Functional reconstitution of the purified sodium channel protein from rat sarcolemma.

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  • Author(s): Weigele JB; Barchi RL
  • Source:
    Proceedings of the National Academy of Sciences of the United States of America [Proc Natl Acad Sci U S A] 1982 Jun; Vol. 79 (11), pp. 3651-5.
  • Publication Type:
    Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S.
  • Language:
    English
  • Additional Information
    • Source:
      Publisher: National Academy of Sciences Country of Publication: United States NLM ID: 7505876 Publication Model: Print Cited Medium: Print ISSN: 0027-8424 (Print) Linking ISSN: 00278424 NLM ISO Abbreviation: Proc Natl Acad Sci U S A Subsets: MEDLINE
    • Publication Information:
      Original Publication: Washington, DC : National Academy of Sciences
    • Subject Terms:
      Ion Channels/*physiology ; Sarcolemma/*analysis ; Sodium/*physiology; Animals ; Biological Transport ; Freeze Fracturing ; Hot Temperature ; Ion Channels/drug effects ; Liposomes ; Muscle Proteins/isolation & purification ; Rats ; Saxitoxin/pharmacology
    • Abstract:
      The purified saxitoxin (STX) binding component of the rat sarcolemmal sodium channel (SBC) has been reconstituted into phospholipid vesicles. The reconstituted SBC displays the pharmacological properties and the ability to control sodium fluxes expected of a functional sodium channel. Batrachotoxin (BTX) increases 22Na+ influx into reconstituted SBC vesicles by greater than 100% over control at early time points. The BTX-stimulated 22Na+ influx is specifically and quantitatively blocked by STX. Veratridine and aconitine also stimulate Na+-flux--although less effectively than BTX--in the order: BTX greater than veratridine greater than aconitine. The logarithmic dose--response curves for BTX and veratridine are sigmoidal with a K0.5 of 1.5 microM and 35 microM, respectively. Vesicles containing the reconstituted SBC demonstrate 3H-labeled STX binding to a single class of high affinity sites witha Kd of 5--7 nM at 0 degrees C; the thermal stability of the STX receptor is markedly enhanced by reconstitution. Our results confirm that the purified STX binding component from rat sarcolemma constitutes the sodium channel itself and contains at least those components sufficient for channel activation, transmembrane ion movement, and inhibition by STX.
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    • Grant Information:
      NS 18013 United States NS NINDS NIH HHS
    • Accession Number:
      0 (Ion Channels)
      0 (Liposomes)
      0 (Muscle Proteins)
      35523-89-8 (Saxitoxin)
      9NEZ333N27 (Sodium)
    • Publication Date:
      Date Created: 19820601 Date Completed: 19820917 Latest Revision: 20190501
    • Publication Date:
      20221213
    • Accession Number:
      PMC346481
    • Accession Number:
      10.1073/pnas.79.11.3651
    • Accession Number:
      6285356