Inhibition of the Ca2v+-activated K+-channel by sapecin B, an insect antibacterial protein

Masafumi Shimoda, Hiroshi Takagi, Shoichiro Kurata, Tohru Yoshioka, Shunji Natori

Research output: Contribution to journalArticlepeer-review

18 Citations (Scopus)

Abstract

Sapecin is an antibacterial protein of the flesh fly and sapecin B is its homologue structurally similar to charybdotoxin of scorpion venom, which is known to be a K+ channel inhibitor. We found that, like charybdotoxin, sapecin B inhibits part of the voltage pulse-induced K+ currents of rat cerebellar Purkinje cells. We suggest that this effect is due to inhibition of the Ca+-activated K+ channel. Probably, sapecin B is a naturally occurring K+ channel inhibitor as well as an antibacterial protein.

Original languageEnglish
Pages (from-to)59-62
Number of pages4
JournalFEBS Letters
Volume339
Issue number1-2
DOIs
Publication statusPublished - 1994 Feb 14
Externally publishedYes

Keywords

  • Antibacterial protein
  • Charybdotoxin
  • K channel inhibitor
  • Purkinje cell
  • Sapecin B

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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