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Anionic phospholipids activate ATP-sensitive potassium channels

Z Fan1, J C Makielski

  • 1Department of Medicine, University of Wisconsin, Madison, Wisconsin 53792, USA. zfan@facstaff.wisc.edu

The Journal of Biological Chemistry
|February 28, 1997
PubMed
Summary
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Anionic phospholipids activate ATP-sensitive potassium channels (KATP) in various cells, including pancreatic beta-cells. This activation depends on the negative charge of the phospholipids, suggesting a novel regulatory mechanism for KATP channels.

Area of Science:

  • Biochemistry
  • Cell Biology
  • Physiology

Background:

  • ATP-sensitive potassium channels (KATP) are crucial for insulin release from pancreatic beta-cells.
  • KATP channels also play significant roles in cardiac and skeletal muscle cells.

Purpose of the Study:

  • To investigate the role of anionic phospholipids in the activation of KATP channels.
  • To elucidate the mechanism by which phospholipids modulate KATP channel activity.

Main Methods:

  • Activation assays of KATP channels in pancreatic beta-cells, cardiac myocytes, skeletal muscle cells, and a cloned KATP (SUR/Kir6.2) expressed in mammalian cells.
  • Experiments involving polyvalent cations to screen phospholipid charges and phospholipase treatments to alter lipid structure.
  • Site-directed mutagenesis of positively charged amino acid residues in the Kir6.2 subunit.

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Main Results:

  • Anionic phospholipids activated KATP channels in all cell types and the cloned channel.
  • Activation effectiveness correlated with the number of negative charges on the phospholipid head group.
  • Polyvalent cations and phospholipase treatment reduced or abolished phospholipid-induced activation, indicating the importance of intact, negatively charged phospholipids.
  • Mutations in the C-terminus of Kir6.2 affected channel activity and phospholipid activation.

Conclusions:

  • Intact anionic phospholipids, rather than their cleavage products, are critical for KATP channel activation.
  • The C-terminal region of Kir6.2 is involved in phospholipid-mediated activation.
  • Metabolism of anionic phospholipids may represent a novel regulatory mechanism for KATP and other inward rectifier ion channels.