Journal
NEUROCHEMISTRY INTERNATIONAL
Volume 47, Issue 4, Pages 243-247Publisher
PERGAMON-ELSEVIER SCIENCE LTD
DOI: 10.1016/j.neuint.2005.05.002
Keywords
vesicular acetylcholine transporter; vesamicol; tetraphenylphosphonium; ethidium; transport assay; acetylcholine-binding site; PC12(A123.7) cells
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Funding
- NINDS NIH HHS [NS15047] Funding Source: Medline
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The acetylcholine-binding site in vesicular acetylcholine transporter faces predominantly toward the outside of the vesicle when resting but predominantly toward the inside when transporting. Transport-related reorientation is detected by an ATP-induced decrease in the ability of saturating substrate to displace allosterically bound [3 H]vesamicol. The assay was used here to determine whether structurally diverse compounds are transported by rat VAChT expressed in PC12(A123.7) cells. Competition by ethidium, tetraphenylphosphonium and other monovalent organic cations with [H-3]vesamicol is decreased when ATP is added, and the effect depends on proton-motive force. The results indicate that many organic molecules carrying +1 charge are transported, even though the compounds do not resemble acetylcholine in structural details. (c) 2005 Elsevier Ltd. All rights reserved.
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