Neuronal release of soluble nucleotidases and their role in neurotransmitter inactivation

Latchezar D. Todorov, Svetlana Mihaylova-Todorova, Timothy D. Westfall, Peter Sneddon, Charles Kennedy, Richard A. Bjur and David P. Westfall
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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

Nature, 1997, vol. 387, issue 6628, 76-79

Abstract: 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.

Date: 1997
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DOI: 10.1038/387076a0

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