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ID 34246
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Author
Sawada, Keisuke
Echigo, Noriko
Juge, Narinobu
Yamamoto, Akitsugu
Abstract

ATP is a major chemical transmitter in purinergic signal transmission. Before secretion, ATP is stored in secretory vesicles found in purinergic cells. Although the presence of active transport mechanisms for ATP has been postulated for a long time, the proteins responsible for its vesicular accumulation remains unknown. The transporter encoded by the human and mouse SLC17A9 gene, a novel member of an anion transporter family, was predominantly expressed in the brain and adrenal gland. The mouse and bovine counterparts were associated with adrenal chromaffin granules. Proteoliposomes containing purified transporter actively took up ATP, ADP, and GTP by using membrane potential as the driving force. The uptake properties of the reconstituted transporter were similar to that of the ATP uptake by synaptic vesicles and chromaffin granules. Suppression of endogenous SLC17A9 expression in PC12 cells decreased exocytosis of ATP. These findings strongly suggest that SLC17A9 protein is a vesicular nucleotide transporter and should lead to the elucidation of the molecular mechanism of ATP secretion in purinergic signal transmission.

Keywords
chromaffin granule
synaptic vesicle
ATP
storage and exocytosis
purinergic signaling.
Note
Published with permission from the copyright holder.
This is a author's copy,as published in PNAS , 2008
Publisher URL: http://dx.doi.org/10.1073/pnas.0800141105
Copyright © 2008 by the National Academy of Sciences
Published Date
2008-04-01
Publication Title
Proceedings of the National Academy of Sciences of the United States of America
Volume
volume105
Issue
issue15
Start Page
5683
End Page
5686
Content Type
Journal Article
language
英語
Refereed
True
DOI
Submission Path
biochemistry/8