Inhibition of the Ca(2+)-activated K(+)-channel by sapecin B, an insect antibacterial protein.
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.
Shimoda
M
M
Faculty of Pharmaceutical Sciences, University of Tokyo, Japan.
Takagi
H
H
Kurata
S
S
Yoshioka
T
T
Natori
S
S
D000818:Animals; D000890:Anti-Infective Agents / Q000494:pharmacology*; D002118:Calcium / Q000378:metabolism; D002460:Cell Line; D018999:Charybdotoxin; D004175:Diptera; D004553:Electric Conductivity; D007301:Insect Hormones / Q000494:pharmacology*; D019476:Insect Proteins; D026902:Potassium Channel Blockers; D015221:Potassium Channels / Q000502:physiology; D011689:Purkinje Cells / Q000502:physiology; D051381:Rats; D012604:Scorpion Venoms / Q000494:pharmacology
D000890:Anti-Infective Agents; D007301:Insect Hormones; D019476:Insect Proteins; D026902:Potassium Channel Blockers; D015221:Potassium Channels; D012604:Scorpion Venoms; C080667:sapecin B protein, Sarcophaga peregrina; D018999:Charybdotoxin; D002118:Calcium