Alteration of the voltage-dependence of the twitch tension in frog skeletal muscle fibres by a polyether, Bistramide A.
Bistramide A, a toxin isolated from Lissoclinum bistratum Sluiter, was applied to frog skeletal muscle fibres. Micromolar concentrations of toxin decreased the amplitude of the twitch tension. Bistramide A shifted the activation and the steady-state inactivation characteristics of the tension on the voltage axis towards more positive and negative membrane potentials respectively. The data suggest that Bistramide A binds to the activated and inactivated state of the dihydropyridine-receptor which senses the T-tubule membrane potential.
Sauviat
M P
MP
Laboratoire de Physiologie Cellulaire (URA CNRS 1121), Université de Paris XI, Centre d'Orsay, France.
Verbist
J F
JF
D000081:Acetamides; D000818:Animals; D020746:Calcium Channels, L-Type; D004594:Electrophysiology; D004988:Ethers, Cyclic / Q000633:toxicity*; D066298:In Vitro Techniques; D008387:Marine Toxins / Q000633:toxicity*; D008564:Membrane Potentials / Q000187:drug effects / Q000502:physiology; D008954:Models, Biological; D009119:Muscle Contraction / Q000187:drug effects* / Q000502:physiology; D009124:Muscle Proteins / Q000187:drug effects / Q000502:physiology; D009132:Muscles / Q000187:drug effects / Q000502:physiology; D011714:Pyrans; D011893:Rana esculenta; D013141:Spiro Compounds
D000081:Acetamides; D020746:Calcium Channels, L-Type; D004988:Ethers, Cyclic; D008387:Marine Toxins; D009124:Muscle Proteins; D011714:Pyrans; D013141:Spiro Compounds; C059975:bistratene A