Parkin prevents mitochondrial swelling and cytochrome c release in mitochondria-dependent cell death
Identifieur interne : 002372 ( Main/Curation ); précédent : 002371; suivant : 002373Parkin prevents mitochondrial swelling and cytochrome c release in mitochondria-dependent cell death
Auteurs : Fre De Ric Darios ; Olga Corti ; Christoph B. Lu Cking ; Cornelia Hampe ; Marie-Paule Muriel ; Nacer Abbas ; Wen-Jie Gu ; Etienne C. Hirsch ; Thomas Rooney [France] ; Merle Ruberg ; Alexis BriceSource :
- Human Molecular Genetics [ 0964-6906 ] ; 2003-03-01.
Abstract
Parkin gene mutations have been implicated in autosomal-recessive early-onset parkinsonism and lead to specific degeneration of dopaminergic neurons in midbrain. To investigate the role of Parkin in neuronal cell death, we overproduced this protein in PC12 cells in an inducible manner. In this cell line, neuronally differentiated by nerve growth factor, Parkin overproduction protected against cell death mediated by ceramide, but not by a variety of other cell death inducers (H2O2, 4-hydroxynonenal, rotenone, 6-OHDA, tunicamycin, 2-mercaptoethanol and staurosporine). Protection was abrogated by the proteasome inhibitor epoxomicin and disease-causing variants, indicating that it was mediated by the E3 ubiquitin ligase activity of Parkin. Interestingly, Parkin acted by delaying mitochondrial swelling and subsequent cytochrome c release and caspase-3 activation observed in ceramide-mediated cell death. Subcellular fractionation demonstrated enrichment of Parkin in the mitochondrial fraction and its association with the outer mitochondrial membrane. Together, these results suggest that Parkin may promote the degradation of substrates localized in mitochondria and involved in the late mitochondrial phase of ceramide-mediated cell death. Loss of this function may underlie the degeneration of nigral dopaminergic neurons in patients with Parkin mutations.
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DOI: 10.1093/hmg/ddg044
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Fre De Ric Darios<affiliation><mods:affiliation>INSERM U289, Hôpital de la Salpêtrière, 75013 Paris, France and</mods:affiliation><wicri:noCountry code="subField">France and</wicri:noCountry></affiliation><affiliation><mods:affiliation>INSERM U289, Hôpital de la Salpêtrière, 75013 Paris, France and</mods:affiliation><wicri:noCountry code="subField">France and</wicri:noCountry></affiliation><affiliation><mods:affiliation>INSERM U289, Hôpital de la Salpêtrière, 75013 Paris, France and</mods:affiliation><wicri:noCountry code="subField">France and</wicri:noCountry></affiliation><affiliation><mods:affiliation>INSERM U289, Hôpital de la Salpêtrière, 75013 Paris, France and</mods:affiliation><wicri:noCountry code="subField">France and</wicri:noCountry></affiliation><affiliation><mods:affiliation>INSERM U289, Hôpital de la Salpêtrière, 75013 Paris, France and</mods:affiliation><wicri:noCountry code="subField">France and</wicri:noCountry></affiliation><affiliation><mods:affiliation>INSERM U289, Hôpital de la Salpêtrière, 75013 Paris, France and</mods:affiliation><wicri:noCountry code="subField">France and</wicri:noCountry></affiliation><affiliation><mods:affiliation>INSERM U289, Hôpital de la Salpêtrière, 75013 Paris, France and</mods:affiliation><wicri:noCountry code="subField">France and</wicri:noCountry></affiliation><affiliation><mods:affiliation>INSERM U289, Hôpital de la Salpêtrière, 75013 Paris, France and</mods:affiliation><wicri:noCountry code="subField">France and</wicri:noCountry></affiliation><affiliation><mods:affiliation>INSERM U289, Hôpital de la Salpêtrière, 75013 Paris, France and</mods:affiliation><wicri:noCountry code="subField">France and</wicri:noCountry></affiliation><affiliation><mods:affiliation>INSERM U289, Hôpital de la Salpêtrière, 75013 Paris, France and</mods:affiliation><wicri:noCountry code="subField">France and</wicri:noCountry></affiliation>Le document en format XML
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Lu Cking</name><affiliation><mods:affiliation>INSERM U289, Hôpital de la Salpêtrière, 75013 Paris, France and</mods:affiliation><wicri:noCountry code="subField">France and</wicri:noCountry></affiliation></author><author><name sortKey="Hampe, Cornelia" sort="Hampe, Cornelia" uniqKey="Hampe C" first="Cornelia" last="Hampe">Cornelia Hampe</name><affiliation><mods:affiliation>INSERM U289, Hôpital de la Salpêtrière, 75013 Paris, France and</mods:affiliation><wicri:noCountry code="subField">France and</wicri:noCountry></affiliation></author><author><name sortKey="Muriel, Marie Paule" sort="Muriel, Marie Paule" uniqKey="Muriel M" first="Marie-Paule" last="Muriel">Marie-Paule Muriel</name><affiliation><mods:affiliation>INSERM U289, Hôpital de la Salpêtrière, 75013 Paris, France and</mods:affiliation><wicri:noCountry code="subField">France and</wicri:noCountry></affiliation></author><author><name sortKey="Abbas, Nacer" sort="Abbas, Nacer" uniqKey="Abbas N" first="Nacer" last="Abbas">Nacer Abbas</name><affiliation><mods:affiliation>INSERM U289, Hôpital de la Salpêtrière, 75013 Paris, France and</mods:affiliation><wicri:noCountry code="subField">France and</wicri:noCountry></affiliation></author><author><name sortKey="Gu, Wen Jie" sort="Gu, Wen Jie" uniqKey="Gu W" first="Wen-Jie" last="Gu">Wen-Jie Gu</name><affiliation><mods:affiliation>INSERM U289, Hôpital de la Salpêtrière, 75013 Paris, France and</mods:affiliation><wicri:noCountry code="subField">France and</wicri:noCountry></affiliation></author><author><name sortKey="Hirsch, Etienne C" sort="Hirsch, Etienne C" uniqKey="Hirsch E" first="Etienne C." last="Hirsch">Etienne C. Hirsch</name><affiliation><mods:affiliation>INSERM U289, Hôpital de la Salpêtrière, 75013 Paris, France and</mods:affiliation><wicri:noCountry code="subField">France and</wicri:noCountry></affiliation></author><author><name sortKey="Rooney, Thomas" sort="Rooney, Thomas" uniqKey="Rooney T" first="Thomas" last="Rooney">Thomas Rooney</name><affiliation wicri:level="1"><mods:affiliation>Aventis Pharma, 94400 Vitry-Sur-Seine, France</mods:affiliation><country xml:lang="fr">France</country><wicri:regionArea>Aventis Pharma, 94400 Vitry-Sur-Seine</wicri:regionArea></affiliation></author><author><name sortKey="Ruberg, Merle" sort="Ruberg, Merle" uniqKey="Ruberg M" first="Merle" last="Ruberg">Merle Ruberg</name><affiliation><mods:affiliation>INSERM U289, Hôpital de la Salpêtrière, 75013 Paris, France and</mods:affiliation><wicri:noCountry code="subField">France and</wicri:noCountry></affiliation></author><author><name sortKey="Brice, Alexis" sort="Brice, Alexis" uniqKey="Brice A" first="Alexis" last="Brice">Alexis Brice</name><affiliation><mods:affiliation>INSERM U289, Hôpital de la Salpêtrière, 75013 Paris, France and</mods:affiliation><wicri:noCountry code="subField">France and</wicri:noCountry></affiliation></author></analytic><monogr></monogr><series><title level="j">Human Molecular Genetics</title><title level="j" type="abbrev">Hum. Mol. Genet.</title><idno type="ISSN">0964-6906</idno><idno type="eISSN">1460-2083</idno><imprint><publisher>Oxford University Press</publisher><date type="published" when="2003-03-01">2003-03-01</date><biblScope unit="volume">12</biblScope><biblScope unit="issue">5</biblScope><biblScope unit="page" from="517">517</biblScope><biblScope unit="page" to="526">526</biblScope></imprint><idno type="ISSN">0964-6906</idno></series><idno type="istex">657759B8DA3EB71DB47D334186F46E0115B256A6</idno><idno type="DOI">10.1093/hmg/ddg044</idno><idno type="local">ddg044</idno></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0964-6906</idno></seriesStmt></fileDesc><profileDesc><textClass></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Parkin gene mutations have been implicated in autosomal-recessive early-onset parkinsonism and lead to specific degeneration of dopaminergic neurons in midbrain. To investigate the role of Parkin in neuronal cell death, we overproduced this protein in PC12 cells in an inducible manner. In this cell line, neuronally differentiated by nerve growth factor, Parkin overproduction protected against cell death mediated by ceramide, but not by a variety of other cell death inducers (H2O2, 4-hydroxynonenal, rotenone, 6-OHDA, tunicamycin, 2-mercaptoethanol and staurosporine). Protection was abrogated by the proteasome inhibitor epoxomicin and disease-causing variants, indicating that it was mediated by the E3 ubiquitin ligase activity of Parkin. Interestingly, Parkin acted by delaying mitochondrial swelling and subsequent cytochrome c release and caspase-3 activation observed in ceramide-mediated cell death. Subcellular fractionation demonstrated enrichment of Parkin in the mitochondrial fraction and its association with the outer mitochondrial membrane. Together, these results suggest that Parkin may promote the degradation of substrates localized in mitochondria and involved in the late mitochondrial phase of ceramide-mediated cell death. Loss of this function may underlie the degeneration of nigral dopaminergic neurons in patients with Parkin mutations.</div></front></TEI></record>Pour manipuler ce document sous Unix (Dilib)
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