Aggregation and neurotoxicity of recombinant α-synuclein aggregates initiated by dimerization
Identifieur interne : 000E73 ( Main/Merge ); précédent : 000E72; suivant : 000E74Aggregation and neurotoxicity of recombinant α-synuclein aggregates initiated by dimerization
Auteurs : Alireza Roostaee [Canada] ; Simon Beaudoin [Canada] ; Antanas Staskevicius [Canada] ; Xavier Roucou [Canada]Source :
- Molecular Neurodegeneration [ 1750-1326 ] ; 2013.
English descriptors
- KwdEn :
- Animals, Hippocampus (pathology), In Situ Nick-End Labeling, Male, Mice, Mice, Inbred C57BL, Parkinson Disease (pathology), Protein Multimerization, Protein Structure, Secondary, Recombinant Proteins (chemistry), Recombinant Proteins (toxicity), alpha-Synuclein (chemistry), alpha-Synuclein (toxicity).
- MESH :
- chemical , chemistry : Recombinant Proteins, alpha-Synuclein.
- pathology : Hippocampus, Parkinson Disease.
- chemical , toxicity : Recombinant Proteins, alpha-Synuclein.
- Animals, In Situ Nick-End Labeling, Male, Mice, Mice, Inbred C57BL, Protein Multimerization, Protein Structure, Secondary.
Abstract
Aggregation of the α-Synuclein (α-Syn) protein, amyloid fibril formation and progressive neurodegeneration are the neuropathological hallmarks of Parkinson's Disease (PD). However, a detailed mechanism of α-Syn aggregation/fibrillogenesis and the exact nature of toxic oligomeric species produced during amyloid formation process are still unknown.
In this study, the rates of α-Syn aggregation were compared for the recombinant wild-type (WT) α-Syn and a structurally relevant chimeric homologous protein containing an inducible Fv dimerizing domain (α-SynFv), capable to form dimers in the presence of a divalent ligand (AP20187). In the presence of AP20187, we report a rapid random coil into β-sheet conformational transformation of α-SynFv within 24 h, whereas WT α-Syn showed 24 h delay to achieve β-sheet structure after 48 h. Fluorescence ANS and ThT binding experiments demonstrate an accelerated oligomer/amyloid formation of dimerized α-SynFv, compared to the slower oligomerization and amyloidogenesis of WT α-Syn or α-SynFv without dimerizer AP20187. Both α-SynFv and α-Syn pre-fibrillar aggregates internalized cells and induced neurotoxicity when injected into the hippocampus of wild-type mice. These recombinant toxic aggregates further converted into non-toxic amyloids which were successfully amplified by protein misfolding cyclic amplification method, providing the first evidence for the
Together, we show that dimerization is important for α-Syn conformational transition and aggregation. In addition, α-Syn dimerization can accelerate the formation of neurotoxic aggregates and amyloid fibrils which can be amplified
Url:
DOI: 10.1186/1750-1326-8-5
PubMed: 23339399
PubMed Central: 3764494
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PMC:3764494Le document en format XML
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dimerization</title><author><name sortKey="Roostaee, Alireza" sort="Roostaee, Alireza" uniqKey="Roostaee A" first="Alireza" last="Roostaee">Alireza Roostaee</name><affiliation wicri:level="1"><nlm:aff id="I1">Department of Biochemistry, Université de Sherbrooke, 3001 12eme avenue nord, Sherbrooke J1H 5N4QC, Canada</nlm:aff><country xml:lang="fr">Canada</country><wicri:regionArea>Department of Biochemistry, Université de Sherbrooke, 3001 12eme avenue nord, Sherbrooke J1H 5N4QC</wicri:regionArea><wicri:noRegion>Sherbrooke J1H 5N4QC</wicri:noRegion></affiliation></author><author><name sortKey="Beaudoin, Simon" sort="Beaudoin, Simon" uniqKey="Beaudoin S" first="Simon" last="Beaudoin">Simon Beaudoin</name><affiliation wicri:level="1"><nlm:aff id="I1">Department of Biochemistry, Université de Sherbrooke, 3001 12eme avenue nord, Sherbrooke J1H 5N4QC, Canada</nlm:aff><country xml:lang="fr">Canada</country><wicri:regionArea>Department of Biochemistry, Université de Sherbrooke, 3001 12eme avenue nord, Sherbrooke J1H 5N4QC</wicri:regionArea><wicri:noRegion>Sherbrooke J1H 5N4QC</wicri:noRegion></affiliation></author><author><name sortKey="Staskevicius, Antanas" sort="Staskevicius, Antanas" uniqKey="Staskevicius A" first="Antanas" last="Staskevicius">Antanas Staskevicius</name><affiliation wicri:level="1"><nlm:aff id="I1">Department of Biochemistry, Université de Sherbrooke, 3001 12eme avenue nord, Sherbrooke J1H 5N4QC, Canada</nlm:aff><country xml:lang="fr">Canada</country><wicri:regionArea>Department of Biochemistry, Université de Sherbrooke, 3001 12eme avenue nord, Sherbrooke J1H 5N4QC</wicri:regionArea><wicri:noRegion>Sherbrooke J1H 5N4QC</wicri:noRegion></affiliation></author><author><name sortKey="Roucou, Xavier" sort="Roucou, Xavier" uniqKey="Roucou X" first="Xavier" last="Roucou">Xavier Roucou</name><affiliation wicri:level="1"><nlm:aff id="I1">Department of Biochemistry, Université de Sherbrooke, 3001 12eme avenue nord, Sherbrooke J1H 5N4QC, Canada</nlm:aff><country xml:lang="fr">Canada</country><wicri:regionArea>Department of Biochemistry, Université de Sherbrooke, 3001 12eme avenue nord, Sherbrooke J1H 5N4QC</wicri:regionArea><wicri:noRegion>Sherbrooke J1H 5N4QC</wicri:noRegion></affiliation></author></analytic><series><title level="j">Molecular Neurodegeneration</title><idno type="eISSN">1750-1326</idno><imprint><date when="2013">2013</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Animals</term><term>Hippocampus (pathology)</term><term>In Situ Nick-End Labeling</term><term>Male</term><term>Mice</term><term>Mice, Inbred C57BL</term><term>Parkinson Disease (pathology)</term><term>Protein Multimerization</term><term>Protein Structure, Secondary</term><term>Recombinant Proteins (chemistry)</term><term>Recombinant Proteins (toxicity)</term><term>alpha-Synuclein (chemistry)</term><term>alpha-Synuclein (toxicity)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Recombinant Proteins</term><term>alpha-Synuclein</term></keywords><keywords scheme="MESH" qualifier="pathology" xml:lang="en"><term>Hippocampus</term><term>Parkinson Disease</term></keywords><keywords scheme="MESH" type="chemical" qualifier="toxicity" xml:lang="en"><term>Recombinant Proteins</term><term>alpha-Synuclein</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>In Situ Nick-End Labeling</term><term>Male</term><term>Mice</term><term>Mice, Inbred C57BL</term><term>Protein Multimerization</term><term>Protein Structure, Secondary</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><sec><title>Background</title><p>Aggregation of the α-Synuclein (α-Syn) protein, amyloid fibril formation and progressive neurodegeneration are the neuropathological hallmarks of Parkinson's Disease (PD). However, a detailed mechanism of α-Syn aggregation/fibrillogenesis and the exact nature of toxic oligomeric species produced during amyloid formation process are still unknown.</p></sec><sec><title>Results</title><p>In this study, the rates of α-Syn aggregation were compared for the recombinant wild-type (WT) α-Syn and a structurally relevant chimeric homologous protein containing an inducible Fv dimerizing domain (α-Syn<sup>Fv</sup>), capable to form dimers in the presence of a divalent ligand (AP20187). In the presence of AP20187, we report a rapid random coil into β-sheet conformational transformation of α-Syn<sup>Fv</sup> within 24 h, whereas WT α-Syn showed 24 h delay to achieve β-sheet structure after 48 h. Fluorescence ANS and ThT binding experiments demonstrate an accelerated oligomer/amyloid formation of dimerized α-Syn<sup>Fv</sup>, compared to the slower oligomerization and amyloidogenesis of WT α-Syn or α-Syn<sup>Fv</sup> without dimerizer AP20187. Both α-Syn<sup>Fv</sup> and α-Syn pre-fibrillar aggregates internalized cells and induced neurotoxicity when injected into the hippocampus of wild-type mice. These recombinant toxic aggregates further converted into non-toxic amyloids which were successfully amplified by protein misfolding cyclic amplification method, providing the first evidence for the <italic>in vitro</italic> propagation of synthetic α-Syn aggregates.</p></sec><sec><title>Conclusions</title><p>Together, we show that dimerization is important for α-Syn conformational transition and aggregation. In addition, α-Syn dimerization can accelerate the formation of neurotoxic aggregates and amyloid fibrils which can be amplified <italic>in vitro</italic>. A detailed characterization of the mechanism of α-Syn aggregation/amyloidogenesis and toxicity is crucial to comprehend Parkinson's disease pathology at the molecular level.</p></sec></div></front><back><div1 type="bibliography"><listBibl><biblStruct><analytic><author><name sortKey="Baba, M" uniqKey="Baba M">M Baba</name></author><author><name sortKey="Nakajo, S" uniqKey="Nakajo S">S Nakajo</name></author><author><name sortKey="Tu, Ph" uniqKey="Tu P">PH Tu</name></author><author><name sortKey="Tomita, T" uniqKey="Tomita T">T Tomita</name></author><author><name sortKey="Nakaya, K" uniqKey="Nakaya K">K Nakaya</name></author><author><name sortKey="Lee, Vm" uniqKey="Lee V">VM Lee</name></author><author><name sortKey="Trojanowski, Jq" uniqKey="Trojanowski J">JQ Trojanowski</name></author><author><name sortKey="Iwatsubo, T" uniqKey="Iwatsubo T">T Iwatsubo</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Goedert, M" uniqKey="Goedert M">M 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J">J Freund</name></author><author><name sortKey="Kalbitzer, Hr" uniqKey="Kalbitzer H">HR Kalbitzer</name></author></analytic></biblStruct></listBibl></div1></back></TEI></record>Pour manipuler ce document sous Unix (Dilib)
EXPLOR_STEP=$WICRI_ROOT/Wicri/Canada/explor/ParkinsonCanadaV1/Data/Main/Merge
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