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    Cholesterol through the looking glass: Ability of its enantiomer also to elicit homeostatic responses

    Access Status
    Open access via publisher
    Authors
    Kristiana, Ina
    Luu, W.
    Stevenson, J.
    Cartland, S.
    Jessup, W.
    Belani, J.
    Rychnovsky, S.
    Brown, A.
    Date
    2012
    Collection
    • Curtin Research Publications
    Type
    Journal Article
    Metadata
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    Abstract

    How cholesterol is sensed to maintain homeostasis has been explained by direct binding to a specific protein, Scap, or through altering the physical properties of the membrane. The enantiomer of cholesterol (ent-cholesterol) is a valuable tool in distinguishing between these two models because it shares non-specific membrane effects with native cholesterol (nat-cholesterol), but not specific binding interactions. This is the first study to compare ent- and nat-cholesterol directly on major molecular parameters of cholesterol homeostasis. We found that ent-cholesterol suppressed activation of the master transcriptional regulator of cholesterol metabolism, SREBP-2, almost as effectively as nat-cholesterol. Importantly, ent-cholesterol induced a conformational change in the cholesterol-sensing protein Scap in isolated membranes in vitro, even when steps were taken to eliminate potential confounding effects from endogenous cholesterol. Ent-cholesterol also accelerated proteasomal degradation of the key cholesterol biosynthetic enzyme, squalene monooxygenase. Together, these findings provide compelling evidence that cholesterol maintains its own homeostasis not only via direct protein interactions, but also by altering membrane properties. © 2012 by The American Society for Biochemistry and Molecular Biology, Inc.

    Citation
    Kristiana, I. and Luu, W. and Stevenson, J. and Cartland, S. and Jessup, W. and Belani, J. and Rychnovsky, S. et al. 2012. Cholesterol through the looking glass: Ability of its enantiomer also to elicit homeostatic responses. Journal of Biological Chemistry. 287 (40): pp. 33897-33904.
    Source Title
    Journal of Biological Chemistry
    URI
    http://hdl.handle.net/20.500.11937/34257
    DOI
    10.1074/jbc.M112.360537
    Department
    Curtin Water Quality Research Centre

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