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.
| Original language | English |
|---|---|
| Pages (from-to) | 5683-5686 |
| Number of pages | 4 |
| Journal | Proceedings of the National Academy of Sciences of the United States of America |
| Volume | 105 |
| Issue number | 15 |
| DOIs | |
| Publication status | Published - Apr 15 2008 |
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Keywords
- ATP
- Chromaffin granule
- Purinergic signaling
- Storage and exocytosis
- Synaptic vesicle
ASJC Scopus subject areas
- Genetics
- General
Cite this
Identification of a vesicular nucleotide transporter. / Sawada, Keisuke; Echigo, Noriko; Juge, Narinobu; Miyaji, Takaaki; Otsuka, Masato; Omote, Hiroshi; Yamamoto, Akitsugu; Moriyama, Yoshinori.
In: Proceedings of the National Academy of Sciences of the United States of America, Vol. 105, No. 15, 15.04.2008, p. 5683-5686.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Identification of a vesicular nucleotide transporter
AU - Sawada, Keisuke
AU - Echigo, Noriko
AU - Juge, Narinobu
AU - Miyaji, Takaaki
AU - Otsuka, Masato
AU - Omote, Hiroshi
AU - Yamamoto, Akitsugu
AU - Moriyama, Yoshinori
PY - 2008/4/15
Y1 - 2008/4/15
N2 - 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.
AB - 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.
KW - ATP
KW - Chromaffin granule
KW - Purinergic signaling
KW - Storage and exocytosis
KW - Synaptic vesicle
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U2 - 10.1073/pnas.0800141105
DO - 10.1073/pnas.0800141105
M3 - Article
VL - 105
SP - 5683
EP - 5686
JO - Proceedings of the National Academy of Sciences of the United States of America
JF - Proceedings of the National Academy of Sciences of the United States of America
SN - 0027-8424
IS - 15
ER -