Na-K-activated ATPase and the release of acetylcholine and noradrenaline

E. S. Vizi, T. Torok, A. Seregi, P. Serfǒzǒ, V. Adam-Vizi

Research output: Contribution to journalArticle

39 Citations (Scopus)


It has been shown that different experimental conditions known to inhibit Na-K-activated ATPase, an enzyme present in the neuronal membranes, are able to promote transmitter release (ACh, NA, etc.) from different tissues, simply by making the membrane leaky. Under physiological conditions, Ca entering the cell transiently inhibits membrane ATPase, resulting in a transient change in membrane permeability and a subsequent release of transmitter. When membrane ATPase inhibitor was used one part of the release proved to be Ca-independent. This finding indicates that the voltage and Ca-dependent link of transmitter release can be by-passed by direct membrane ATPase inhibitors (ouabain). Neurochemical and electrophysiological evidence was obtained on mouse diaphragm that most of the released ACh is cytoplasmic and Na-K ATPase inhibition is reponsible for its release. The stimulation of membrane ATPase (by switching off K and its readmission) results in an inhibition of both ACh and noradrenaline release evoked by axonal stimulation. It is suggested that, in those cases where the varicose axon terminals do not make synaptic contact, the transmitter released from the cytoplasmic pool contributes to the transmission, since during diffusion (sometimes few thousand nm) transmitter of different origins becomes mixed up.

Original languageEnglish
Pages (from-to)399-406
Number of pages8
JournalJournal de Physiologie
Issue number4
Publication statusPublished - Dec 1 1982

ASJC Scopus subject areas

  • Physiology

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