Striatal cholinergic neurotransmission requires VGLUT3.
Identifieur interne : 001164 ( Main/Exploration ); précédent : 001163; suivant : 001165Striatal cholinergic neurotransmission requires VGLUT3.
Auteurs : Alexandra B. Nelson ; Timothy G. Bussert ; Anatol C. Kreitzer [États-Unis] ; Rebecca P. Seal [États-Unis]Source :
- The Journal of neuroscience : the official journal of the Society for Neuroscience [ 1529-2401 ] ; 2014.
Descripteurs français
- KwdFr :
- Acide glutamique (métabolisme), Acétylcholine (métabolisme), Animaux, Corps strié (métabolisme), Corps strié (physiologie), Interneurones (métabolisme), Interneurones (physiologie), Neurones cholinergiques (métabolisme), Neurones cholinergiques (physiologie), Souris, Souris transgéniques, Systèmes de transport d'acides aminés acides (génétique), Systèmes de transport d'acides aminés acides (métabolisme), Transmission synaptique (physiologie).
- MESH :
- génétique : Systèmes de transport d'acides aminés acides.
- métabolisme : Acide glutamique, Acétylcholine, Corps strié, Interneurones, Neurones cholinergiques, Systèmes de transport d'acides aminés acides.
- physiologie : Corps strié, Interneurones, Neurones cholinergiques, Transmission synaptique.
- Animaux, Souris, Souris transgéniques.
English descriptors
- KwdEn :
- Acetylcholine (metabolism), Amino Acid Transport Systems, Acidic (genetics), Amino Acid Transport Systems, Acidic (metabolism), Animals, Cholinergic Neurons (metabolism), Cholinergic Neurons (physiology), Corpus Striatum (metabolism), Corpus Striatum (physiology), Glutamic Acid (metabolism), Interneurons (metabolism), Interneurons (physiology), Mice, Mice, Transgenic, Synaptic Transmission (physiology).
- MESH :
- chemical , genetics : Amino Acid Transport Systems, Acidic.
- chemical , metabolism : Acetylcholine, Amino Acid Transport Systems, Acidic, Glutamic Acid.
- metabolism : Cholinergic Neurons, Corpus Striatum, Interneurons.
- physiology : Cholinergic Neurons, Corpus Striatum, Interneurons, Synaptic Transmission.
- Animals, Mice, Mice, Transgenic.
Abstract
It is now clear that many neuronal populations release more than one classical neurotransmitter, yet in most cases the functional role of corelease is unknown. Striatal cholinergic interneurons release both glutamate and acetylcholine, and vesicular loading of glutamate has been shown to enhance acetylcholine content. Using a combination of optogenetics and whole-cell recordings in mice, we now provide physiological evidence that optogenetic stimulation of cholinergic interneurons triggers monosynaptic glutamate- and acetylcholine-mediated currents in striatal fast-spiking interneurons (FSIs), both of which depend on the expression of the vesicular glutamate transporter 3 (VGLUT3). In contrast to corticostriatal glutamatergic inputs onto FSIs, which are mediated primarily by AMPA-type glutamate receptors, glutamate release by cholinergic interneurons activates both AMPA- and NMDA-type glutamate receptors, suggesting a unique role for these inputs in the modulation of FSI activity. Importantly, we find that the loss of VGLUT3 not only markedly attenuates glutamatergic and cholinergic inputs on FSIs, but also significantly decreases disynaptic GABAergic input onto medium spiny neurons (MSNs), the major output neurons of the striatum. Our data demonstrate that VGLUT3 is required for normal cholinergic signaling onto FSIs, as well as for acetylcholine-dependent disynaptic inhibition of MSNs. Thus, by supporting fast glutamatergic transmission as well as by modulating the strength of cholinergic signaling, VGLUT3 has the capacity to exert widespread influence on the striatal network.
DOI: 10.1523/JNEUROSCI.0901-14.2014
PubMed: 24966377
Affiliations:
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Nelson</name><affiliation><nlm:affiliation>Gladstone Institute for Neurological Disease, J. David Gladstone Institutes, San Francisco, California 94158, Department of Neurology, University of California, San Francisco 94117.</nlm:affiliation><wicri:noCountry code="subField">San Francisco 94117</wicri:noCountry></affiliation></author><author><name sortKey="Bussert, Timothy G" sort="Bussert, Timothy G" uniqKey="Bussert T" first="Timothy G" last="Bussert">Timothy G. Bussert</name><affiliation><nlm:affiliation>Department of Neurobiology, University of Pittsburgh School of Medicine, Pittsburgh, Pennsylvania 15213, and.</nlm:affiliation><wicri:noCountry code="subField">and</wicri:noCountry></affiliation></author><author><name sortKey="Kreitzer, Anatol C" sort="Kreitzer, Anatol C" uniqKey="Kreitzer A" first="Anatol C" last="Kreitzer">Anatol C. Kreitzer</name><affiliation wicri:level="3"><nlm:affiliation>Gladstone Institute for Neurological Disease, J. David Gladstone Institutes, San Francisco, California 94158, Department of Neurology, University of California, San Francisco 94117, Department of Physiology, University of California at San Francisco, San Francisco, California 94117 rpseal@pitt.edu akreitzer@gladstone.ucsf.edu.</nlm:affiliation><country wicri:rule="url">États-Unis</country><wicri:regionArea>Gladstone Institute for Neurological Disease, J. David Gladstone Institutes, San Francisco, California 94158, Department of Neurology, University of California, San Francisco 94117, Department of Physiology, University of California at San Francisco, San Francisco</wicri:regionArea><placeName><settlement type="city">San Francisco</settlement><region type="state">Californie</region></placeName></affiliation></author><author><name sortKey="Seal, Rebecca P" sort="Seal, Rebecca P" uniqKey="Seal R" first="Rebecca P" last="Seal">Rebecca P. Seal</name><affiliation wicri:level="1"><nlm:affiliation>Department of Neurobiology, University of Pittsburgh School of Medicine, Pittsburgh, Pennsylvania 15213, and rpseal@pitt.edu akreitzer@gladstone.ucsf.edu.</nlm:affiliation><country wicri:rule="url">États-Unis</country><wicri:regionArea>Department of Neurobiology, University of Pittsburgh School of Medicine, Pittsburgh, Pennsylvania 15213</wicri:regionArea><wicri:noRegion>Pennsylvania 15213</wicri:noRegion></affiliation></author></analytic><series><title level="j">The Journal of neuroscience : the official journal of the Society for Neuroscience</title><idno type="eISSN">1529-2401</idno><imprint><date when="2014" type="published">2014</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Acetylcholine (metabolism)</term><term>Amino Acid Transport Systems, Acidic (genetics)</term><term>Amino Acid Transport Systems, Acidic (metabolism)</term><term>Animals</term><term>Cholinergic Neurons (metabolism)</term><term>Cholinergic Neurons (physiology)</term><term>Corpus Striatum (metabolism)</term><term>Corpus Striatum (physiology)</term><term>Glutamic Acid (metabolism)</term><term>Interneurons (metabolism)</term><term>Interneurons (physiology)</term><term>Mice</term><term>Mice, Transgenic</term><term>Synaptic Transmission (physiology)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Acide glutamique (métabolisme)</term><term>Acétylcholine (métabolisme)</term><term>Animaux</term><term>Corps strié (métabolisme)</term><term>Corps strié (physiologie)</term><term>Interneurones (métabolisme)</term><term>Interneurones (physiologie)</term><term>Neurones cholinergiques (métabolisme)</term><term>Neurones cholinergiques (physiologie)</term><term>Souris</term><term>Souris transgéniques</term><term>Systèmes de transport d'acides aminés acides (génétique)</term><term>Systèmes de transport d'acides aminés acides (métabolisme)</term><term>Transmission synaptique (physiologie)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Amino Acid Transport Systems, Acidic</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Acetylcholine</term><term>Amino Acid Transport Systems, Acidic</term><term>Glutamic Acid</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Systèmes de transport d'acides aminés acides</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Cholinergic Neurons</term><term>Corpus Striatum</term><term>Interneurons</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Acide glutamique</term><term>Acétylcholine</term><term>Corps strié</term><term>Interneurones</term><term>Neurones cholinergiques</term><term>Systèmes de transport d'acides aminés acides</term></keywords><keywords scheme="MESH" qualifier="physiologie" xml:lang="fr"><term>Corps strié</term><term>Interneurones</term><term>Neurones cholinergiques</term><term>Transmission synaptique</term></keywords><keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>Cholinergic Neurons</term><term>Corpus Striatum</term><term>Interneurons</term><term>Synaptic Transmission</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Mice</term><term>Mice, Transgenic</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Animaux</term><term>Souris</term><term>Souris transgéniques</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">It is now clear that many neuronal populations release more than one classical neurotransmitter, yet in most cases the functional role of corelease is unknown. Striatal cholinergic interneurons release both glutamate and acetylcholine, and vesicular loading of glutamate has been shown to enhance acetylcholine content. Using a combination of optogenetics and whole-cell recordings in mice, we now provide physiological evidence that optogenetic stimulation of cholinergic interneurons triggers monosynaptic glutamate- and acetylcholine-mediated currents in striatal fast-spiking interneurons (FSIs), both of which depend on the expression of the vesicular glutamate transporter 3 (VGLUT3). In contrast to corticostriatal glutamatergic inputs onto FSIs, which are mediated primarily by AMPA-type glutamate receptors, glutamate release by cholinergic interneurons activates both AMPA- and NMDA-type glutamate receptors, suggesting a unique role for these inputs in the modulation of FSI activity. Importantly, we find that the loss of VGLUT3 not only markedly attenuates glutamatergic and cholinergic inputs on FSIs, but also significantly decreases disynaptic GABAergic input onto medium spiny neurons (MSNs), the major output neurons of the striatum. Our data demonstrate that VGLUT3 is required for normal cholinergic signaling onto FSIs, as well as for acetylcholine-dependent disynaptic inhibition of MSNs. Thus, by supporting fast glutamatergic transmission as well as by modulating the strength of cholinergic signaling, VGLUT3 has the capacity to exert widespread influence on the striatal network.</div></front></TEI><affiliations><list><country><li>États-Unis</li></country><region><li>Californie</li></region><settlement><li>San Francisco</li></settlement></list><tree><noCountry><name sortKey="Bussert, Timothy G" sort="Bussert, Timothy G" uniqKey="Bussert T" first="Timothy G" last="Bussert">Timothy G. Bussert</name><name sortKey="Nelson, Alexandra B" sort="Nelson, Alexandra B" uniqKey="Nelson A" first="Alexandra B" last="Nelson">Alexandra B. Nelson</name></noCountry><country name="États-Unis"><region name="Californie"><name sortKey="Kreitzer, Anatol C" sort="Kreitzer, Anatol C" uniqKey="Kreitzer A" first="Anatol C" last="Kreitzer">Anatol C. Kreitzer</name></region><name sortKey="Seal, Rebecca P" sort="Seal, Rebecca P" uniqKey="Seal R" first="Rebecca P" last="Seal">Rebecca P. Seal</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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