Protein cysteine S-nitrosylation inhibits vesicular uptake of neurotransmitters.
Identifieur interne : 000352 ( PubMed/Corpus ); précédent : 000351; suivant : 000353Protein cysteine S-nitrosylation inhibits vesicular uptake of neurotransmitters.
Auteurs : Y. Wang ; Z. Zhou ; T. Leylek ; H. Tan ; Y. Sun ; F E Parkinson ; J-F WangSource :
- Neuroscience [ 1873-7544 ] ; 2015.
English descriptors
- KwdEn :
- Acetylcholine (metabolism), Animals, Brain (drug effects), Brain (metabolism), Dopamine (metabolism), Glutamic Acid (metabolism), Mice, Nitric Oxide (metabolism), Nitric Oxide Donors (pharmacology), S-Nitrosoglutathione (analogs & derivatives), S-Nitrosoglutathione (pharmacology), Tritium, Vesicular Acetylcholine Transport Proteins (metabolism), Vesicular Glutamate Transport Protein 1 (metabolism), Vesicular Glutamate Transport Protein 2 (metabolism), Vesicular Monoamine Transport Proteins (metabolism).
- MESH :
- chemical , analogs & derivatives : S-Nitrosoglutathione.
- chemical , metabolism : Acetylcholine, Dopamine, Glutamic Acid, Nitric Oxide, Vesicular Acetylcholine Transport Proteins, Vesicular Glutamate Transport Protein 1, Vesicular Glutamate Transport Protein 2, Vesicular Monoamine Transport Proteins.
- drug effects : Brain.
- metabolism : Brain.
- chemical , pharmacology : Nitric Oxide Donors, S-Nitrosoglutathione.
- Animals, Mice, Tritium.
Abstract
Previous studies have shown that nitric oxide can induce cysteine S-nitrosylation of total protein in synaptosomes, suggesting that nitric oxide may contribute to the regulation of synaptic protein function. Vesicular neurotransmitter transporters pack neurotransmitters into synaptic vesicles and play an important role in neurotransmission. In the central nervous system, vesicular monoamine transporter 2 (VMAT2) is responsible for the uptake of monoamines, vesicular acetylcholine transporter (VAChT) is responsible for the uptake of acetylcholine, while vesicular glutamate transporters 1 and 2 (VGLUT1 and VGLUT2) are responsible for the uptake of glutamate. The purpose of this study was to investigate the role of cysteine S-nitrosylation in the regulation of these vesicular neurotransmitter transporters. Using the biotin switch assay followed by avidin precipitation and immunoblotting we found that the nitric oxide donor nitrosoglutathione (GSNO) not only increased total cysteine S-nitrosylation, but also increased cysteine S-nitrosylation of VMAT2, VAChT, VGLUT1 and VGLUT2 in the mouse brain. Further, GSNO also decreased the vesicular uptake of [(3)H]dopamine, [(3)H]acetylcholine and [(3)H]glutamate. Our studies suggest that the cysteine S-nitrosylation may play an important role in the regulation of vesicular neurotransmitter transport.
DOI: 10.1016/j.neuroscience.2015.10.052
PubMed: 26541750
Links to Exploration step
pubmed:26541750Le document en format XML
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Leylek</name><affiliation><nlm:affiliation>Kleysen Institute for Advanced Medicine, Health Sciences Centre, Winnipeg, Canada; Department of Pharmacology and Therapeutics, University of Manitoba, Winnipeg, Canada.</nlm:affiliation></affiliation></author><author><name sortKey="Tan, H" sort="Tan, H" uniqKey="Tan H" first="H" last="Tan">H. Tan</name><affiliation><nlm:affiliation>Kleysen Institute for Advanced Medicine, Health Sciences Centre, Winnipeg, Canada; Department of Pharmacology and Therapeutics, University of Manitoba, Winnipeg, Canada.</nlm:affiliation></affiliation></author><author><name sortKey="Sun, Y" sort="Sun, Y" uniqKey="Sun Y" first="Y" last="Sun">Y. Sun</name><affiliation><nlm:affiliation>Kleysen Institute for Advanced Medicine, Health Sciences Centre, Winnipeg, Canada; Department of Pharmacology and Therapeutics, University of Manitoba, Winnipeg, Canada.</nlm:affiliation></affiliation></author><author><name sortKey="Parkinson, F E" sort="Parkinson, F E" uniqKey="Parkinson F" first="F E" last="Parkinson">F E Parkinson</name><affiliation><nlm:affiliation>Kleysen Institute for Advanced Medicine, Health Sciences Centre, Winnipeg, Canada; Department of Pharmacology and Therapeutics, University of Manitoba, Winnipeg, Canada.</nlm:affiliation></affiliation></author><author><name sortKey="Wang, J F" sort="Wang, J F" uniqKey="Wang J" first="J-F" last="Wang">J-F Wang</name><affiliation><nlm:affiliation>Kleysen Institute for Advanced Medicine, Health Sciences Centre, Winnipeg, Canada; Department of Pharmacology and Therapeutics, University of Manitoba, Winnipeg, Canada; Department of Psychiatry, University of Manitoba, Winnipeg, Canada. Electronic address: jun-feng.wang@umanitoba.ca.</nlm:affiliation></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2015">2015</date><idno type="RBID">pubmed:26541750</idno><idno type="pmid">26541750</idno><idno type="doi">10.1016/j.neuroscience.2015.10.052</idno><idno type="wicri:Area/PubMed/Corpus">000352</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">000352</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Protein cysteine S-nitrosylation inhibits vesicular uptake of neurotransmitters.</title><author><name sortKey="Wang, Y" sort="Wang, Y" uniqKey="Wang Y" first="Y" last="Wang">Y. Wang</name><affiliation><nlm:affiliation>Kleysen Institute for Advanced Medicine, Health Sciences Centre, Winnipeg, Canada; Department of Pharmacology and Therapeutics, University of Manitoba, Winnipeg, Canada.</nlm:affiliation></affiliation></author><author><name sortKey="Zhou, Z" sort="Zhou, Z" uniqKey="Zhou Z" first="Z" last="Zhou">Z. Zhou</name><affiliation><nlm:affiliation>Kleysen Institute for Advanced Medicine, Health Sciences Centre, Winnipeg, Canada; Department of Pharmacology and Therapeutics, University of Manitoba, Winnipeg, Canada.</nlm:affiliation></affiliation></author><author><name sortKey="Leylek, T" sort="Leylek, T" uniqKey="Leylek T" first="T" last="Leylek">T. Leylek</name><affiliation><nlm:affiliation>Kleysen Institute for Advanced Medicine, Health Sciences Centre, Winnipeg, Canada; Department of Pharmacology and Therapeutics, University of Manitoba, Winnipeg, Canada.</nlm:affiliation></affiliation></author><author><name sortKey="Tan, H" sort="Tan, H" uniqKey="Tan H" first="H" last="Tan">H. Tan</name><affiliation><nlm:affiliation>Kleysen Institute for Advanced Medicine, Health Sciences Centre, Winnipeg, Canada; Department of Pharmacology and Therapeutics, University of Manitoba, Winnipeg, Canada.</nlm:affiliation></affiliation></author><author><name sortKey="Sun, Y" sort="Sun, Y" uniqKey="Sun Y" first="Y" last="Sun">Y. Sun</name><affiliation><nlm:affiliation>Kleysen Institute for Advanced Medicine, Health Sciences Centre, Winnipeg, Canada; Department of Pharmacology and Therapeutics, University of Manitoba, Winnipeg, Canada.</nlm:affiliation></affiliation></author><author><name sortKey="Parkinson, F E" sort="Parkinson, F E" uniqKey="Parkinson F" first="F E" last="Parkinson">F E Parkinson</name><affiliation><nlm:affiliation>Kleysen Institute for Advanced Medicine, Health Sciences Centre, Winnipeg, Canada; Department of Pharmacology and Therapeutics, University of Manitoba, Winnipeg, Canada.</nlm:affiliation></affiliation></author><author><name sortKey="Wang, J F" sort="Wang, J F" uniqKey="Wang J" first="J-F" last="Wang">J-F Wang</name><affiliation><nlm:affiliation>Kleysen Institute for Advanced Medicine, Health Sciences Centre, Winnipeg, Canada; Department of Pharmacology and Therapeutics, University of Manitoba, Winnipeg, Canada; Department of Psychiatry, University of Manitoba, Winnipeg, Canada. Electronic address: jun-feng.wang@umanitoba.ca.</nlm:affiliation></affiliation></author></analytic><series><title level="j">Neuroscience</title><idno type="eISSN">1873-7544</idno><imprint><date when="2015" type="published">2015</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Acetylcholine (metabolism)</term><term>Animals</term><term>Brain (drug effects)</term><term>Brain (metabolism)</term><term>Dopamine (metabolism)</term><term>Glutamic Acid (metabolism)</term><term>Mice</term><term>Nitric Oxide (metabolism)</term><term>Nitric Oxide Donors (pharmacology)</term><term>S-Nitrosoglutathione (analogs & derivatives)</term><term>S-Nitrosoglutathione (pharmacology)</term><term>Tritium</term><term>Vesicular Acetylcholine Transport Proteins (metabolism)</term><term>Vesicular Glutamate Transport Protein 1 (metabolism)</term><term>Vesicular Glutamate Transport Protein 2 (metabolism)</term><term>Vesicular Monoamine Transport Proteins (metabolism)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="analogs & derivatives" xml:lang="en"><term>S-Nitrosoglutathione</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Acetylcholine</term><term>Dopamine</term><term>Glutamic Acid</term><term>Nitric Oxide</term><term>Vesicular Acetylcholine Transport Proteins</term><term>Vesicular Glutamate Transport Protein 1</term><term>Vesicular Glutamate Transport Protein 2</term><term>Vesicular Monoamine Transport Proteins</term></keywords><keywords scheme="MESH" qualifier="drug effects" xml:lang="en"><term>Brain</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Brain</term></keywords><keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Nitric Oxide Donors</term><term>S-Nitrosoglutathione</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Mice</term><term>Tritium</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Previous studies have shown that nitric oxide can induce cysteine S-nitrosylation of total protein in synaptosomes, suggesting that nitric oxide may contribute to the regulation of synaptic protein function. Vesicular neurotransmitter transporters pack neurotransmitters into synaptic vesicles and play an important role in neurotransmission. In the central nervous system, vesicular monoamine transporter 2 (VMAT2) is responsible for the uptake of monoamines, vesicular acetylcholine transporter (VAChT) is responsible for the uptake of acetylcholine, while vesicular glutamate transporters 1 and 2 (VGLUT1 and VGLUT2) are responsible for the uptake of glutamate. The purpose of this study was to investigate the role of cysteine S-nitrosylation in the regulation of these vesicular neurotransmitter transporters. Using the biotin switch assay followed by avidin precipitation and immunoblotting we found that the nitric oxide donor nitrosoglutathione (GSNO) not only increased total cysteine S-nitrosylation, but also increased cysteine S-nitrosylation of VMAT2, VAChT, VGLUT1 and VGLUT2 in the mouse brain. Further, GSNO also decreased the vesicular uptake of [(3)H]dopamine, [(3)H]acetylcholine and [(3)H]glutamate. Our studies suggest that the cysteine S-nitrosylation may play an important role in the regulation of vesicular neurotransmitter transport.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">26541750</PMID><DateCreated><Year>2015</Year><Month>11</Month><Day>28</Day></DateCreated><DateCompleted><Year>2016</Year><Month>09</Month><Day>14</Day></DateCompleted><DateRevised><Year>2015</Year><Month>11</Month><Day>28</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1873-7544</ISSN><JournalIssue CitedMedium="Internet"><Volume>311</Volume><PubDate><Year>2015</Year><Month>Dec</Month><Day>17</Day></PubDate></JournalIssue><Title>Neuroscience</Title><ISOAbbreviation>Neuroscience</ISOAbbreviation></Journal><ArticleTitle>Protein cysteine S-nitrosylation inhibits vesicular uptake of neurotransmitters.</ArticleTitle><Pagination><MedlinePgn>374-81</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1016/j.neuroscience.2015.10.052</ELocationID><ELocationID EIdType="pii" ValidYN="Y">S0306-4522(15)00980-X</ELocationID><Abstract><AbstractText>Previous studies have shown that nitric oxide can induce cysteine S-nitrosylation of total protein in synaptosomes, suggesting that nitric oxide may contribute to the regulation of synaptic protein function. Vesicular neurotransmitter transporters pack neurotransmitters into synaptic vesicles and play an important role in neurotransmission. In the central nervous system, vesicular monoamine transporter 2 (VMAT2) is responsible for the uptake of monoamines, vesicular acetylcholine transporter (VAChT) is responsible for the uptake of acetylcholine, while vesicular glutamate transporters 1 and 2 (VGLUT1 and VGLUT2) are responsible for the uptake of glutamate. The purpose of this study was to investigate the role of cysteine S-nitrosylation in the regulation of these vesicular neurotransmitter transporters. Using the biotin switch assay followed by avidin precipitation and immunoblotting we found that the nitric oxide donor nitrosoglutathione (GSNO) not only increased total cysteine S-nitrosylation, but also increased cysteine S-nitrosylation of VMAT2, VAChT, VGLUT1 and VGLUT2 in the mouse brain. Further, GSNO also decreased the vesicular uptake of [(3)H]dopamine, [(3)H]acetylcholine and [(3)H]glutamate. Our studies suggest that the cysteine S-nitrosylation may play an important role in the regulation of vesicular neurotransmitter transport.</AbstractText><CopyrightInformation>Copyright © 2015 IBRO. Published by Elsevier Ltd. All rights reserved.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Wang</LastName><ForeName>Y</ForeName><Initials>Y</Initials><AffiliationInfo><Affiliation>Kleysen Institute for Advanced Medicine, Health Sciences Centre, Winnipeg, Canada; Department of Pharmacology and Therapeutics, University of Manitoba, Winnipeg, Canada.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Zhou</LastName><ForeName>Z</ForeName><Initials>Z</Initials><AffiliationInfo><Affiliation>Kleysen Institute for Advanced Medicine, Health Sciences Centre, Winnipeg, Canada; Department of Pharmacology and Therapeutics, University of Manitoba, Winnipeg, Canada.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Leylek</LastName><ForeName>T</ForeName><Initials>T</Initials><AffiliationInfo><Affiliation>Kleysen Institute for Advanced Medicine, Health Sciences Centre, Winnipeg, Canada; Department of Pharmacology and Therapeutics, University of Manitoba, Winnipeg, Canada.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Tan</LastName><ForeName>H</ForeName><Initials>H</Initials><AffiliationInfo><Affiliation>Kleysen Institute for Advanced Medicine, Health Sciences Centre, Winnipeg, Canada; Department of Pharmacology and Therapeutics, University of Manitoba, Winnipeg, Canada.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Sun</LastName><ForeName>Y</ForeName><Initials>Y</Initials><AffiliationInfo><Affiliation>Kleysen Institute for Advanced Medicine, Health Sciences Centre, Winnipeg, Canada; Department of Pharmacology and Therapeutics, University of Manitoba, Winnipeg, Canada.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Parkinson</LastName><ForeName>F E</ForeName><Initials>FE</Initials><AffiliationInfo><Affiliation>Kleysen Institute for Advanced Medicine, Health Sciences Centre, Winnipeg, Canada; Department of Pharmacology and Therapeutics, University of Manitoba, Winnipeg, Canada.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Wang</LastName><ForeName>J-F</ForeName><Initials>JF</Initials><AffiliationInfo><Affiliation>Kleysen Institute for Advanced Medicine, Health Sciences Centre, Winnipeg, Canada; Department of Pharmacology and Therapeutics, University of Manitoba, Winnipeg, Canada; Department of Psychiatry, University of Manitoba, Winnipeg, Canada. 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Donors</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D026422" MajorTopicYN="N">S-Nitrosoglutathione</DescriptorName><QualifierName UI="Q000031" MajorTopicYN="N">analogs & derivatives</QualifierName><QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D014316" MajorTopicYN="N">Tritium</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D050494" MajorTopicYN="N">Vesicular Acetylcholine Transport Proteins</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D050598" MajorTopicYN="N">Vesicular Glutamate Transport Protein 1</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D050599" MajorTopicYN="N">Vesicular Glutamate Transport Protein 2</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D050493" MajorTopicYN="N">Vesicular Monoamine Transport Proteins</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading></MeshHeadingList><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">neurotransmitter uptake</Keyword><Keyword MajorTopicYN="N">nitric oxide</Keyword><Keyword MajorTopicYN="N">nitrosylation</Keyword><Keyword MajorTopicYN="N">vesicular neurotransmitter transporters</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2015</Year><Month>07</Month><Day>31</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2015</Year><Month>10</Month><Day>25</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2015</Year><Month>10</Month><Day>28</Day></PubMedPubDate><PubMedPubDate 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