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    Structural requirements for charged lipid molecules to directly increase or suppress K+ channel activity in smooth muscle cells. Effects of fatty acids, lysophosphatidate, acyl coenzyme A and sphingosine

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    Authors
    Petrou, Steven
    Ordway, Richard W.
    Hamilton, James A.
    Walsh, John V.
    Singer, Joshua J.
    UMass Chan Affiliations
    Department of Physiology
    Graduate School of Biomedical Sciences
    Document Type
    Journal Article
    Publication Date
    1994-03-01
    Keywords
    Acyl Coenzyme A; Amines; Animals; Bufo marinus; Cell Separation; Electrochemistry; Electrophysiology; Fatty Acids; Lipid Bilayers; Lipids; Lysophospholipids; Muscle, Smooth; Potassium Channels; Sphingosine
    Life Sciences
    Medicine and Health Sciences
    
    Metadata
    Show full item record
    Link to Full Text
    https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2216847/
    Abstract
    We determined the structural features necessary for fatty acids to exert their action on K+ channels of gastric smooth muscle cells. Examination of the effects of a variety of synthetic and naturally occurring lipid compounds on K+ channel activity in cell-attached and excised membrane patches revealed that negatively charged analogs of medium to long chain fatty acids (but not short chain analogs) as well as certain other negatively charged lipids activate the channels. In contrast, positively charged, medium to long chain analogs suppress activity, and neutral analogs are without effect. The key requirements for effective compounds seem to be a sufficiently hydrophobic domain and the presence of a charged group. Furthermore, those negatively charged compounds unable to "flip" across the bilayer are effective only when applied at the cytosolic surface of the membrane, suggesting that the site of fatty acid action is also located there. Finally, because some of the effective compounds, for example, the fatty acids themselves, lysophosphatidate, acyl Coenzyme A, and sphingosine, are naturally occurring substances and can be liberated by agonist-activated or metabolic enzymes, they may act as second messengers targeting ion channels.
    Source

    J Gen Physiol. 1994 Mar;103(3):471-86.

    DOI
    10.1085/jgp.103.3.471
    Permanent Link to this Item
    http://hdl.handle.net/20.500.14038/34335
    PubMed ID
    8195783
    Related Resources

    Link to article in PubMed

    ae974a485f413a2113503eed53cd6c53
    10.1085/jgp.103.3.471
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