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    Site of action of fatty acids and other charged lipids on BKCa channels from arterial smooth muscle cells

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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
    2002-11-01
    Keywords
    Amines
    Anions
    Arteries
    Cell Membrane
    Cells, Cultured
    Dose-Response Relationship, Drug
    Fatty Acids
    *Lipid Metabolism
    Lipids
    Membrane Potentials
    Muscle, Smooth, Vascular
    Myocytes, Smooth Muscle
    Palmitoyl Coenzyme A
    Peptide Fragments
    Potassium Channels, Calcium-Activated
    Quaternary Ammonium Compounds
    Trimethyl Ammonium Compounds
    Life Sciences
    Medicine and Health Sciences
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    Link to Full Text
    http://dx.doi.org/10.1152/ajpcell.00364.2002
    Abstract
    Fatty acids and other negatively charged single-chain lipids increase large-conductance Ca(2+)-activated K(+) (BK(Ca)) channel activity, whereas sphingosine and other positively charged single-chain lipids suppress activity. Because these molecules are effective on both inside-out and outside-out patches and because they can flip across the bilayer, the location of their site of action is unclear. To identify the site of action of charged lipids on this channel, we used two compounds that are unlikely to flip across the lipid bilayer. Palmitoyl coenzyme A (PCoA) was used to identify the site of action of negatively charged lipids, and a positively charged myristoylated pentapeptide (myr-KPRPK) was used to investigate the site of action of positively charged lipids. The effect of these compounds on channel activity was studied in excised patches using patch-clamp techniques. In "normal" ionic strength solutions and in experiments where high-ionic strength solutions were used to shield membrane surface charge, PCoA increased channel activity only when applied to outside-out patches, suggesting that the site of action of negatively charged lipids is located on the outer surface of the membrane. A decrease in activity, similar to that of other positively charged lipids, was observed only when myr-KPRPK was applied to outside-out patches, suggesting that positively charged lipids suppress activity by also acting on the outer membrane surface. Some channel blockade effects of myr-KPRPK and KPRPK are also described. The sidedness of action suggests that modulation of channel activity by single-chain lipids can occur by their interaction with the channel protein.
    Source
    Am J Physiol Cell Physiol. 2003 Mar;284(3):C607-19. Epub 2002 Oct 30. Link to article on publisher's site
    DOI
    10.1152/ajpcell.00364.2002
    Permanent Link to this Item
    http://hdl.handle.net/20.500.14038/38245
    PubMed ID
    12409285
    Related Resources
    Link to article in PubMed
    ae974a485f413a2113503eed53cd6c53
    10.1152/ajpcell.00364.2002
    Scopus Count
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