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    Modulation of BK(Ca) channel activity by fatty acids: structural requirements and mechanism of action

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    Authors
    Clarke, Alison L.
    Petrou, Steven
    Walsh, John V. Jr.
    Singer, Joshua J.
    UMass Chan Affiliations
    Department of Physiology
    Document Type
    Journal Article
    Publication Date
    2002-10-10
    Keywords
    Amines
    Animals
    Arachidonic Acid
    Cell Membrane
    Electrochemistry
    Fatty Acids
    Ion Channel Gating
    Large-Conductance Calcium-Activated Potassium Channels
    Muscle, Smooth, Vascular
    Myristic Acid
    Oleic Acid
    Phosphoprotein Phosphatase
    Potassium Channels, Calcium-Activated
    Protein Kinases
    Rabbits
    Sphingosine
    Structure-Activity Relationship
    Life Sciences
    Medicine and Health Sciences
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    Link to Full Text
    https://doi.org/10.1152/ajpcell.00035.2002
    Abstract
    To determine the mechanism of fatty acid modulation of rabbit pulmonary artery large-conductance Ca2+ -activated K+ (BK(Ca)) channel activity, we studied effects of fatty acids and other lipids on channel activity in excised patches with patch-clamp techniques. The structural features of the fatty acid required to increase BK(Ca) channel activity (or average number of open channels, NP(o)) were identified to be the negatively charged head group and a sufficiently long (C > 8) carbon chain. Positively charged lipids like sphingosine, which have a sufficiently long alkyl chain (C >or= 8), produced a decrease in NP(o). Neutral and short-chain lipids did not alter NP(o). Screening of membrane surface charge with high-ionic-strength bathing solutions (330 mM K+ or 130 mM K+, 300 mM Na+) did not alter the modulation of the BK(Ca) channel NP(o) by fatty acids and other charged lipids, indicating that channel modulation is unlikely to be due to an alteration of the membrane electric field or the attraction of local counterions to the channel. Fatty acids and other negatively charged lipids were able to modulate BK(Ca) channel activity in bathing solutions containing 0 mM Ca2+, 20 mM EGTA, suggesting that calcium is not required for this modulation. Together, these results indicate that modulation of BK(Ca) channels by fatty acids and other charged lipids most likely occurs by their direct interaction with the channel protein itself or with some other channel-associated component.
    Source

    Am J Physiol Cell Physiol. 2002 Nov;283(5):C1441-53. Link to article on publisher's site

    DOI
    10.1152/ajpcell.00035.2002
    Permanent Link to this Item
    http://hdl.handle.net/20.500.14038/38267
    PubMed ID
    12372805
    Related Resources

    Link to article in PubMed

    ae974a485f413a2113503eed53cd6c53
    10.1152/ajpcell.00035.2002
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