Vesicular acetylcholine transporter: Difference between revisions

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{{Infobox_gene}}
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The '''Vesicular acetylcholine transporter''' ('''VAChT''') is a [[neurotransmitter transporter]] which is responsible for loading [[acetylcholine]] (ACh) into [[Synaptic vesicle|secretory organelles]] in neurons making acetylcholine available for secretion.<ref name="pmid11099462">{{cite journal | vauthors = Erickson JD, Varoqui H | title = Molecular analysis of vesicular amine transporter function and targeting to secretory organelles | journal = FASEB Journal | volume = 14 | issue = 15 | pages = 2450–8 | date = Dec 2000 | pmid = 11099462 | doi = 10.1096/fj.00-0206rev }}</ref><ref name="pmid8622973">{{cite journal | vauthors = Weihe E, Tao-Cheng JH, Schäfer MK, Erickson JD, Eiden LE | title = Visualization of the vesicular acetylcholine transporter in cholinergic nerve terminals and its targeting to a specific population of small synaptic vesicles | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 93 | issue = 8 | pages = 3547–52 | date = Apr 1996 | pmid = 8622973 | pmc = 39647 | doi = 10.1073/pnas.93.8.3547 }}</ref> It is encoded by '''Solute carrier family 18, member 3''' (SLC18A3) [[gene]]. VAChT is able to transport ACh into vesicles by relying on an exchange between protons that were previously pumped into the vesicle diffusing out. ACh molecules are then carried into the vesicle by the action of exiting protons.<ref>{{cite web|last=Waymire|first=Jack|title=Storage of ACh|url=http://neuroscience.uth.tmc.edu/s1/chapter11.html|publisher=University of Texas Medical Center}}</ref> Acetylcholine transport utilizes a proton gradient established by a [[vacuolar ATPase]]. This gene is located within the first intron of the [[choline acetyltransferase]] gene.
The '''Vesicular acetylcholine transporter''' ('''VAChT''') is a [[neurotransmitter transporter]] which is responsible for loading [[acetylcholine]] (ACh) into [[Synaptic vesicle|secretory organelles]] in [[Neuron|neurons]] making acetylcholine available for secretion.<ref name="pmid11099462">{{cite journal | vauthors = Erickson JD, Varoqui H | title = Molecular analysis of vesicular amine transporter function and targeting to secretory organelles | journal = FASEB Journal | volume = 14 | issue = 15 | pages = 2450–8 | date = Dec 2000 | pmid = 11099462 | doi = 10.1096/fj.00-0206rev }}</ref><ref name="pmid8622973">{{cite journal | vauthors = Weihe E, Tao-Cheng JH, Schäfer MK, Erickson JD, Eiden LE | title = Visualization of the vesicular acetylcholine transporter in cholinergic nerve terminals and its targeting to a specific population of small synaptic vesicles | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 93 | issue = 8 | pages = 3547–52 | date = Apr 1996 | pmid = 8622973 | pmc = 39647 | doi = 10.1073/pnas.93.8.3547 }}</ref> It is encoded by '''Solute carrier family 18, member 3''' (SLC18A3) [[gene]], located within the first [[intron]] of the [[choline acetyltransferase]] gene. VAChT is able to transport ACh into vesicles by relying on an exchange between [[Proton|protons]] (H<sup>+</sup>) that were previously pumped into the vesicle diffusing out, thus acting as an [[antiporter]]. ACh molecules are then carried into the vesicle by the action of exiting protons.<ref>{{cite web|last=Waymire|first=Jack|title=Storage of ACh|url=http://neuroscience.uth.tmc.edu/s1/chapter11.html|publisher=University of Texas Medical Center}}</ref> Acetylcholine transport utilizes a proton gradient established by a [[vacuolar ATPase]].


== VAChT uptake inhibitors ==
== VAChT uptake inhibitors ==
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{{refbegin | 2}}
* {{cite journal | vauthors = Matsuo A, Bellier JP, Nishimura M, Yasuhara O, Saito N, Kimura H | title = Nuclear choline acetyltransferase activates transcription of a high-affinity choline transporter | journal = The Journal of Biological Chemistry | volume = 286 | issue = 7 | pages = 5836–45 | date = Feb 2011 | pmid = 21163949 | pmc = 3037696 | doi = 10.1074/jbc.M110.147611 }}
* {{cite journal | vauthors = Matsuo A, Bellier JP, Nishimura M, Yasuhara O, Saito N, Kimura H | title = Nuclear choline acetyltransferase activates transcription of a high-affinity choline transporter | journal = The Journal of Biological Chemistry | volume = 286 | issue = 7 | pages = 5836–45 | date = Feb 2011 | pmid = 21163949 | pmc = 3037696 | doi = 10.1074/jbc.M110.147611 }}
* {{cite journal | vauthors = Lau JK, Brown KC, Thornhill BA, Crabtree CM, Dom AM, Witte TR, Hardman WE, McNees CA, Stover CA, Carpenter AB, Luo H, Chen YC, Shiflett BS, Dasgupta P | title = Inhibition of cholinergic signaling causes apoptosis in human bronchioalveolar carcinoma | journal = Cancer Research | volume = 73 | issue = 4 | pages = 1328–39 | date = Feb 2013 | pmid = 23222296 | doi = 10.1158/0008-5472.CAN-12-3190 }}
* {{cite journal | vauthors = Lau JK, Brown KC, Thornhill BA, Crabtree CM, Dom AM, Witte TR, Hardman WE, McNees CA, Stover CA, Carpenter AB, Luo H, Chen YC, Shiflett BS, Dasgupta P | title = Inhibition of cholinergic signaling causes apoptosis in human bronchioalveolar carcinoma | journal = Cancer Research | volume = 73 | issue = 4 | pages = 1328–39 | date = Feb 2013 | pmid = 23222296 | doi = 10.1158/0008-5472.CAN-12-3190 | url = https://works.bepress.com/jamie_lau/3/download/ }}
* {{cite journal | vauthors = Varoqui H, Erickson JD | title = Active transport of acetylcholine by the human vesicular acetylcholine transporter | journal = The Journal of Biological Chemistry | volume = 271 | issue = 44 | pages = 27229–32 | date = Nov 1996 | pmid = 8910293 | doi = 10.1074/jbc.271.44.27229 }}
* {{cite journal | vauthors = Varoqui H, Erickson JD | title = Active transport of acetylcholine by the human vesicular acetylcholine transporter | journal = The Journal of Biological Chemistry | volume = 271 | issue = 44 | pages = 27229–32 | date = Nov 1996 | pmid = 8910293 | doi = 10.1074/jbc.271.44.27229 }}
* {{cite journal | vauthors = Harold D, Peirce T, Moskvina V, Myers A, Jones S, Hollingworth P, Moore P, Lovestone S, Powell J, Foy C, Archer N, Walter S, Edmonson A, McIlroy S, Craig D, Passmore PA, Goate A, Hardy J, O'Donovan M, Williams J, Liddell M, Owen MJ, Jones L | title = Sequence variation in the CHAT locus shows no association with late-onset Alzheimer's disease | journal = Human Genetics | volume = 113 | issue = 3 | pages = 258–67 | date = Aug 2003 | pmid = 12759818 | doi = 10.1007/s00439-003-0960-2 }}
* {{cite journal | vauthors = Harold D, Peirce T, Moskvina V, Myers A, Jones S, Hollingworth P, Moore P, Lovestone S, Powell J, Foy C, Archer N, Walter S, Edmonson A, McIlroy S, Craig D, Passmore PA, Goate A, Hardy J, O'Donovan M, Williams J, Liddell M, Owen MJ, Jones L | title = Sequence variation in the CHAT locus shows no association with late-onset Alzheimer's disease | journal = Human Genetics | volume = 113 | issue = 3 | pages = 258–67 | date = Aug 2003 | pmid = 12759818 | doi = 10.1007/s00439-003-0960-2 }}

Latest revision as of 19:06, 30 November 2018

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The Vesicular acetylcholine transporter (VAChT) is a neurotransmitter transporter which is responsible for loading acetylcholine (ACh) into secretory organelles in neurons making acetylcholine available for secretion.[1][2] It is encoded by Solute carrier family 18, member 3 (SLC18A3) gene, located within the first intron of the choline acetyltransferase gene. VAChT is able to transport ACh into vesicles by relying on an exchange between protons (H+) that were previously pumped into the vesicle diffusing out, thus acting as an antiporter. ACh molecules are then carried into the vesicle by the action of exiting protons.[3] Acetylcholine transport utilizes a proton gradient established by a vacuolar ATPase.

VAChT uptake inhibitors

Radiolabeled compounds

PET imaging of the VAChT may provide insights into early diagnosis of Alzheimer's disease.

  • (−)-trans-2-Hydroxy-3-(4-(4-[18F]fluorobenzoyl)piperidino)tetralin; racemate: Ki = 2.70 nM for VAChT, 191 nM for σ1, and 251 nM for σ2[4]

References

  1. ↑ Erickson JD, Varoqui H (Dec 2000). "Molecular analysis of vesicular amine transporter function and targeting to secretory organelles". FASEB Journal. 14 (15): 2450–8. doi:10.1096/fj.00-0206rev. PMID 11099462.
  2. ↑ Weihe E, Tao-Cheng JH, Schäfer MK, Erickson JD, Eiden LE (Apr 1996). "Visualization of the vesicular acetylcholine transporter in cholinergic nerve terminals and its targeting to a specific population of small synaptic vesicles". Proceedings of the National Academy of Sciences of the United States of America. 93 (8): 3547–52. doi:10.1073/pnas.93.8.3547. PMC 39647. PMID 8622973.
  3. ↑ Waymire, Jack. "Storage of ACh". University of Texas Medical Center.
  4. ↑ Tu Z, Efange SM, Xu J, Li S, Jones LA, Parsons SM, Mach RH (Mar 2009). "Synthesis and in vitro and in vivo evaluation of 18F-labeled positron emission tomography (PET) ligands for imaging the vesicular acetylcholine transporter". Journal of Medicinal Chemistry. 52 (5): 1358–69. doi:10.1021/jm8012344. PMC 2765529. PMID 19203271.

Further reading

External links


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