Links to Exploration step
Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Characterization of Heparin-induced Glyceraldehyde-3-phosphate Dehydrogenase Early Amyloid-like Oligomers and Their Implication in α-Synuclein Aggregation<xref ref-type="fn" rid="FN1">*</xref><xref ref-type="fn" rid="FN2"><sup><inline-graphic xlink:href="sbox.jpg"></inline-graphic></sup></xref></title><author><name sortKey="Torres Bugeau, Clarisa M" sort="Torres Bugeau, Clarisa M" uniqKey="Torres Bugeau C" first="Clarisa M." last="Torres-Bugeau">Clarisa M. Torres-Bugeau</name><affiliation><nlm:aff id="aff1"></nlm:aff></affiliation></author><author><name sortKey="Avila, Cesar L" sort="Avila, Cesar L" uniqKey="Avila C" first="César L." last="Ávila">César L. Ávila</name><affiliation><nlm:aff id="aff1"></nlm:aff></affiliation></author><author><name sortKey="Raisman Vozari, Rita" sort="Raisman Vozari, Rita" uniqKey="Raisman Vozari R" first="Rita" last="Raisman-Vozari">Rita Raisman-Vozari</name><affiliation><nlm:aff id="aff2">INSERM, UMRS 975, CRICM, ICM, Thérapeutique Expérimentale de la Neurodégénérescence, Paris 91010 Créteil Cedex, France,</nlm:aff></affiliation></author><author><name sortKey="Papy Garcia, Dulce" sort="Papy Garcia, Dulce" uniqKey="Papy Garcia D" first="Dulce" last="Papy-Garcia">Dulce Papy-Garcia</name><affiliation><nlm:aff id="aff3"></nlm:aff></affiliation></author><author><name sortKey="Itri, Rosangela" sort="Itri, Rosangela" uniqKey="Itri R" first="Rosangela" last="Itri">Rosangela Itri</name><affiliation><nlm:aff id="aff4"></nlm:aff></affiliation></author><author><name sortKey="Barbosa, Leandro R S" sort="Barbosa, Leandro R S" uniqKey="Barbosa L" first="Leandro R. S." last="Barbosa">Leandro R. S. Barbosa</name><affiliation><nlm:aff id="aff4"></nlm:aff></affiliation></author><author><name sortKey="Cortez, Leonardo M" sort="Cortez, Leonardo M" uniqKey="Cortez L" first="Leonardo M." last="Cortez">Leonardo M. Cortez</name><affiliation><nlm:aff id="aff5"></nlm:aff></affiliation></author><author><name sortKey="Sim, Valerie L" sort="Sim, Valerie L" uniqKey="Sim V" first="Valerie L." last="Sim">Valerie L. Sim</name><affiliation><nlm:aff id="aff5"></nlm:aff></affiliation></author><author><name sortKey="Chehin, Rosana N" sort="Chehin, Rosana N" uniqKey="Chehin R" first="Rosana N." last="Chehín">Rosana N. Chehín</name><affiliation><nlm:aff id="aff1"></nlm:aff></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PMC</idno><idno type="pmid">22134915</idno><idno type="pmc">3268401</idno><idno type="url">http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3268401</idno><idno type="RBID">PMC:3268401</idno><idno type="doi">10.1074/jbc.M111.303503</idno><date when="2011">2011</date><idno type="wicri:Area/Pmc/Corpus">000563</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Corpus" wicri:corpus="PMC">000563</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">Characterization of Heparin-induced Glyceraldehyde-3-phosphate Dehydrogenase Early Amyloid-like Oligomers and Their Implication in α-Synuclein Aggregation<xref ref-type="fn" rid="FN1">*</xref><xref ref-type="fn" rid="FN2"><sup><inline-graphic xlink:href="sbox.jpg"></inline-graphic></sup></xref></title><author><name sortKey="Torres Bugeau, Clarisa M" sort="Torres Bugeau, Clarisa M" uniqKey="Torres Bugeau C" first="Clarisa M." last="Torres-Bugeau">Clarisa M. Torres-Bugeau</name><affiliation><nlm:aff id="aff1"></nlm:aff></affiliation></author><author><name sortKey="Avila, Cesar L" sort="Avila, Cesar L" uniqKey="Avila C" first="César L." last="Ávila">César L. Ávila</name><affiliation><nlm:aff id="aff1"></nlm:aff></affiliation></author><author><name sortKey="Raisman Vozari, Rita" sort="Raisman Vozari, Rita" uniqKey="Raisman Vozari R" first="Rita" last="Raisman-Vozari">Rita Raisman-Vozari</name><affiliation><nlm:aff id="aff2">INSERM, UMRS 975, CRICM, ICM, Thérapeutique Expérimentale de la Neurodégénérescence, Paris 91010 Créteil Cedex, France,</nlm:aff></affiliation></author><author><name sortKey="Papy Garcia, Dulce" sort="Papy Garcia, Dulce" uniqKey="Papy Garcia D" first="Dulce" last="Papy-Garcia">Dulce Papy-Garcia</name><affiliation><nlm:aff id="aff3"></nlm:aff></affiliation></author><author><name sortKey="Itri, Rosangela" sort="Itri, Rosangela" uniqKey="Itri R" first="Rosangela" last="Itri">Rosangela Itri</name><affiliation><nlm:aff id="aff4"></nlm:aff></affiliation></author><author><name sortKey="Barbosa, Leandro R S" sort="Barbosa, Leandro R S" uniqKey="Barbosa L" first="Leandro R. S." last="Barbosa">Leandro R. S. Barbosa</name><affiliation><nlm:aff id="aff4"></nlm:aff></affiliation></author><author><name sortKey="Cortez, Leonardo M" sort="Cortez, Leonardo M" uniqKey="Cortez L" first="Leonardo M." last="Cortez">Leonardo M. Cortez</name><affiliation><nlm:aff id="aff5"></nlm:aff></affiliation></author><author><name sortKey="Sim, Valerie L" sort="Sim, Valerie L" uniqKey="Sim V" first="Valerie L." last="Sim">Valerie L. Sim</name><affiliation><nlm:aff id="aff5"></nlm:aff></affiliation></author><author><name sortKey="Chehin, Rosana N" sort="Chehin, Rosana N" uniqKey="Chehin R" first="Rosana N." last="Chehín">Rosana N. Chehín</name><affiliation><nlm:aff id="aff1"></nlm:aff></affiliation></author></analytic><series><title level="j">The Journal of Biological Chemistry</title><idno type="ISSN">0021-9258</idno><idno type="eISSN">1083-351X</idno><imprint><date when="2011">2011</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><p><bold>Background:</bold> GAPDH and glycosaminoglycans (GAGs) have been routinely found in Parkinson disease amyloid aggregates.</p><p><bold>Results:</bold> Heparin and heparan sulfate induce the formation of GAPDH amyloid-like oligomers, which were characterized by using biophysical techniques.</p><p><bold>Conclusion:</bold> Heparin-induced GAPDH early oligomeric species are able to reduce the amount of α-synuclein (AS) prefibrillar species.</p><p><bold>Significance:</bold> GAPDH oligomeric species might be taken into account in recruiting of AS toxic species.</p></div></front></TEI><pmc article-type="research-article"><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">J Biol Chem</journal-id><journal-id journal-id-type="hwp">jbc</journal-id><journal-id journal-id-type="pmc">jbc</journal-id><journal-id journal-id-type="publisher-id">JBC</journal-id><journal-title-group><journal-title>The Journal of Biological Chemistry</journal-title></journal-title-group><issn pub-type="ppub">0021-9258</issn><issn pub-type="epub">1083-351X</issn><publisher><publisher-name>American Society for Biochemistry and Molecular Biology</publisher-name><publisher-loc>9650 Rockville Pike, Bethesda, MD 20814, U.S.A.</publisher-loc></publisher></journal-meta><article-meta><article-id pub-id-type="pmid">22134915</article-id><article-id pub-id-type="pmc">3268401</article-id><article-id pub-id-type="publisher-id">M111.303503</article-id><article-id pub-id-type="doi">10.1074/jbc.M111.303503</article-id><article-categories><subj-group subj-group-type="heading"><subject>Protein Structure and Folding</subject></subj-group></article-categories><title-group><article-title>Characterization of Heparin-induced Glyceraldehyde-3-phosphate Dehydrogenase Early Amyloid-like Oligomers and Their Implication in α-Synuclein Aggregation<xref ref-type="fn" rid="FN1">*</xref><xref ref-type="fn" rid="FN2"><sup><inline-graphic xlink:href="sbox.jpg"></inline-graphic></sup></xref></article-title><alt-title alt-title-type="short">Heparin-induced GAPDH Amyloid Aggregation</alt-title></title-group><contrib-group><contrib contrib-type="author"><name><surname>Torres-Bugeau</surname><given-names>Clarisa M.</given-names></name><xref ref-type="aff" rid="aff1"><sup>‡</sup></xref><xref ref-type="author-notes" rid="FN3"><sup>1</sup></xref></contrib><contrib contrib-type="author"><name><surname>Ávila</surname><given-names>César L.</given-names></name><xref ref-type="aff" rid="aff1"><sup>‡</sup></xref><xref ref-type="author-notes" rid="FN4"><sup>2</sup></xref></contrib><contrib contrib-type="author"><name><surname>Raisman-Vozari</surname><given-names>Rita</given-names></name><xref ref-type="aff" rid="aff2"><sup>§</sup></xref></contrib><contrib contrib-type="author"><name><surname>Papy-Garcia</surname><given-names>Dulce</given-names></name><xref ref-type="aff" rid="aff3"><sup>¶</sup></xref></contrib><contrib contrib-type="author"><name><surname>Itri</surname><given-names>Rosangela</given-names></name><xref ref-type="aff" rid="aff4"><sup>‖</sup></xref><xref ref-type="author-notes" rid="FN5"><sup>3</sup></xref></contrib><contrib contrib-type="author"><name><surname>Barbosa</surname><given-names>Leandro R. S.</given-names></name><xref ref-type="aff" rid="aff4"><sup>‖</sup></xref></contrib><contrib contrib-type="author"><name><surname>Cortez</surname><given-names>Leonardo M.</given-names></name><xref ref-type="aff" rid="aff5">**</xref></contrib><contrib contrib-type="author"><name><surname>Sim</surname><given-names>Valerie L.</given-names></name><xref ref-type="aff" rid="aff5">**</xref></contrib><contrib contrib-type="author"><name><surname>Chehín</surname><given-names>Rosana N.</given-names></name><xref ref-type="aff" rid="aff1"><sup>‡</sup></xref><xref ref-type="author-notes" rid="FN4"><sup>2</sup></xref><xref ref-type="corresp" rid="cor1"><sup>4</sup></xref></contrib><aff id="aff1">From the<label>‡</label>Instituto Superior de Investigaciones Biológicas, CCT-Tucumán and Insitituto de Química Biológica Dr Bernabé Bloj (CONICET-UNT), Tucumán T4000ILI, Argentina,</aff><aff id="aff2"><label>§</label>INSERM, UMRS 975, CRICM, ICM, Thérapeutique Expérimentale de la Neurodégénérescence, Paris 91010 Créteil Cedex, France,</aff><aff id="aff3">the<label>¶</label>Laboratoire CRRET EAC CNRS 7149, Université Paris Est Créteil, 94010 Créteil, France,</aff><aff id="aff4">the<label>‖</label>Instituto de Física da Universidade de São Paulo, São Paulo 05508-900, Brazil, and</aff><aff id="aff5">the<label>**</label>Centre for Prions and Protein Folding Diseases, University of Alberta, Edmonton, Alberta T6G 2M8, Canada</aff></contrib-group><author-notes><corresp id="cor1"><label>4</label> To whom correspondence should be addressed: <addr-line>INSIBIO, Chacabuco 461 (4000)-Tucuman-Argentina.</addr-line> Tel./Fax: <phone>54-381-4248921</phone>; E-mail: <email>rosana@fbqf.unt.edu.ar</email>.</corresp><fn fn-type="other" id="FN3"><label>1</label><p>Recipient of a CONICET fellowship.</p></fn><fn fn-type="other" id="FN4"><label>2</label><p>Researcher of CONICET.</p></fn><fn fn-type="other" id="FN5"><label>3</label><p>Recipient of a Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq) research fellowship.</p></fn></author-notes><pub-date pub-type="ppub"><day>20</day><month>1</month><year>2012</year></pub-date><pub-date pub-type="epub"><day>1</day><month>12</month><year>2011</year></pub-date><volume>287</volume><issue>4</issue><fpage>2398</fpage><lpage>2409</lpage><history><date date-type="received"><day>12</day><month>9</month><year>2011</year></date><date date-type="rev-recd"><day>21</day><month>11</month><year>2011</year></date></history><permissions><copyright-statement>© 2012 by The American Society for Biochemistry and Molecular Biology, Inc.</copyright-statement><copyright-year>2012</copyright-year></permissions><self-uri xlink:title="pdf" xlink:type="simple" xlink:href="zbc00412002398.pdf"></self-uri><abstract abstract-type="teaser"><p><bold>Background:</bold> GAPDH and glycosaminoglycans (GAGs) have been routinely found in Parkinson disease amyloid aggregates.</p><p><bold>Results:</bold> Heparin and heparan sulfate induce the formation of GAPDH amyloid-like oligomers, which were characterized by using biophysical techniques.</p><p><bold>Conclusion:</bold> Heparin-induced GAPDH early oligomeric species are able to reduce the amount of α-synuclein (AS) prefibrillar species.</p><p><bold>Significance:</bold> GAPDH oligomeric species might be taken into account in recruiting of AS toxic species.</p></abstract><abstract><p>Lewy bodies and Lewy neurites, neuropathological hallmarks of several neurological diseases, are mainly made of filamentous assemblies of α-synuclein. However, other macromolecules including Tau, ubiquitin, glyceraldehyde-3-phosphate dehydrogenase, and glycosaminoglycans are routinely found associated with these amyloid deposits. Glyceraldehyde-3-phosphate dehydrogenase is a glycolytic enzyme that can form fibrillar aggregates in the presence of acidic membranes, but its role in Parkinson disease is still unknown. In this work, the ability of heparin to trigger the amyloid aggregation of this protein at physiological conditions of pH and temperature is demonstrated by infrared and fluorescence spectroscopy, dynamic light scattering, small angle x-ray scattering, circular dichroism, and fluorescence microscopy. Aggregation proceeds through the formation of short rod-like oligomers, which elongates in one dimension. Heparan sulfate was also capable of inducing glyceraldehyde-3-phosphate dehydrogenase aggregation, but chondroitin sulfates A, B, and C together with dextran sulfate had a negligible effect. Aided with molecular docking simulations, a putative binding site on the protein is proposed providing a rational explanation for the structural specificity of heparin and heparan sulfate. Finally, it is demonstrated that <italic>in vitro</italic> the early oligomers present in the glyceraldehyde-3-phosphate dehydrogenase fibrillation pathway promote α-synuclein aggregation. Taking into account the toxicity of α-synuclein prefibrillar species, the heparin-induced glyceraldehyde-3-phosphate dehydrogenase early oligomers might come in useful as a novel therapeutic strategy in Parkinson disease and other synucleinopathies.</p></abstract><kwd-group><kwd>Alpha-Synuclein</kwd><kwd>Amyloid</kwd><kwd>Glycosaminoglycan</kwd><kwd>Heparin</kwd><kwd>Parkinson Disease</kwd><kwd>Glyceraldehyde-3-phosphate Dehydrogenase Oligomers</kwd></kwd-group></article-meta></front></pmc></record>Pour manipuler ce document sous Unix (Dilib)
EXPLOR_STEP=$WICRI_ROOT/Wicri/Canada/explor/ParkinsonCanadaV1/Data/Pmc/Corpus
HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 000563 | SxmlIndent | more
Ou
HfdSelect -h $EXPLOR_AREA/Data/Pmc/Corpus/biblio.hfd -nk 000563 | SxmlIndent | more
Pour mettre un lien sur cette page dans le réseau Wicri
{{Explor lien
|wiki= Wicri/Canada
|area= ParkinsonCanadaV1
|flux= Pmc
|étape= Corpus
|type= RBID
|clé=
|texte=
}}
| This area was generated with Dilib version V0.6.29. |  |