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Haem can bind to and inhibit mammalian calcium-dependent Slo1 BK channels

Author

Listed:
  • Xiang Dong Tang

    (University of Pennsylvania)

  • Rong Xu

    (University of Pennsylvania)

  • Mark F. Reynolds

    (Saint Joseph's University)

  • Maria L. Garcia

    (Merck Research Laboratories)

  • Stefan H. Heinemann

    (Medical Faculty of the Friedrich Schiller University Jena)

  • Toshinori Hoshi

    (University of Pennsylvania)

Abstract

Haem is essential for living organisms, functioning as a crucial element in the redox-sensitive reaction centre in haemproteins1. During the biogenesis of these proteins, the haem cofactor is typically incorporated enzymatically into the haem pockets of the apo-haemprotein as the functionally indispensable prosthetic group2,3. A class of ion channel, the large-conductance calcium-dependent Slo1 BK channels, possesses a conserved haem-binding sequence motif. Here we present electrophysiological and structural evidence showing that haem directly regulates cloned human Slo1 channels and wild-type BK channels in rat brain. Both oxidized and reduced haem binds to the hSlo1 channel protein and profoundly inhibits transmembrane K+ currents by decreasing the frequency of channel opening. This direct regulation of the BK channel identifies a previously unknown role of haem as an acute signalling molecule.

Suggested Citation

  • Xiang Dong Tang & Rong Xu & Mark F. Reynolds & Maria L. Garcia & Stefan H. Heinemann & Toshinori Hoshi, 2003. "Haem can bind to and inhibit mammalian calcium-dependent Slo1 BK channels," Nature, Nature, vol. 425(6957), pages 531-535, October.
    • Handle: RePEc:nat:nature:v:425:y:2003:i:6957:d:10.1038_nature02003
    DOI: 10.1038/nature02003
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