter
    • Qa-SNARE Proteins


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