Coexistence of two classes of glibenclamide-inhibitable ATP-regulated K+ channels in avian skeletal muscle.

Avian skeletal muscle expresses two types of ATP-sensitive K+ channels which have a unitary conductance of 15pS. These K+ channels can be distinguished pharmacologically by their high or low sensitivity to the antidiabetic sulphonylurea blocker glibenclamide. Both channels are activated by the K+ channel opener cromakalim. Chick skeletal muscle expresses high-affinity binding sites for [3H]glibenclamide (Kd = 0.6nM) which presumably correspond to the ATP-sensitive K+ channels with the greatest sensitivity to glibenclamide. The density of these high-affinity binding sites varies during muscle development. The maximum density (500fmol/mg protein) appears at 16 days in ovo, i.e. at a period when myoblasts have differentiated into myotubes and when innervation of myotubes has started. After this maximum, the level of [3H]glibenclamide-binding sites decreases to a plateau value of 100fmol/mg protein at 2-5 days post-natal. When muscle cells are put in cultures, the high-affinity binding sites disappear rapidly. Neither glibenclamide nor cromakalim have any effect on normal physiological chick muscle contraction. They have no effect on contracture and/or 86Rb+ efflux produced by metabolic poisoning.