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)

    Research output: Contribution to journalArticle

    23 Citations (Scopus)

    Abstract

    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
    Volume10
    Issue number11
    DOIs
    Publication statusPublished - 4 Nov 2011

    Fingerprint

    Cell membranes
    Adipocytes
    Proteomics
    Cell Membrane
    Membrane Proteins
    Adiponectin Receptors
    Association reactions
    Insulin
    Sodium-Hydrogen Antiporter
    Hydrolases
    Metabolism
    Organelles
    Blood Proteins
    Proteins
    Collagen
    Chemical analysis
    Research
    Therapeutics

    Keywords

    • 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

    Cite this

    Prior, M. J., Larance, M., Lawrence, R. T., Soul, J., Humphrey, S., Burchfield, J., ... James, D. E. (2011). Quantitative proteomic analysis of the adipocyte plasma membrane. Journal of Proteome Research, 10(11), 4970-4982. https://doi.org/10.1021/pr200446r
    Prior, Matthew J ; Larance, Mark ; Lawrence, Robert T ; Soul, Jamie ; Humphrey, Sean ; Burchfield, James ; Kistler, Carol ; Davey, Jonathon R ; La-Borde, Penelope J ; Buckley, Michael ; Kanazawa, Hiroshi ; Parton, Robert G ; Guilhaus, Michael ; James, David E. / Quantitative proteomic analysis of the adipocyte plasma membrane. In: Journal of Proteome Research. 2011 ; Vol. 10, No. 11. pp. 4970-4982.
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    abstract = "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.",
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    Prior, MJ, Larance, M, Lawrence, RT, Soul, J, Humphrey, S, Burchfield, J, Kistler, C, Davey, JR, La-Borde, PJ, Buckley, M, Kanazawa, H, Parton, RG, Guilhaus, M & James, DE 2011, 'Quantitative proteomic analysis of the adipocyte plasma membrane', Journal of Proteome Research, vol. 10, no. 11, pp. 4970-4982. https://doi.org/10.1021/pr200446r

    Quantitative proteomic analysis of the adipocyte plasma membrane. / Prior, Matthew J; Larance, Mark; Lawrence, Robert T; Soul, Jamie; Humphrey, Sean; Burchfield, James; Kistler, Carol; Davey, Jonathon R; La-Borde, Penelope J; Buckley, Michael; Kanazawa, Hiroshi; Parton, Robert G; Guilhaus, Michael; James, David E (Lead / Corresponding author).

    In: Journal of Proteome Research, Vol. 10, No. 11, 04.11.2011, p. 4970-4982.

    Research output: Contribution to journalArticle

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    AU - La-Borde, Penelope J

    AU - Buckley, Michael

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    AU - Guilhaus, Michael

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    AB - 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.

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    KW - Proteomics

    KW - Cell Membrane

    KW - Syntaxin 16

    KW - Sodium-Hydrogen Antiporter

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    Prior MJ, Larance M, Lawrence RT, Soul J, Humphrey S, Burchfield J et al. Quantitative proteomic analysis of the adipocyte plasma membrane. Journal of Proteome Research. 2011 Nov 4;10(11):4970-4982. https://doi.org/10.1021/pr200446r