Oxidative Stress Effect of Dopamine on α-Synuclein: Electroanalysis of Solvent Interactions
Identifieur interne : 000787 ( Pmc/Checkpoint ); précédent : 000786; suivant : 000788Oxidative Stress Effect of Dopamine on α-Synuclein: Electroanalysis of Solvent Interactions
Auteurs : Tiffiny Chan ; Ari M. Chow ; Xin R. Cheng ; Derek X0a W. F. Tang ; Ian R. Brown ; Kagan KermanSource :
- ACS Chemical Neuroscience [ 1948-7193 ] ; 2012.
Abstract
The interaction of dopamine (DA) and α-synuclein (α-S) can lead to protein misfolding and neuronal death triggered by oxidative stress relevant to the progression of Parkinson’s disease (PD). In this study, interfacial properties associated with DA-induced α-S aggregation under various solution conditions (i.e., pH, ionic strength) were investigated in vitro. The electrochemical oxidation of tyrosine (Tyr) residues in α-S was detected in the presence of DA. DA concentration dependence was analyzed and found to significantly affect α-S aggregation pathways. At low pH, DA was shown to be stable and produced no observable difference in interfacial properties. Between pH 7 and 11, DA promoted α-S aggregation. Significant differences in oxidation current signals in response to high pH and ionic strength suggested the importance of initial interactions in the stabilization of toxic oligomeric structures and subsequent off-pathways of α-S. Our results demonstrate the importance of solution interactions with α-S and the unique information that electrochemical techniques can provide for the investigation of α-S aggregation at early stages, an important step toward the development of future PD therapeutics.
Url:
DOI: 10.1021/cn300034t
PubMed: 22860226
PubMed Central: 3399574
Affiliations:
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of Dopamine on α-Synuclein:
Electroanalysis of Solvent Interactions</title><author><name sortKey="Chan, Tiffiny" sort="Chan, Tiffiny" uniqKey="Chan T" first="Tiffiny" last="Chan">Tiffiny Chan</name><affiliation><nlm:aff id="aff1">Department of Physical and Environmental Sciences,</nlm:aff></affiliation></author><author><name sortKey="Chow, Ari M" sort="Chow, Ari M" uniqKey="Chow A" first="Ari M." last="Chow">Ari M. Chow</name><affiliation><nlm:aff id="aff1">Centre for the Neurobiology of Stress, Department of Biological Sciences,<institution>University of Toronto Scarborough</institution>, 1265 Military Trail, Toronto, ON, M1C 1A4 Canada</nlm:aff><wicri:noCountry code="subfield">M1C 1A4 Canada</wicri:noCountry></affiliation></author><author><name sortKey="Cheng, Xin R" sort="Cheng, Xin R" uniqKey="Cheng X" first="Xin R." last="Cheng">Xin R. Cheng</name><affiliation><nlm:aff id="aff1">Department of Physical and Environmental Sciences,</nlm:aff></affiliation></author><author><name sortKey="Tang, Derek X0a W F" sort="Tang, Derek X0a W F" uniqKey="Tang D" first="Derek X0a W. F." last="Tang">Derek X0a W. F. Tang</name><affiliation><nlm:aff id="aff1">Centre for the Neurobiology of Stress, Department of Biological Sciences,<institution>University of Toronto Scarborough</institution>, 1265 Military Trail, Toronto, ON, M1C 1A4 Canada</nlm:aff><wicri:noCountry code="subfield">M1C 1A4 Canada</wicri:noCountry></affiliation></author><author><name sortKey="Brown, Ian R" sort="Brown, Ian R" uniqKey="Brown I" first="Ian R." last="Brown">Ian R. Brown</name><affiliation><nlm:aff id="aff1">Centre for the Neurobiology of Stress, Department of Biological Sciences,<institution>University of Toronto Scarborough</institution>, 1265 Military Trail, Toronto, ON, M1C 1A4 Canada</nlm:aff><wicri:noCountry code="subfield">M1C 1A4 Canada</wicri:noCountry></affiliation></author><author><name sortKey="Kerman, Kagan" sort="Kerman, Kagan" uniqKey="Kerman K" first="Kagan" last="Kerman">Kagan Kerman</name><affiliation><nlm:aff id="aff1">Department of Physical and Environmental Sciences,</nlm:aff></affiliation><affiliation><nlm:aff id="aff1">Centre for the Neurobiology of Stress, Department of Biological Sciences,<institution>University of Toronto Scarborough</institution>, 1265 Military Trail, Toronto, ON, M1C 1A4 Canada</nlm:aff><wicri:noCountry code="subfield">M1C 1A4 Canada</wicri:noCountry></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PMC</idno><idno type="pmid">22860226</idno><idno type="pmc">3399574</idno><idno type="url">http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3399574</idno><idno type="RBID">PMC:3399574</idno><idno type="doi">10.1021/cn300034t</idno><date when="2012">2012</date><idno type="wicri:Area/Pmc/Corpus">000187</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Corpus" wicri:corpus="PMC">000187</idno><idno type="wicri:Area/Pmc/Curation">000187</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Curation">000187</idno><idno type="wicri:Area/Pmc/Checkpoint">000787</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Checkpoint">000787</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">Oxidative Stress Effect
of Dopamine on α-Synuclein:
Electroanalysis of Solvent Interactions</title><author><name sortKey="Chan, Tiffiny" sort="Chan, Tiffiny" uniqKey="Chan T" first="Tiffiny" last="Chan">Tiffiny Chan</name><affiliation><nlm:aff id="aff1">Department of Physical and Environmental Sciences,</nlm:aff></affiliation></author><author><name sortKey="Chow, Ari M" sort="Chow, Ari M" uniqKey="Chow A" first="Ari M." last="Chow">Ari M. Chow</name><affiliation><nlm:aff id="aff1">Centre for the Neurobiology of Stress, Department of Biological Sciences,<institution>University of Toronto Scarborough</institution>, 1265 Military Trail, Toronto, ON, M1C 1A4 Canada</nlm:aff><wicri:noCountry code="subfield">M1C 1A4 Canada</wicri:noCountry></affiliation></author><author><name sortKey="Cheng, Xin R" sort="Cheng, Xin R" uniqKey="Cheng X" first="Xin R." last="Cheng">Xin R. Cheng</name><affiliation><nlm:aff id="aff1">Department of Physical and Environmental Sciences,</nlm:aff></affiliation></author><author><name sortKey="Tang, Derek X0a W F" sort="Tang, Derek X0a W F" uniqKey="Tang D" first="Derek X0a W. F." last="Tang">Derek X0a W. F. Tang</name><affiliation><nlm:aff id="aff1">Centre for the Neurobiology of Stress, Department of Biological Sciences,<institution>University of Toronto Scarborough</institution>, 1265 Military Trail, Toronto, ON, M1C 1A4 Canada</nlm:aff><wicri:noCountry code="subfield">M1C 1A4 Canada</wicri:noCountry></affiliation></author><author><name sortKey="Brown, Ian R" sort="Brown, Ian R" uniqKey="Brown I" first="Ian R." last="Brown">Ian R. Brown</name><affiliation><nlm:aff id="aff1">Centre for the Neurobiology of Stress, Department of Biological Sciences,<institution>University of Toronto Scarborough</institution>, 1265 Military Trail, Toronto, ON, M1C 1A4 Canada</nlm:aff><wicri:noCountry code="subfield">M1C 1A4 Canada</wicri:noCountry></affiliation></author><author><name sortKey="Kerman, Kagan" sort="Kerman, Kagan" uniqKey="Kerman K" first="Kagan" last="Kerman">Kagan Kerman</name><affiliation><nlm:aff id="aff1">Department of Physical and Environmental Sciences,</nlm:aff></affiliation><affiliation><nlm:aff id="aff1">Centre for the Neurobiology of Stress, Department of Biological Sciences,<institution>University of Toronto Scarborough</institution>, 1265 Military Trail, Toronto, ON, M1C 1A4 Canada</nlm:aff><wicri:noCountry code="subfield">M1C 1A4 Canada</wicri:noCountry></affiliation></author></analytic><series><title level="j">ACS Chemical Neuroscience</title><idno type="ISSN">1948-7193</idno><idno type="eISSN">1948-7193</idno><imprint><date when="2012">2012</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><p content-type="toc-graphic"><graphic xlink:href="cn-2012-00034t_0003" id="ab-tgr1"></graphic></p><p>The interaction of dopamine (DA) and α-synuclein
(α-S)
can lead to protein misfolding and neuronal death triggered by oxidative
stress relevant to the progression of Parkinson’s disease (PD).
In this study, interfacial properties associated with DA-induced α-S
aggregation under various solution conditions (i.e., pH, ionic strength)
were investigated in vitro. The electrochemical oxidation of tyrosine
(Tyr) residues in α-S was detected in the presence of DA. DA
concentration dependence was analyzed and found to significantly affect
α-S aggregation pathways. At low pH, DA was shown to be stable
and produced no observable difference in interfacial properties. Between
pH 7 and 11, DA promoted α-S aggregation. Significant differences
in oxidation current signals in response to high pH and ionic strength
suggested the importance of initial interactions in the stabilization
of toxic oligomeric structures and subsequent off-pathways of α-S.
Our results demonstrate the importance of solution interactions with
α-S and the unique information that electrochemical techniques
can provide for the investigation of α-S aggregation at early
stages, an important step toward the development of future PD therapeutics.</p></div></front></TEI><pmc article-type="research-article" xml:lang="EN"><pmc-comment>The publisher of this article does not allow downloading of the full text in XML form.</pmc-comment>
<front><journal-meta><journal-id journal-id-type="nlm-ta">ACS Chem Neurosci</journal-id><journal-id journal-id-type="iso-abbrev">ACS Chem Neurosci</journal-id><journal-id journal-id-type="publisher-id">cn</journal-id><journal-id journal-id-type="coden">acncdm</journal-id><journal-title-group><journal-title>ACS Chemical Neuroscience</journal-title></journal-title-group><issn pub-type="ppub">1948-7193</issn><issn pub-type="epub">1948-7193</issn><publisher><publisher-name>American Chemical
Society</publisher-name></publisher></journal-meta><article-meta><article-id pub-id-type="pmid">22860226</article-id><article-id pub-id-type="pmc">3399574</article-id><article-id pub-id-type="doi">10.1021/cn300034t</article-id><article-categories><subj-group><subject>Research Article</subject></subj-group></article-categories><title-group><article-title>Oxidative Stress Effect
of Dopamine on α-Synuclein:
Electroanalysis of Solvent Interactions</article-title></title-group><contrib-group><contrib contrib-type="author" id="ath1"><name><surname>Chan</surname><given-names>Tiffiny</given-names></name><xref rid="aff1" ref-type="aff">†</xref></contrib><contrib contrib-type="author" id="ath2"><name><surname>Chow</surname><given-names>Ari M.</given-names></name><xref rid="aff1" ref-type="aff">‡</xref></contrib><contrib contrib-type="author" id="ath3"><name><surname>Cheng</surname><given-names>Xin R.</given-names></name><xref rid="aff1" ref-type="aff">†</xref></contrib><contrib contrib-type="author" id="ath4"><name><surname>Tang</surname><given-names>Derek
W. F.</given-names></name><xref rid="aff1" ref-type="aff">‡</xref></contrib><contrib contrib-type="author" id="ath5"><name><surname>Brown</surname><given-names>Ian R.</given-names></name><xref rid="aff1" ref-type="aff">‡</xref></contrib><contrib contrib-type="author" corresp="yes" id="ath6"><name><surname>Kerman</surname><given-names>Kagan</given-names></name><xref rid="cor1" ref-type="other">*</xref><xref rid="aff1" ref-type="aff">†</xref><xref rid="aff1" ref-type="aff">‡</xref></contrib><aff id="aff1"><sup>†</sup>Department of Physical and Environmental Sciences,<sup>‡</sup>Centre for the Neurobiology of Stress, Department of Biological Sciences,<institution>University of Toronto Scarborough</institution>, 1265 Military Trail, Toronto, ON, M1C 1A4 Canada</aff></contrib-group><author-notes><corresp id="cor1"><label>*</label>E-mail: <email>kagan.kerman@utoronto.ca</email>. Telephone: <phone>+1-416-287-7249</phone>.</corresp></author-notes><pub-date pub-type="epub"><day>16</day><month>05</month><year>2012</year></pub-date><pub-date pub-type="collection"><day>18</day><month>07</month><year>2012</year></pub-date><volume>3</volume><issue>7</issue><fpage>569</fpage><lpage>574</lpage><history><date date-type="received"><day>14</day><month>03</month><year>2012</year></date><date date-type="accepted"><day>16</day><month>05</month><year>2012</year></date></history><permissions><copyright-statement>Copyright © 2012 American Chemical Society</copyright-statement><copyright-year>2012</copyright-year><copyright-holder>American Chemical Society</copyright-holder></permissions><abstract><p content-type="toc-graphic"><graphic xlink:href="cn-2012-00034t_0003" id="ab-tgr1"></graphic></p><p>The interaction of dopamine (DA) and α-synuclein
(α-S)
can lead to protein misfolding and neuronal death triggered by oxidative
stress relevant to the progression of Parkinson’s disease (PD).
In this study, interfacial properties associated with DA-induced α-S
aggregation under various solution conditions (i.e., pH, ionic strength)
were investigated in vitro. The electrochemical oxidation of tyrosine
(Tyr) residues in α-S was detected in the presence of DA. DA
concentration dependence was analyzed and found to significantly affect
α-S aggregation pathways. At low pH, DA was shown to be stable
and produced no observable difference in interfacial properties. Between
pH 7 and 11, DA promoted α-S aggregation. Significant differences
in oxidation current signals in response to high pH and ionic strength
suggested the importance of initial interactions in the stabilization
of toxic oligomeric structures and subsequent off-pathways of α-S.
Our results demonstrate the importance of solution interactions with
α-S and the unique information that electrochemical techniques
can provide for the investigation of α-S aggregation at early
stages, an important step toward the development of future PD therapeutics.</p></abstract><kwd-group><kwd>Dopamine</kwd><kwd>electroanalysis</kwd><kwd>α-synuclein</kwd><kwd>aggregation</kwd><kwd>tyrosine</kwd><kwd>Parkinson’s disease</kwd></kwd-group><custom-meta-group><custom-meta><meta-name>document-id-old-9</meta-name><meta-value>cn300034t</meta-value></custom-meta><custom-meta><meta-name>document-id-new-14</meta-name><meta-value>cn-2012-00034t</meta-value></custom-meta><custom-meta><meta-name>ccc-price</meta-name><meta-value></meta-value></custom-meta></custom-meta-group></article-meta><notes id="notes-500"><title>Author Contributions</title><p>T.C., A.M.C.,
X.R.C., and D.W.F.T. designed and performed experiments, analysed
data, and wrote the paper; I.R.B. and K.K. provided biological and
analytical tools, designed experiments, analysed data, and wrote the
paper.</p></notes></front></pmc><affiliations><list></list><tree><noCountry><name sortKey="Brown, Ian R" sort="Brown, Ian R" uniqKey="Brown I" first="Ian R." last="Brown">Ian R. Brown</name><name sortKey="Chan, Tiffiny" sort="Chan, Tiffiny" uniqKey="Chan T" first="Tiffiny" last="Chan">Tiffiny Chan</name><name sortKey="Cheng, Xin R" sort="Cheng, Xin R" uniqKey="Cheng X" first="Xin R." last="Cheng">Xin R. Cheng</name><name sortKey="Chow, Ari M" sort="Chow, Ari M" uniqKey="Chow A" first="Ari M." last="Chow">Ari M. Chow</name><name sortKey="Kerman, Kagan" sort="Kerman, Kagan" uniqKey="Kerman K" first="Kagan" last="Kerman">Kagan Kerman</name><name sortKey="Tang, Derek X0a W F" sort="Tang, Derek X0a W F" uniqKey="Tang D" first="Derek X0a W. F." last="Tang">Derek X0a W. F. Tang</name></noCountry></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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