Mortalin inhibition in experimental Parkinson's disease
Identifieur interne : 000A98 ( Main/Curation ); précédent : 000A97; suivant : 000A99Mortalin inhibition in experimental Parkinson's disease
Auteurs : Davide Chiasserini [Italie] ; Alessandro Tozzi [Italie] ; Antonio De Iure [Italie] ; Michela Tantucci [Italie] ; Federica Susta [Italie] ; Pier Luigi Orvietani [Italie] ; Keizo Koya [États-Unis] ; Luciano Binaglia [Italie] ; Paolo Calabresi [Italie]Source :
- Movement Disorders [ 0885-3185 ] ; 2011-08-01.
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Abstract
Among heat shock proteins, mortalin has been linked to the pathogenesis of Parkinson's disease. In the present work a rat model of Parkinson's disease was used to analyze the expression of striatal proteins and, more specifically, mortalin expression. The possible involvement of mortalin in Parkinson's disease pathogenesis was further investigated by utilizing an electrophysiological approach and pharmacological inhibition of mortalin in both the physiological and the parkinsonian states. Proteomic analysis was used to investigate changes in striatal protein expression in the 6‐hydroxydopamine rat model of Parkinson's disease. The electrophysiological effects of MKT‐077, a rhodamine‐123 analogue acting as an inhibitor of mortalin, were measured by field potential recordings from corticostriatal brain slices obtained from control, sham‐operated, and 6‐hydroxydopamine–denervated animals. Slices in the presence of rotenone, an inhibitor of mitochondrial complex I, were also analyzed. Proteomic analysis revealed downregulation of mortalin in the striata of 6‐hydroxydopamine–treated rats in comparison with sham‐operated animals. MKT‐077 reduced corticostriatal field potential amplitude in physiological conditions, inducing membrane depolarization and inward current in striatal medium spiny neurons. In addition, we observed that concentrations of MKT‐077 not inducing any electrophysiological effect in physiological conditions caused significant changes in striatal slices from parkinsonian animals as well as in slices treated with a submaximal concentration of rotenone. These findings suggest a critical link between mortalin function and mitochondrial activity in both physiological and pathological conditions mimicking Parkinson's disease. © 2011 Movement Disorder Society
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DOI: 10.1002/mds.23647
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Lucia—I.R.C.C.S., Rome</wicri:regionArea></affiliation></author><author><name sortKey="Tantucci, Michela" sort="Tantucci, Michela" uniqKey="Tantucci M" first="Michela" last="Tantucci">Michela Tantucci</name><affiliation wicri:level="1"><mods:affiliation>Clinica Neurologica, Università degli studi di Perugia, Ospedale S. Maria della Misericordia, Perugia, Italy</mods:affiliation><country xml:lang="fr">Italie</country><wicri:regionArea>Clinica Neurologica, Università degli studi di Perugia, Ospedale S. Maria della Misericordia, Perugia</wicri:regionArea></affiliation></author><author><name sortKey="Susta, Federica" sort="Susta, Federica" uniqKey="Susta F" first="Federica" last="Susta">Federica Susta</name><affiliation wicri:level="1"><mods:affiliation>Dipartimento di Medicina Interna, Sezione di Biochimica, Università di Perugia, Perugia, Italy</mods:affiliation><country xml:lang="fr">Italie</country><wicri:regionArea>Dipartimento di Medicina Interna, Sezione di Biochimica, Università di Perugia, Perugia</wicri:regionArea></affiliation></author><author><name sortKey="Orvietani, Pier Luigi" sort="Orvietani, Pier Luigi" uniqKey="Orvietani P" first="Pier Luigi" last="Orvietani">Pier Luigi Orvietani</name><affiliation wicri:level="1"><mods:affiliation>Dipartimento di Medicina Interna, Sezione di Biochimica, Università di Perugia, Perugia, Italy</mods:affiliation><country xml:lang="fr">Italie</country><wicri:regionArea>Dipartimento di Medicina Interna, Sezione di Biochimica, Università di Perugia, Perugia</wicri:regionArea></affiliation></author><author><name sortKey="Koya, Keizo" sort="Koya, Keizo" uniqKey="Koya K" first="Keizo" last="Koya">Keizo Koya</name><affiliation wicri:level="1"><mods:affiliation>Synta Pharmaceuticals Corp., Lexington, Massachusetts, USA</mods:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Synta Pharmaceuticals Corp., Lexington, Massachusetts</wicri:regionArea></affiliation></author><author><name sortKey="Binaglia, Luciano" sort="Binaglia, Luciano" uniqKey="Binaglia L" first="Luciano" last="Binaglia">Luciano Binaglia</name><affiliation wicri:level="1"><mods:affiliation>Dipartimento di Medicina Interna, Sezione di Biochimica, Università di Perugia, Perugia, Italy</mods:affiliation><country xml:lang="fr">Italie</country><wicri:regionArea>Dipartimento di Medicina Interna, Sezione di Biochimica, Università di Perugia, Perugia</wicri:regionArea></affiliation></author><author><name sortKey="Calabresi, Paolo" sort="Calabresi, Paolo" uniqKey="Calabresi P" first="Paolo" last="Calabresi">Paolo Calabresi</name><affiliation wicri:level="1"><mods:affiliation>Clinica Neurologica, Università degli studi di Perugia, Ospedale S. Maria della Misericordia, Perugia, Italy</mods:affiliation><country xml:lang="fr">Italie</country><wicri:regionArea>Clinica Neurologica, Università degli studi di Perugia, Ospedale S. Maria della Misericordia, Perugia</wicri:regionArea></affiliation><affiliation wicri:level="1"><mods:affiliation>Fondazione S. Lucia—I.R.C.C.S., Rome, Italy</mods:affiliation><country xml:lang="fr">Italie</country><wicri:regionArea>Fondazione S. Lucia—I.R.C.C.S., Rome</wicri:regionArea></affiliation></author></analytic><monogr></monogr><series><title level="j">Movement Disorders</title><title level="j" type="abbrev">Mov. Disord.</title><idno type="ISSN">0885-3185</idno><idno type="eISSN">1531-8257</idno><imprint><publisher>Wiley Subscription Services, Inc., A Wiley Company</publisher><pubPlace>Hoboken</pubPlace><date type="published" when="2011-08-01">2011-08-01</date><biblScope unit="volume">26</biblScope><biblScope unit="issue">9</biblScope><biblScope unit="page" from="1639">1639</biblScope><biblScope unit="page" to="1647">1647</biblScope></imprint><idno type="ISSN">0885-3185</idno></series><idno type="istex">50D32C6A650908F0A66D37519E1B249E0D005A43</idno><idno type="DOI">10.1002/mds.23647</idno><idno type="ArticleID">MDS23647</idno></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0885-3185</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>6‐hydroxydopamine</term><term>Parkinson's disease</term><term>heat shock protein</term><term>mitochondria</term><term>mortalin</term><term>rotenone</term></keywords></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Among heat shock proteins, mortalin has been linked to the pathogenesis of Parkinson's disease. In the present work a rat model of Parkinson's disease was used to analyze the expression of striatal proteins and, more specifically, mortalin expression. The possible involvement of mortalin in Parkinson's disease pathogenesis was further investigated by utilizing an electrophysiological approach and pharmacological inhibition of mortalin in both the physiological and the parkinsonian states. Proteomic analysis was used to investigate changes in striatal protein expression in the 6‐hydroxydopamine rat model of Parkinson's disease. The electrophysiological effects of MKT‐077, a rhodamine‐123 analogue acting as an inhibitor of mortalin, were measured by field potential recordings from corticostriatal brain slices obtained from control, sham‐operated, and 6‐hydroxydopamine–denervated animals. Slices in the presence of rotenone, an inhibitor of mitochondrial complex I, were also analyzed. Proteomic analysis revealed downregulation of mortalin in the striata of 6‐hydroxydopamine–treated rats in comparison with sham‐operated animals. MKT‐077 reduced corticostriatal field potential amplitude in physiological conditions, inducing membrane depolarization and inward current in striatal medium spiny neurons. In addition, we observed that concentrations of MKT‐077 not inducing any electrophysiological effect in physiological conditions caused significant changes in striatal slices from parkinsonian animals as well as in slices treated with a submaximal concentration of rotenone. These findings suggest a critical link between mortalin function and mitochondrial activity in both physiological and pathological conditions mimicking Parkinson's disease. © 2011 Movement Disorder Society</div></front></TEI></record>Pour manipuler ce document sous Unix (Dilib)
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