Ouabain induces acetylcholine release from pure cholinergic synaptosomes independently of extracellular calcium concentration

Neurochem Res. 1988 Nov;13(11):1035-41. doi: 10.1007/BF00973147.

Abstract

We have studied the correlation between [3H]ouabain binding sites, (Na+ + K+)ATPase (EC 3.6.1.3) activity and acetylcholine (ACh) release in different subcellular fractions of Torpedo marmorata electric organ (homogenate, synaptosomes, presynaptic plasma membranes). Presynaptic plasma membranes contained the greater number of [3H]ouabain binding sites, in good agreement with the high (Na+ + K+)ATPase activity found in this fraction. Blockade of this enzymatic activity by ouabain dose-dependently induced ACh release from pure cholinergic synaptosomes, either in the presence or absence of extracellular calcium ions. We suggest that one of the mechanisms involved in the ouabain-induced ACh release in the absence of Ca2+o may be an increase in Na+i that could (a) evoke Ca2+ release from internal stores and (b) inhibit ATP-dependent Ca2+ uptake by synaptic vesicles.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acetylcholine / metabolism*
  • Animals
  • Calcium / metabolism*
  • Cell Membrane / metabolism
  • Cholinergic Fibers / metabolism*
  • Electric Organ
  • In Vitro Techniques
  • Ouabain / metabolism
  • Ouabain / pharmacology*
  • Radioligand Assay
  • Sodium / metabolism
  • Synaptosomes / metabolism*
  • Torpedo

Substances

  • Ouabain
  • Sodium
  • Acetylcholine
  • Calcium