Nanoparticles restore lysosomal acidification defects: Implications for Parkinson and other lysosomal-related diseases
Identifieur interne : 000120 ( Pmc/Curation ); précédent : 000119; suivant : 000121Nanoparticles restore lysosomal acidification defects: Implications for Parkinson and other lysosomal-related diseases
Auteurs : Mathieu Bourdenx [France] ; Jonathan Daniel [France] ; Emilie Genin [France] ; Federico N. Soria [France] ; Mireille Blanchard-Desce [France] ; Erwan Bezard [France] ; Benjamin Dehay [France]Source :
- Autophagy [ 1554-8627 ] ; 2016.
Abstract
Lysosomal impairment causes lysosomal storage disorders (LSD) and is involved in pathogenesis of neurodegenerative diseases, notably Parkinson disease (PD). Strategies enhancing or restoring lysosomal-mediated degradation thus appear as tantalizing disease-modifying therapeutics. Here we demonstrate that poly(DL-lactide-
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DOI: 10.1080/15548627.2015.1136769
PubMed: 26761717
PubMed Central: 4835967
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type="url">http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4835967</idno><idno type="RBID">PMC:4835967</idno><idno type="doi">10.1080/15548627.2015.1136769</idno><date when="2016">2016</date><idno type="wicri:Area/Pmc/Corpus">000120</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Corpus" wicri:corpus="PMC">000120</idno><idno type="wicri:Area/Pmc/Curation">000120</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Curation">000120</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">Nanoparticles restore lysosomal acidification defects: Implications for Parkinson and other lysosomal-related diseases</title><author><name sortKey="Bourdenx, Mathieu" sort="Bourdenx, Mathieu" uniqKey="Bourdenx M" first="Mathieu" last="Bourdenx">Mathieu Bourdenx</name><affiliation wicri:level="1"><nlm:aff id="af0001"><institution>University de Bordeaux, Institut des Maladies Neurodégénératives</institution>,<addr-line>UMR 5293</addr-line>, Bordeaux,<country>France</country></nlm:aff><country xml:lang="fr">France</country><wicri:regionArea># see nlm:aff country strict</wicri:regionArea></affiliation><affiliation wicri:level="1"><nlm:aff id="af0002"><institution>CNRS, Institut des Maladies Neurodégénératives</institution>,<addr-line>UMR 5293</addr-line>, Bordeaux,<country>France</country></nlm:aff><country xml:lang="fr">France</country><wicri:regionArea># see nlm:aff country strict</wicri:regionArea></affiliation></author><author><name sortKey="Daniel, Jonathan" sort="Daniel, Jonathan" uniqKey="Daniel J" first="Jonathan" last="Daniel">Jonathan Daniel</name><affiliation wicri:level="1"><nlm:aff id="af0003"><institution>University de Bordeaux, Institut des Sciences Moléculaires</institution>,<addr-line>UMR 5255</addr-line>, Talence,<country>France</country></nlm:aff><country xml:lang="fr">France</country><wicri:regionArea># see nlm:aff country strict</wicri:regionArea></affiliation></author><author><name sortKey="Genin, Emilie" sort="Genin, Emilie" uniqKey="Genin E" first="Emilie" last="Genin">Emilie Genin</name><affiliation wicri:level="1"><nlm:aff id="af0003"><institution>University de Bordeaux, Institut des Sciences Moléculaires</institution>,<addr-line>UMR 5255</addr-line>, Talence,<country>France</country></nlm:aff><country xml:lang="fr">France</country><wicri:regionArea># see nlm:aff country strict</wicri:regionArea></affiliation></author><author><name sortKey="Soria, Federico N" sort="Soria, Federico N" uniqKey="Soria F" first="Federico N." last="Soria">Federico N. Soria</name><affiliation wicri:level="1"><nlm:aff id="af0001"><institution>University de Bordeaux, Institut des Maladies Neurodégénératives</institution>,<addr-line>UMR 5293</addr-line>, Bordeaux,<country>France</country></nlm:aff><country xml:lang="fr">France</country><wicri:regionArea># see nlm:aff country strict</wicri:regionArea></affiliation><affiliation wicri:level="1"><nlm:aff id="af0002"><institution>CNRS, Institut des Maladies Neurodégénératives</institution>,<addr-line>UMR 5293</addr-line>, Bordeaux,<country>France</country></nlm:aff><country xml:lang="fr">France</country><wicri:regionArea># see nlm:aff country strict</wicri:regionArea></affiliation></author><author><name sortKey="Blanchard Desce, Mireille" sort="Blanchard Desce, Mireille" uniqKey="Blanchard Desce M" first="Mireille" last="Blanchard-Desce">Mireille Blanchard-Desce</name><affiliation wicri:level="1"><nlm:aff id="af0003"><institution>University de Bordeaux, Institut des Sciences Moléculaires</institution>,<addr-line>UMR 5255</addr-line>, Talence,<country>France</country></nlm:aff><country xml:lang="fr">France</country><wicri:regionArea># see nlm:aff country strict</wicri:regionArea></affiliation></author><author><name sortKey="Bezard, Erwan" sort="Bezard, Erwan" uniqKey="Bezard E" first="Erwan" last="Bezard">Erwan Bezard</name><affiliation wicri:level="1"><nlm:aff id="af0001"><institution>University de Bordeaux, Institut des Maladies Neurodégénératives</institution>,<addr-line>UMR 5293</addr-line>, Bordeaux,<country>France</country></nlm:aff><country xml:lang="fr">France</country><wicri:regionArea># see nlm:aff country strict</wicri:regionArea></affiliation><affiliation wicri:level="1"><nlm:aff id="af0002"><institution>CNRS, Institut des Maladies Neurodégénératives</institution>,<addr-line>UMR 5293</addr-line>, Bordeaux,<country>France</country></nlm:aff><country xml:lang="fr">France</country><wicri:regionArea># see nlm:aff country strict</wicri:regionArea></affiliation></author><author><name sortKey="Dehay, Benjamin" sort="Dehay, Benjamin" uniqKey="Dehay B" first="Benjamin" last="Dehay">Benjamin Dehay</name><affiliation wicri:level="1"><nlm:aff id="af0001"><institution>University de Bordeaux, Institut des Maladies Neurodégénératives</institution>,<addr-line>UMR 5293</addr-line>, Bordeaux,<country>France</country></nlm:aff><country xml:lang="fr">France</country><wicri:regionArea># see nlm:aff country strict</wicri:regionArea></affiliation><affiliation wicri:level="1"><nlm:aff id="af0002"><institution>CNRS, Institut des Maladies Neurodégénératives</institution>,<addr-line>UMR 5293</addr-line>, Bordeaux,<country>France</country></nlm:aff><country xml:lang="fr">France</country><wicri:regionArea># see nlm:aff country strict</wicri:regionArea></affiliation></author></analytic><series><title level="j">Autophagy</title><idno type="ISSN">1554-8627</idno><idno type="eISSN">1554-8635</idno><imprint><date when="2016">2016</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><title>ABSTRACT</title><p>Lysosomal impairment causes lysosomal storage disorders (LSD) and is involved in pathogenesis of neurodegenerative diseases, notably Parkinson disease (PD). Strategies enhancing or restoring lysosomal-mediated degradation thus appear as tantalizing disease-modifying therapeutics. Here we demonstrate that poly(DL-lactide-<italic>co</italic>-glycolide) (PLGA) acidic nanoparticles (aNP) restore impaired lysosomal function in a series of toxin and genetic cellular models of PD, i.e. ATP13A2-mutant or depleted cells or glucocerebrosidase (GBA)-mutant cells, as well as in a genetic model of lysosomal-related myopathy. We show that PLGA-aNP are transported to the lysosome within 24 h, lower lysosomal pH and rescue chloroquine (CQ)-induced toxicity. Re-acidification of defective lysosomes following PLGA-aNP treatment restores lysosomal function in different pathological contexts. Finally, our results show that PLGA-aNP may be detected after intracerebral injection in neurons and attenuate PD-related neurodegeneration in vivo by mechanisms involving a rescue of compromised lysosomes.</p></div></front></TEI><pmc article-type="brief-report"><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">Autophagy</journal-id><journal-id journal-id-type="iso-abbrev">Autophagy</journal-id><journal-id journal-id-type="pmc">KAUP</journal-id><journal-title-group><journal-title>Autophagy</journal-title></journal-title-group><issn pub-type="ppub">1554-8627</issn><issn pub-type="epub">1554-8635</issn><publisher><publisher-name>Taylor & Francis</publisher-name></publisher></journal-meta><article-meta><article-id pub-id-type="pmid">26761717</article-id><article-id pub-id-type="pmc">4835967</article-id><article-id pub-id-type="publisher-id">1136769</article-id><article-id pub-id-type="doi">10.1080/15548627.2015.1136769</article-id><article-categories><subj-group subj-group-type="heading"><subject>Translational Brief Report</subject></subj-group></article-categories><title-group><article-title>Nanoparticles restore lysosomal acidification defects: Implications for Parkinson and other lysosomal-related diseases</article-title><alt-title alt-title-type="running-authors">m. bourdenx ET AL</alt-title><alt-title alt-title-type="running-title">Autophagy</alt-title></title-group><contrib-group><contrib contrib-type="author"><name><surname>Bourdenx</surname><given-names>Mathieu</given-names></name><xref ref-type="aff" rid="af0001"><sup>a</sup></xref><xref ref-type="aff" rid="af0002"><sup>b</sup></xref></contrib><contrib contrib-type="author"><name><surname>Daniel</surname><given-names>Jonathan</given-names></name><xref ref-type="aff" rid="af0003"><sup>c</sup></xref></contrib><contrib contrib-type="author"><name><surname>Genin</surname><given-names>Emilie</given-names></name><xref ref-type="aff" rid="af0003"><sup>c</sup></xref></contrib><contrib contrib-type="author"><name><surname>Soria</surname><given-names>Federico N.</given-names></name><xref ref-type="aff" rid="af0001"><sup>a</sup></xref><xref ref-type="aff" rid="af0002"><sup>b</sup></xref></contrib><contrib contrib-type="author"><name><surname>Blanchard-Desce</surname><given-names>Mireille</given-names></name><xref ref-type="aff" rid="af0003"><sup>c</sup></xref></contrib><contrib contrib-type="author"><name><surname>Bezard</surname><given-names>Erwan</given-names></name><xref ref-type="aff" rid="af0001"><sup>a</sup></xref><xref ref-type="aff" rid="af0002"><sup>b</sup></xref></contrib><contrib contrib-type="author"><name><surname>Dehay</surname><given-names>Benjamin</given-names></name><xref ref-type="aff" rid="af0001"><sup>a</sup></xref><xref ref-type="aff" rid="af0002"><sup>b</sup></xref></contrib><aff id="af0001"><label>a</label><institution>University de Bordeaux, Institut des Maladies Neurodégénératives</institution>,<addr-line>UMR 5293</addr-line>, Bordeaux,<country>France</country></aff><aff id="af0002"><label>b</label><institution>CNRS, Institut des Maladies Neurodégénératives</institution>,<addr-line>UMR 5293</addr-line>, Bordeaux,<country>France</country></aff><aff id="af0003"><label>c</label><institution>University de Bordeaux, Institut des Sciences Moléculaires</institution>,<addr-line>UMR 5255</addr-line>, Talence,<country>France</country></aff></contrib-group><author-notes><corresp id="an0001"><bold>CONTACT</bold> Benjamin Dehay, Phd <email xlink:href="benjamin.dehay@u-bordeaux.fr">benjamin.dehay@u-bordeaux.fr</email><institution>CNRS UMR 5293, Institute of Neurodegenerative Diseases, University of Bordeaux</institution>, <addr-line>146 rue Léo Saignat</addr-line>, 33076 Bordeaux cedex, <country>France</country></corresp><fn><p>Color versions of one or more of the figures in the article can be found online at <uri xlink:href="http://www.tandfonline.com/kaup">www.tandfonline.com/kaup</uri>.</p></fn><fn><p>Supplemental data for this article can be accessed on the <ext-link ext-link-type="uri" xlink:href="http://dx.doi.org/10.1080/15548627.2015.1136769">publisher's website</ext-link>.</p></fn></author-notes><pub-date pub-type="collection"><month>3</month><year>2016</year></pub-date><pub-date pub-type="epub"><day>13</day><month>1</month><year>2016</year></pub-date><volume>12</volume><issue>3</issue><fpage seq="4">472</fpage><lpage>483</lpage><history><date date-type="received"><day>12</day><month>8</month><year>2014</year></date><date date-type="rev-recd"><day>19</day><month>12</month><year>2015</year></date><date date-type="accepted"><day>22</day><month>12</month><year>2015</year></date></history><permissions><copyright-statement>© 2016 Taylor & Francis</copyright-statement><copyright-year>2016</copyright-year><copyright-holder>Taylor & Francis</copyright-holder></permissions><self-uri content-type="pdf" xlink:href="kaup-12-03-1136769.pdf"></self-uri><abstract><title>ABSTRACT</title><p>Lysosomal impairment causes lysosomal storage disorders (LSD) and is involved in pathogenesis of neurodegenerative diseases, notably Parkinson disease (PD). Strategies enhancing or restoring lysosomal-mediated degradation thus appear as tantalizing disease-modifying therapeutics. Here we demonstrate that poly(DL-lactide-<italic>co</italic>-glycolide) (PLGA) acidic nanoparticles (aNP) restore impaired lysosomal function in a series of toxin and genetic cellular models of PD, i.e. ATP13A2-mutant or depleted cells or glucocerebrosidase (GBA)-mutant cells, as well as in a genetic model of lysosomal-related myopathy. We show that PLGA-aNP are transported to the lysosome within 24 h, lower lysosomal pH and rescue chloroquine (CQ)-induced toxicity. Re-acidification of defective lysosomes following PLGA-aNP treatment restores lysosomal function in different pathological contexts. Finally, our results show that PLGA-aNP may be detected after intracerebral injection in neurons and attenuate PD-related neurodegeneration in vivo by mechanisms involving a rescue of compromised lysosomes.</p></abstract><kwd-group kwd-group-type="author"><title>KEYWORDS</title><kwd>ATP13A2</kwd><kwd>GBA, lysosome; nanoparticles</kwd><kwd>neurodegeneration</kwd><kwd>Parkinson disease</kwd><kwd>XMEA</kwd></kwd-group><counts><fig-count count="7"></fig-count><table-count count="0"></table-count><ref-count count="49"></ref-count><page-count count="12"></page-count></counts></article-meta></front></pmc></record>Pour manipuler ce document sous Unix (Dilib)
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