Cathepsin D expression level affects alpha-synuclein processing, aggregation, and toxicity in vivo
Identifieur interne : 001E72 ( Main/Exploration ); précédent : 001E71; suivant : 001E73Cathepsin D expression level affects alpha-synuclein processing, aggregation, and toxicity in vivo
Auteurs : Valerie Cullen [États-Unis] ; Maria Lindfors [Finlande] ; Juliana Ng [Canada] ; Anders Paetau [Finlande] ; Erika Swinton [Canada] ; Piotr Kolodziej [Canada] ; Heather Boston [Canada] ; Paul Saftig [Allemagne] ; John Woulfe [Canada] ; Mel B. Feany [États-Unis] ; Liisa Myllykangas [Finlande] ; Michael G. Schlossmacher [États-Unis, Canada] ; Jaana Tyynel [Finlande]Source :
- Molecular Brain [ 1756-6606 ] ; 2009.
Abstract
Elevated
Over-expression of human
We conclude from these complementary investigations that: one, CathD can effectively degrade excess aSyn in dopaminergic cells; two,
Url:
DOI: 10.1186/1756-6606-2-5
PubMed: 19203374
PubMed Central: 2644690
Affiliations:
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<country xml:lang="fr">États-Unis</country>
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<author><name sortKey="Myllykangas, Liisa" sort="Myllykangas, Liisa" uniqKey="Myllykangas L" first="Liisa" last="Myllykangas">Liisa Myllykangas</name>
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<author><name sortKey="Schlossmacher, Michael G" sort="Schlossmacher, Michael G" uniqKey="Schlossmacher M" first="Michael G" last="Schlossmacher">Michael G. Schlossmacher</name>
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</placeName>
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<affiliation wicri:level="1"><nlm:aff id="I7">Division of Neuroscience, Ottawa Health Research Institute, Ottawa, Canada</nlm:aff>
<country xml:lang="fr">Canada</country>
<wicri:regionArea>Division of Neuroscience, Ottawa Health Research Institute, Ottawa</wicri:regionArea>
<wicri:noRegion>Ottawa</wicri:noRegion>
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<author><name sortKey="Tyynel, Jaana" sort="Tyynel, Jaana" uniqKey="Tyynel J" first="Jaana" last="Tyynel">Jaana Tyynel</name>
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<country xml:lang="fr">Finlande</country>
<wicri:regionArea>Institute of Biomedicine/Biochemistry, Helsinki University, Helsinki</wicri:regionArea>
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<front><div type="abstract" xml:lang="en"><sec><title>Background</title>
<p>Elevated <italic>SNCA </italic>
gene expression and intracellular accumulation of the encoded α-synuclein (aSyn) protein are associated with the development of Parkinson disease (PD). To date, few enzymes have been examined for their ability to degrade aSyn. Here, we explore the effects of <italic>CTSD </italic>
gene expression, which encodes the lysosomal protease cathepsin D (CathD), on aSyn processing.</p>
</sec>
<sec><title>Results</title>
<p>Over-expression of human <italic>CTSD </italic>
cDNA in dopaminergic MES23.5 cell cultures induced the marked proteolysis of exogenously expressed aSyn proteins in a dose-dependent manner. Unexpectedly, brain extractions, Western blotting and ELISA quantification revealed evidence for reduced levels of soluble endogenous aSyn in <italic>ctsd </italic>
knock-out mice. However, these CathD-deficient mice also contained elevated levels of insoluble, oligomeric aSyn species, as detected by formic acid extraction. In accordance, immunohistochemical studies of <italic>ctsd</italic>
-mutant brain from mice, sheep and humans revealed selective synucleinopathy-like changes that varied slightly among the three species. These changes included intracellular aSyn accumulation and formation of ubiquitin-positive inclusions. Furthermore, using an established <italic>Drosophila </italic>
model of human synucleinopathy, we observed markedly enhanced retinal toxicity in <italic>ctsd</italic>
-null flies.</p>
</sec>
<sec><title>Conclusion</title>
<p>We conclude from these complementary investigations that: one, CathD can effectively degrade excess aSyn in dopaminergic cells; two, <italic>ctsd </italic>
gene mutations result in a lysosomal storage disorder that includes microscopic and biochemical evidence of aSyn misprocessing; and three, CathD deficiency facilitates aSyn toxicity. We therefore postulate that CathD promotes 'synucleinase' activity, and that enhancing its function may lower aSyn concentrations <italic>in vivo</italic>
.</p>
</sec>
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<name sortKey="Myllykangas, Liisa" sort="Myllykangas, Liisa" uniqKey="Myllykangas L" first="Liisa" last="Myllykangas">Liisa Myllykangas</name>
<name sortKey="Myllykangas, Liisa" sort="Myllykangas, Liisa" uniqKey="Myllykangas L" first="Liisa" last="Myllykangas">Liisa Myllykangas</name>
<name sortKey="Paetau, Anders" sort="Paetau, Anders" uniqKey="Paetau A" first="Anders" last="Paetau">Anders Paetau</name>
<name sortKey="Tyynel, Jaana" sort="Tyynel, Jaana" uniqKey="Tyynel J" first="Jaana" last="Tyynel">Jaana Tyynel</name>
</country>
<country name="Canada"><noRegion><name sortKey="Ng, Juliana" sort="Ng, Juliana" uniqKey="Ng J" first="Juliana" last="Ng">Juliana Ng</name>
</noRegion>
<name sortKey="Boston, Heather" sort="Boston, Heather" uniqKey="Boston H" first="Heather" last="Boston">Heather Boston</name>
<name sortKey="Kolodziej, Piotr" sort="Kolodziej, Piotr" uniqKey="Kolodziej P" first="Piotr" last="Kolodziej">Piotr Kolodziej</name>
<name sortKey="Schlossmacher, Michael G" sort="Schlossmacher, Michael G" uniqKey="Schlossmacher M" first="Michael G" last="Schlossmacher">Michael G. Schlossmacher</name>
<name sortKey="Swinton, Erika" sort="Swinton, Erika" uniqKey="Swinton E" first="Erika" last="Swinton">Erika Swinton</name>
<name sortKey="Woulfe, John" sort="Woulfe, John" uniqKey="Woulfe J" first="John" last="Woulfe">John Woulfe</name>
</country>
<country name="Allemagne"><region name="Schleswig-Holstein"><name sortKey="Saftig, Paul" sort="Saftig, Paul" uniqKey="Saftig P" first="Paul" last="Saftig">Paul Saftig</name>
</region>
</country>
</tree>
</affiliations>
</record>
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