Author
Listed:
- Latchezar D. Todorov
(University of Nevada School of Medicine)
- Svetlana Mihaylova-Todorova
(University of Nevada School of Medicine)
- Timothy D. Westfall
(University of Strathclyde, Royal College)
- Peter Sneddon
(University of Strathclyde, Royal College)
- Charles Kennedy
(University of Strathclyde, Royal College)
- Richard A. Bjur
(University of Nevada School of Medicine)
- David P. Westfall
(University of Nevada School of Medicine)
Abstract
Efficient control of synaptic transmission requires a rapid mechanism for terminating the actions of neurotransmitters. For amino acids and monoamines, this is achieved by their uptake into the cell by specific high-affinity transporters1; acetylcholine is first broken down in the extracellular space and then choline is taken up by the cell2. Because ATP is hydrolysed to adenosine by membrane-bound enzymes (ectonucleotidases) that are present in most tissues3,4, it has been assumed that these enzymes terminate the neurotransmitter actions of ATP in the brain5 and in the periphery6,7. We show here, however, that stimulation of sympathetic nerves innervating the guinea-pig vas deferens releases not only neuronal ATP, but also soluble nucleotidases that break down this ATP to adenosine, indicating that inactivation of ATP is increased by nerve activity. This release of specific nucleotidases together with ATP represents a new mechanism for terminating the actions of a neurotransmitter.
Suggested Citation
Latchezar D. Todorov & Svetlana Mihaylova-Todorova & Timothy D. Westfall & Peter Sneddon & Charles Kennedy & Richard A. Bjur & David P. Westfall, 1997.
"Neuronal release of soluble nucleotidases and their role in neurotransmitter inactivation,"
Nature, Nature, vol. 387(6628), pages 76-79, May.
Handle:
RePEc:nat:nature:v:387:y:1997:i:6628:d:10.1038_387076a0
DOI: 10.1038/387076a0
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