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Pflügers Archiv

, Volume 431, Issue 1, pp 117–124 | Cite as

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

  • Michel Fosset
  • Bruno Allard
  • Michel Lazdunski
Original Article Neurophysiology, Muscle and Sensory Organs

Abstract

Avian skeletal muscle expresses two types of ATP-sensitive K+ channels which have a unitary conductance of 15 pS. 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=0.6 nM) 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 (500 fmol/mg protein) appears at 16 days in ovo, i.e. at a period when myoblasts have di¤erentiated 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 100 fmol/mg protein at 2–5 days postnatal. 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.

Key words

Muscle KATP channels Glibenclamide Avian muscle contraction Binding studies Muscle poisoning 

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Copyright information

© Springer-Verlag 1995

Authors and Affiliations

  • Michel Fosset
    • 1
  • Bruno Allard
    • 2
  • Michel Lazdunski
    • 1
  1. 1.Institut de Pharmacologie Moléculaire et CellulaireSophia AntipolisFrance
  2. 2.Laboratoire de Physiologie des Eléments ExcitablesUniversité Claude BernardVilleurbanne CedexFrance

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