Sapecin B alters kinetic properties of rapidly inactivating K(+) channels in rat pituitary GH(3) cells.

Sapecin B is an antibacterial protein isolated and purified from culture medium of the embryonic cell line derived from the flesh fly (Sarcophaga peregrina). It has structural similarities to the scorpion toxin charybdotoxin (CTX). We have first detailed the effects of the newly described toxin (sapecin B) on the gating kinetics of the 4-aminopyridine-sensitive, rapidly inactivating K(+) current in rat pituitary GH(3) cells in order to investigate this protein's site of action, with whole-cell voltage-clamp methods. We have found that sapecin B alters the kinetics of activation and deactivation whereas there was no effect on the inactivation process. None of the effects of sapecin B was voltage dependent. In addition, sapecin B reduced whole-cell conductance. We suggest that the toxin may be ineffective against the voltage-sensitive segment, as well as the N-terminal and C-terminal domains, and CTX and sapecin B probably may have different binding sites.