ParkinsonCanadaV1, PascalFrancis, Corpus, bibRecord, 000598

HO-1-mediated macroautophagy : a mechanism for unregulated iron deposition in aging and degenerating neural tissues

Identifieur interne : 000598 ( PascalFrancis/Corpus ); précédent : 000597; suivant : 000599

HO-1-mediated macroautophagy : a mechanism for unregulated iron deposition in aging and degenerating neural tissues

Auteurs : Hillel Zukor ; WEI SONG ; Adrienne Liberman ; JEANNIE MUI ; Hojatollah Vali ; Carine Fillebeen ; Kostas Pantopoulos ; Ting-Di Wu ; Jean-Luc Guerquin-Kern ; Hyman M. Schipper

Source :

Journal of neurochemistry [ 0022-3042 ] ; 2009.

RBID : Francis:09-0209855

Descripteurs français

Pascal (Inist)
- Fer, Stress oxydatif, Transferrine, Mitochondrie, Maladie de Parkinson, Hème, Encéphale, Dynamique, Pathologie de l'encéphale, Ion, Spectrométrie masse, Démence d'Alzheimer, Technique, Morphologie, Homme.

English descriptors

KwdEn :
- Alzheimer disease, Cerebral disorder, Dynamics, Encephalon, Heme, Human, Ions, Iron, Mass spectrometry, Mitochondria, Morphology, Oxidative stress, Parkinson disease, Technique, Transferrin.

Abstract

Oxidative stress, deposition of non-transferrin iron, and mitochondrial insufficiency occur in the brains of patients with Alzheimer disease (AD) and Parkinson disease (PD). We previously demonstrated that heme oxygenase-1 (HO-1) is up-regulated in AD and PD brain and promotes the accumulation of non-transferrin iron in astroglial mitochondria. Herein, dynamic secondary ion mass spectrometry (SIMS) and other techniques were employed to ascertain (i) the impact of HO-1 over-expression on astroglial mitochondrial morphology in vitro, (ii) the topography of aberrant iron sequestration in astrocytes over-expressing HO-1, and (iii) the role of iron regulatory proteins (IRP) in HO-1-mediated iron deposition. Astroglial hHO-1 over-expression induced cytoplasmic vacuolation, mitochondrial membrane damage, and macroautophagy. HO-1 promoted trapping of redox-active iron and sulfur within many cytopathological profiles without impacting ferroportin, transferrin receptor, ferritin, and IRP2 protein levels or IRP1 activity. Thus, HO-1 activity promotes mitochondrial macroautophagy and sequestration of redox-active iron in astroglia independently of classical iron mobilization pathways. Glial HO-1 may be a rational therapeutic target in AD, PD, and other human CNS conditions characterized by the unregulated deposition of brain iron.

Notice en format standard (ISO 2709)

Pour connaître la documentation sur le format Inist Standard.

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Format Inist (serveur)

NO :	FRANCIS 09-0209855 INIST
ET :	HO-1-mediated macroautophagy : a mechanism for unregulated iron deposition in aging and degenerating neural tissues
AU :	ZUKOR (Hillel); WEI SONG; LIBERMAN (Adrienne); JEANNIE MUI; VALI (Hojatollah); FILLEBEEN (Carine); PANTOPOULOS (Kostas); WU (Ting-Di); GUERQUIN-KERN (Jean-Luc); SCHIPPER (Hyman M.)
AF :	Centre for Neurotranslational Research, Lady Davis Institute for Medical Research, Sir Mortimer B. Davis Jewish General Hospital/Montreal, Quebec/Canada (1 aut., 2 aut., 3 aut., 10 aut.); Department of Neurology and Neurosurgery and Department of Medicine, Division of Geriatrics, McGill University/Montreal, Quebec/Canada (1 aut., 10 aut.); Lady Davis Institute for Medical Research, Sir Mortimer B. Davis Jewish General Hospital/Montreal, Quebec/Canada (1 aut., 2 aut., 3 aut., 6 aut., 7 aut., 10 aut.); Department of Anatomy and Cell Biology, Faculty of Medicine, McGill University/Montreal, Quebec/Canada (4 aut., 5 aut.); Facility for Electron Microscopy Research, McGill University/Montreal, Quebec/Canada (4 aut., 5 aut.); Faculty of Dentistry, McGill University/Montreal, Quebec/Canada (5 aut.); Department of Microbiology and Immunology and Division of Experimental Medicine, McGill University/Montreal, Quebec/Canada (7 aut.); INSERM, U759/Orsay/France (8 aut., 9 aut.); Institut Curie, Laboratoire de Microscopic Ionique/Orsay/France (8 aut., 9 aut.)
DT :	Publication en série; Niveau analytique
SO :	Journal of neurochemistry; ISSN 0022-3042; Coden JONRA9; Royaume-Uni; Da. 2009; Vol. 109; No. 3; Pp. 776-791; Bibl. 2 p.1/4
LA :	Anglais
EA :	Oxidative stress, deposition of non-transferrin iron, and mitochondrial insufficiency occur in the brains of patients with Alzheimer disease (AD) and Parkinson disease (PD). We previously demonstrated that heme oxygenase-1 (HO-1) is up-regulated in AD and PD brain and promotes the accumulation of non-transferrin iron in astroglial mitochondria. Herein, dynamic secondary ion mass spectrometry (SIMS) and other techniques were employed to ascertain (i) the impact of HO-1 over-expression on astroglial mitochondrial morphology in vitro, (ii) the topography of aberrant iron sequestration in astrocytes over-expressing HO-1, and (iii) the role of iron regulatory proteins (IRP) in HO-1-mediated iron deposition. Astroglial hHO-1 over-expression induced cytoplasmic vacuolation, mitochondrial membrane damage, and macroautophagy. HO-1 promoted trapping of redox-active iron and sulfur within many cytopathological profiles without impacting ferroportin, transferrin receptor, ferritin, and IRP2 protein levels or IRP1 activity. Thus, HO-1 activity promotes mitochondrial macroautophagy and sequestration of redox-active iron in astroglia independently of classical iron mobilization pathways. Glial HO-1 may be a rational therapeutic target in AD, PD, and other human CNS conditions characterized by the unregulated deposition of brain iron.
CC :	770D03M
FD :	Fer; Stress oxydatif; Transferrine; Mitochondrie; Maladie de Parkinson; Hème; Encéphale; Dynamique; Pathologie de l'encéphale; Ion; Spectrométrie masse; Démence d'Alzheimer; Technique; Morphologie; Homme
FG :	Pathologie du système nerveux central; Pathologie du système nerveux; Maladie dégénérative; Syndrome extrapyramidal; Névroglie; Système nerveux central
ED :	Iron; Oxidative stress; Transferrin; Mitochondria; Parkinson disease; Heme; Encephalon; Dynamics; Cerebral disorder; Ions; Mass spectrometry; Alzheimer disease; Technique; Morphology; Human
EG :	Central nervous system disease; Nervous system diseases; Degenerative disease; Extrapyramidal syndrome; Neuroglia; Central nervous system
SD :	Hierro; Estrés oxidativo; Transferrina; Mitocondria; Parkinson enfermedad; Heme; Encéfalo; Dinámica; Encéfalo patología; Ión; Espectrometría masa; Demencia Alzheimer; Técnica; Morfología; Hombre
LO :	INIST-4037.354000186050310090
ID :	09-0209855

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Francis:09-0209855

Le document en format XML

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<sZ>1 aut.</sZ>
<sZ>2 aut.</sZ>
<sZ>3 aut.</sZ>
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<s2>Montreal, Quebec</s2>
<s3>CAN</s3>
<sZ>1 aut.</sZ>
<sZ>10 aut.</sZ>
</inist:fA14>
</affiliation>
<affiliation><inist:fA14 i1="03"><s1>Lady Davis Institute for Medical Research, Sir Mortimer B. Davis Jewish General Hospital</s1>
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</author>
<author><name sortKey="Wei Song" sort="Wei Song" uniqKey="Wei Song" last="Wei Song">WEI SONG</name>
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<s2>Montreal, Quebec</s2>
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<sZ>1 aut.</sZ>
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<sZ>1 aut.</sZ>
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<sZ>1 aut.</sZ>
<sZ>2 aut.</sZ>
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<s2>Montreal, Quebec</s2>
<s3>CAN</s3>
<sZ>4 aut.</sZ>
<sZ>5 aut.</sZ>
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<affiliation><inist:fA14 i1="05"><s1>Facility for Electron Microscopy Research, McGill University</s1>
<s2>Montreal, Quebec</s2>
<s3>CAN</s3>
<sZ>4 aut.</sZ>
<sZ>5 aut.</sZ>
</inist:fA14>
</affiliation>
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<author><name sortKey="Vali, Hojatollah" sort="Vali, Hojatollah" uniqKey="Vali H" first="Hojatollah" last="Vali">Hojatollah Vali</name>
<affiliation><inist:fA14 i1="04"><s1>Department of Anatomy and Cell Biology, Faculty of Medicine, McGill University</s1>
<s2>Montreal, Quebec</s2>
<s3>CAN</s3>
<sZ>4 aut.</sZ>
<sZ>5 aut.</sZ>
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</affiliation>
<affiliation><inist:fA14 i1="05"><s1>Facility for Electron Microscopy Research, McGill University</s1>
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<s3>CAN</s3>
<sZ>4 aut.</sZ>
<sZ>5 aut.</sZ>
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<sZ>5 aut.</sZ>
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<s2>Montreal, Quebec</s2>
<s3>CAN</s3>
<sZ>1 aut.</sZ>
<sZ>2 aut.</sZ>
<sZ>3 aut.</sZ>
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<affiliation><inist:fA14 i1="07"><s1>Department of Microbiology and Immunology and Division of Experimental Medicine, McGill University</s1>
<s2>Montreal, Quebec</s2>
<s3>CAN</s3>
<sZ>7 aut.</sZ>
</inist:fA14>
</affiliation>
</author>
<author><name sortKey="Wu, Ting Di" sort="Wu, Ting Di" uniqKey="Wu T" first="Ting-Di" last="Wu">Ting-Di Wu</name>
<affiliation><inist:fA14 i1="08"><s1>INSERM, U759</s1>
<s2>Orsay</s2>
<s3>FRA</s3>
<sZ>8 aut.</sZ>
<sZ>9 aut.</sZ>
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<affiliation><inist:fA14 i1="09"><s1>Institut Curie, Laboratoire de Microscopic Ionique</s1>
<s2>Orsay</s2>
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<sZ>8 aut.</sZ>
<sZ>9 aut.</sZ>
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<author><name sortKey="Guerquin Kern, Jean Luc" sort="Guerquin Kern, Jean Luc" uniqKey="Guerquin Kern J" first="Jean-Luc" last="Guerquin-Kern">Jean-Luc Guerquin-Kern</name>
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<s3>FRA</s3>
<sZ>8 aut.</sZ>
<sZ>9 aut.</sZ>
</inist:fA14>
</affiliation>
<affiliation><inist:fA14 i1="09"><s1>Institut Curie, Laboratoire de Microscopic Ionique</s1>
<s2>Orsay</s2>
<s3>FRA</s3>
<sZ>8 aut.</sZ>
<sZ>9 aut.</sZ>
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</affiliation>
</author>
<author><name sortKey="Schipper, Hyman M" sort="Schipper, Hyman M" uniqKey="Schipper H" first="Hyman M." last="Schipper">Hyman M. Schipper</name>
<affiliation><inist:fA14 i1="01"><s1>Centre for Neurotranslational Research, Lady Davis Institute for Medical Research, Sir Mortimer B. Davis Jewish General Hospital</s1>
<s2>Montreal, Quebec</s2>
<s3>CAN</s3>
<sZ>1 aut.</sZ>
<sZ>2 aut.</sZ>
<sZ>3 aut.</sZ>
<sZ>10 aut.</sZ>
</inist:fA14>
</affiliation>
<affiliation><inist:fA14 i1="02"><s1>Department of Neurology and Neurosurgery and Department of Medicine, Division of Geriatrics, McGill University</s1>
<s2>Montreal, Quebec</s2>
<s3>CAN</s3>
<sZ>1 aut.</sZ>
<sZ>10 aut.</sZ>
</inist:fA14>
</affiliation>
<affiliation><inist:fA14 i1="03"><s1>Lady Davis Institute for Medical Research, Sir Mortimer B. Davis Jewish General Hospital</s1>
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<sZ>1 aut.</sZ>
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<series><title level="j" type="main">Journal of neurochemistry</title>
<title level="j" type="abbreviated">J. neurochem.</title>
<idno type="ISSN">0022-3042</idno>
<imprint><date when="2009">2009</date>
</imprint>
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<seriesStmt><title level="j" type="main">Journal of neurochemistry</title>
<title level="j" type="abbreviated">J. neurochem.</title>
<idno type="ISSN">0022-3042</idno>
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</fileDesc>
<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Alzheimer disease</term>
<term>Cerebral disorder</term>
<term>Dynamics</term>
<term>Encephalon</term>
<term>Heme</term>
<term>Human</term>
<term>Ions</term>
<term>Iron</term>
<term>Mass spectrometry</term>
<term>Mitochondria</term>
<term>Morphology</term>
<term>Oxidative stress</term>
<term>Parkinson disease</term>
<term>Technique</term>
<term>Transferrin</term>
</keywords>
<keywords scheme="Pascal" xml:lang="fr"><term>Fer</term>
<term>Stress oxydatif</term>
<term>Transferrine</term>
<term>Mitochondrie</term>
<term>Maladie de Parkinson</term>
<term>Hème</term>
<term>Encéphale</term>
<term>Dynamique</term>
<term>Pathologie de l'encéphale</term>
<term>Ion</term>
<term>Spectrométrie masse</term>
<term>Démence d'Alzheimer</term>
<term>Technique</term>
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<front><div type="abstract" xml:lang="en">Oxidative stress, deposition of non-transferrin iron, and mitochondrial insufficiency occur in the brains of patients with Alzheimer disease (AD) and Parkinson disease (PD). We previously demonstrated that heme oxygenase-1 (HO-1) is up-regulated in AD and PD brain and promotes the accumulation of non-transferrin iron in astroglial mitochondria. Herein, dynamic secondary ion mass spectrometry (SIMS) and other techniques were employed to ascertain (i) the impact of HO-1 over-expression on astroglial mitochondrial morphology in vitro, (ii) the topography of aberrant iron sequestration in astrocytes over-expressing HO-1, and (iii) the role of iron regulatory proteins (IRP) in HO-1-mediated iron deposition. Astroglial hHO-1 over-expression induced cytoplasmic vacuolation, mitochondrial membrane damage, and macroautophagy. HO-1 promoted trapping of redox-active iron and sulfur within many cytopathological profiles without impacting ferroportin, transferrin receptor, ferritin, and IRP2 protein levels or IRP1 activity. Thus, HO-1 activity promotes mitochondrial macroautophagy and sequestration of redox-active iron in astroglia independently of classical iron mobilization pathways. Glial HO-1 may be a rational therapeutic target in AD, PD, and other human CNS conditions characterized by the unregulated deposition of brain iron.</div>
</front>
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<fA14 i1="02"><s1>Department of Neurology and Neurosurgery and Department of Medicine, Division of Geriatrics, McGill University</s1>
<s2>Montreal, Quebec</s2>
<s3>CAN</s3>
<sZ>1 aut.</sZ>
<sZ>10 aut.</sZ>
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<fA14 i1="03"><s1>Lady Davis Institute for Medical Research, Sir Mortimer B. Davis Jewish General Hospital</s1>
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<fA14 i1="04"><s1>Department of Anatomy and Cell Biology, Faculty of Medicine, McGill University</s1>
<s2>Montreal, Quebec</s2>
<s3>CAN</s3>
<sZ>4 aut.</sZ>
<sZ>5 aut.</sZ>
</fA14>
<fA14 i1="05"><s1>Facility for Electron Microscopy Research, McGill University</s1>
<s2>Montreal, Quebec</s2>
<s3>CAN</s3>
<sZ>4 aut.</sZ>
<sZ>5 aut.</sZ>
</fA14>
<fA14 i1="06"><s1>Faculty of Dentistry, McGill University</s1>
<s2>Montreal, Quebec</s2>
<s3>CAN</s3>
<sZ>5 aut.</sZ>
</fA14>
<fA14 i1="07"><s1>Department of Microbiology and Immunology and Division of Experimental Medicine, McGill University</s1>
<s2>Montreal, Quebec</s2>
<s3>CAN</s3>
<sZ>7 aut.</sZ>
</fA14>
<fA14 i1="08"><s1>INSERM, U759</s1>
<s2>Orsay</s2>
<s3>FRA</s3>
<sZ>8 aut.</sZ>
<sZ>9 aut.</sZ>
</fA14>
<fA14 i1="09"><s1>Institut Curie, Laboratoire de Microscopic Ionique</s1>
<s2>Orsay</s2>
<s3>FRA</s3>
<sZ>8 aut.</sZ>
<sZ>9 aut.</sZ>
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<fC01 i1="01" l="ENG"><s0>Oxidative stress, deposition of non-transferrin iron, and mitochondrial insufficiency occur in the brains of patients with Alzheimer disease (AD) and Parkinson disease (PD). We previously demonstrated that heme oxygenase-1 (HO-1) is up-regulated in AD and PD brain and promotes the accumulation of non-transferrin iron in astroglial mitochondria. Herein, dynamic secondary ion mass spectrometry (SIMS) and other techniques were employed to ascertain (i) the impact of HO-1 over-expression on astroglial mitochondrial morphology in vitro, (ii) the topography of aberrant iron sequestration in astrocytes over-expressing HO-1, and (iii) the role of iron regulatory proteins (IRP) in HO-1-mediated iron deposition. Astroglial hHO-1 over-expression induced cytoplasmic vacuolation, mitochondrial membrane damage, and macroautophagy. HO-1 promoted trapping of redox-active iron and sulfur within many cytopathological profiles without impacting ferroportin, transferrin receptor, ferritin, and IRP2 protein levels or IRP1 activity. Thus, HO-1 activity promotes mitochondrial macroautophagy and sequestration of redox-active iron in astroglia independently of classical iron mobilization pathways. Glial HO-1 may be a rational therapeutic target in AD, PD, and other human CNS conditions characterized by the unregulated deposition of brain iron.</s0>
</fC01>
<fC02 i1="01" i2="X"><s0>770D03M</s0>
<s1>IV</s1>
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<fC03 i1="01" i2="X" l="FRE"><s0>Fer</s0>
<s2>NC</s2>
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</fC03>
<fC03 i1="01" i2="X" l="ENG"><s0>Iron</s0>
<s2>NC</s2>
<s5>01</s5>
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<fC03 i1="02" i2="X" l="FRE"><s0>Stress oxydatif</s0>
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<s5>02</s5>
</fC03>
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<s5>03</s5>
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<fC03 i1="03" i2="X" l="ENG"><s0>Transferrin</s0>
<s5>03</s5>
</fC03>
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<s5>03</s5>
</fC03>
<fC03 i1="04" i2="X" l="FRE"><s0>Mitochondrie</s0>
<s5>04</s5>
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<fC03 i1="04" i2="X" l="ENG"><s0>Mitochondria</s0>
<s5>04</s5>
</fC03>
<fC03 i1="04" i2="X" l="SPA"><s0>Mitocondria</s0>
<s5>04</s5>
</fC03>
<fC03 i1="05" i2="X" l="FRE"><s0>Maladie de Parkinson</s0>
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<s5>05</s5>
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<fC03 i1="05" i2="X" l="ENG"><s0>Parkinson disease</s0>
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<s5>05</s5>
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<fC03 i1="05" i2="X" l="SPA"><s0>Parkinson enfermedad</s0>
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<s5>06</s5>
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<s5>06</s5>
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<s5>06</s5>
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<fC03 i1="07" i2="X" l="FRE"><s0>Encéphale</s0>
<s5>07</s5>
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<s5>07</s5>
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<fC03 i1="08" i2="X" l="FRE"><s0>Dynamique</s0>
<s5>08</s5>
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<s5>08</s5>
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<s5>09</s5>
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<s5>10</s5>
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<fC03 i1="10" i2="X" l="SPA"><s0>Ión</s0>
<s2>NA</s2>
<s5>10</s5>
</fC03>
<fC03 i1="11" i2="X" l="FRE"><s0>Spectrométrie masse</s0>
<s5>11</s5>
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<s5>11</s5>
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<s5>11</s5>
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<s5>12</s5>
</fC03>
<fC03 i1="12" i2="X" l="ENG"><s0>Alzheimer disease</s0>
<s5>12</s5>
</fC03>
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<s5>12</s5>
</fC03>
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<s5>13</s5>
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<s5>13</s5>
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<fC03 i1="13" i2="X" l="SPA"><s0>Técnica</s0>
<s5>13</s5>
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<s5>14</s5>
</fC03>
<fC03 i1="14" i2="X" l="ENG"><s0>Morphology</s0>
<s5>14</s5>
</fC03>
<fC03 i1="14" i2="X" l="SPA"><s0>Morfología</s0>
<s5>14</s5>
</fC03>
<fC03 i1="15" i2="X" l="FRE"><s0>Homme</s0>
<s5>54</s5>
</fC03>
<fC03 i1="15" i2="X" l="ENG"><s0>Human</s0>
<s5>54</s5>
</fC03>
<fC03 i1="15" i2="X" l="SPA"><s0>Hombre</s0>
<s5>54</s5>
</fC03>
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<s5>20</s5>
</fC07>
<fC07 i1="01" i2="X" l="ENG"><s0>Central nervous system disease</s0>
<s5>20</s5>
</fC07>
<fC07 i1="01" i2="X" l="SPA"><s0>Sistema nervosio central patología</s0>
<s5>20</s5>
</fC07>
<fC07 i1="02" i2="X" l="FRE"><s0>Pathologie du   système nerveux</s0>
<s5>21</s5>
</fC07>
<fC07 i1="02" i2="X" l="ENG"><s0>Nervous system diseases</s0>
<s5>21</s5>
</fC07>
<fC07 i1="02" i2="X" l="SPA"><s0>Sistema nervioso patología</s0>
<s5>21</s5>
</fC07>
<fC07 i1="03" i2="X" l="FRE"><s0>Maladie dégénérative</s0>
<s5>22</s5>
</fC07>
<fC07 i1="03" i2="X" l="ENG"><s0>Degenerative disease</s0>
<s5>22</s5>
</fC07>
<fC07 i1="03" i2="X" l="SPA"><s0>Enfermedad degenerativa</s0>
<s5>22</s5>
</fC07>
<fC07 i1="04" i2="X" l="FRE"><s0>Syndrome extrapyramidal</s0>
<s5>23</s5>
</fC07>
<fC07 i1="04" i2="X" l="ENG"><s0>Extrapyramidal syndrome</s0>
<s5>23</s5>
</fC07>
<fC07 i1="04" i2="X" l="SPA"><s0>Extrapiramidal síndrome</s0>
<s5>23</s5>
</fC07>
<fC07 i1="05" i2="X" l="FRE"><s0>Névroglie</s0>
<s5>24</s5>
</fC07>
<fC07 i1="05" i2="X" l="ENG"><s0>Neuroglia</s0>
<s5>24</s5>
</fC07>
<fC07 i1="05" i2="X" l="SPA"><s0>Neuroglia</s0>
<s5>24</s5>
</fC07>
<fC07 i1="06" i2="X" l="FRE"><s0>Système nerveux central</s0>
<s5>25</s5>
</fC07>
<fC07 i1="06" i2="X" l="ENG"><s0>Central nervous system</s0>
<s5>25</s5>
</fC07>
<fC07 i1="06" i2="X" l="SPA"><s0>Sistema nervioso central</s0>
<s5>25</s5>
</fC07>
<fN21><s1>152</s1>
</fN21>
<fN44 i1="01"><s1>OTO</s1>
</fN44>
<fN82><s1>OTO</s1>
</fN82>
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<server><NO>FRANCIS 09-0209855 INIST</NO>
<ET>HO-1-mediated macroautophagy : a mechanism for unregulated iron deposition in aging and degenerating neural tissues</ET>
<AU>ZUKOR (Hillel); WEI SONG; LIBERMAN (Adrienne); JEANNIE MUI; VALI (Hojatollah); FILLEBEEN (Carine); PANTOPOULOS (Kostas); WU (Ting-Di); GUERQUIN-KERN (Jean-Luc); SCHIPPER (Hyman M.)</AU>
<AF>Centre for Neurotranslational Research, Lady Davis Institute for Medical Research, Sir Mortimer B. Davis Jewish General Hospital/Montreal, Quebec/Canada (1 aut., 2 aut., 3 aut., 10 aut.); Department of Neurology and Neurosurgery and Department of Medicine, Division of Geriatrics, McGill University/Montreal, Quebec/Canada (1 aut., 10 aut.); Lady Davis Institute for Medical Research, Sir Mortimer B. Davis Jewish General Hospital/Montreal, Quebec/Canada (1 aut., 2 aut., 3 aut., 6 aut., 7 aut., 10 aut.); Department of Anatomy and Cell Biology, Faculty of Medicine, McGill University/Montreal, Quebec/Canada (4 aut., 5 aut.); Facility for Electron Microscopy Research, McGill University/Montreal, Quebec/Canada (4 aut., 5 aut.); Faculty of Dentistry, McGill University/Montreal, Quebec/Canada (5 aut.); Department of Microbiology and Immunology and Division of Experimental Medicine, McGill University/Montreal, Quebec/Canada (7 aut.); INSERM, U759/Orsay/France (8 aut., 9 aut.); Institut Curie, Laboratoire de Microscopic Ionique/Orsay/France (8 aut., 9 aut.)</AF>
<DT>Publication en série; Niveau analytique</DT>
<SO>Journal of neurochemistry; ISSN 0022-3042; Coden JONRA9; Royaume-Uni; Da. 2009; Vol. 109; No. 3; Pp. 776-791; Bibl. 2 p.1/4</SO>
<LA>Anglais</LA>
<EA>Oxidative stress, deposition of non-transferrin iron, and mitochondrial insufficiency occur in the brains of patients with Alzheimer disease (AD) and Parkinson disease (PD). We previously demonstrated that heme oxygenase-1 (HO-1) is up-regulated in AD and PD brain and promotes the accumulation of non-transferrin iron in astroglial mitochondria. Herein, dynamic secondary ion mass spectrometry (SIMS) and other techniques were employed to ascertain (i) the impact of HO-1 over-expression on astroglial mitochondrial morphology in vitro, (ii) the topography of aberrant iron sequestration in astrocytes over-expressing HO-1, and (iii) the role of iron regulatory proteins (IRP) in HO-1-mediated iron deposition. Astroglial hHO-1 over-expression induced cytoplasmic vacuolation, mitochondrial membrane damage, and macroautophagy. HO-1 promoted trapping of redox-active iron and sulfur within many cytopathological profiles without impacting ferroportin, transferrin receptor, ferritin, and IRP2 protein levels or IRP1 activity. Thus, HO-1 activity promotes mitochondrial macroautophagy and sequestration of redox-active iron in astroglia independently of classical iron mobilization pathways. Glial HO-1 may be a rational therapeutic target in AD, PD, and other human CNS conditions characterized by the unregulated deposition of brain iron.</EA>
<CC>770D03M</CC>
<FD>Fer; Stress oxydatif; Transferrine; Mitochondrie; Maladie de Parkinson; Hème; Encéphale; Dynamique; Pathologie de l'encéphale; Ion; Spectrométrie masse; Démence d'Alzheimer; Technique; Morphologie; Homme</FD>
<FG>Pathologie du   système nerveux central; Pathologie du système nerveux; Maladie dégénérative; Syndrome extrapyramidal; Névroglie; Système nerveux central</FG>
<ED>Iron; Oxidative stress; Transferrin; Mitochondria; Parkinson disease; Heme; Encephalon; Dynamics; Cerebral disorder; Ions; Mass spectrometry; Alzheimer disease; Technique; Morphology; Human</ED>
<EG>Central nervous system disease; Nervous system diseases; Degenerative disease; Extrapyramidal syndrome; Neuroglia; Central nervous system</EG>
<SD>Hierro; Estrés oxidativo; Transferrina; Mitocondria; Parkinson enfermedad; Heme; Encéfalo; Dinámica; Encéfalo patología; Ión; Espectrometría masa; Demencia Alzheimer; Técnica; Morfología; Hombre</SD>
<LO>INIST-4037.354000186050310090</LO>
<ID>09-0209855</ID>
</server>
</inist>
</record>

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	La maladie de Parkinson au Canada (serveur d'exploration)
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La maladie de Parkinson au Canada (serveur d'exploration)

HO-1-mediated macroautophagy : a mechanism for unregulated iron deposition in aging and degenerating neural tissues

HO-1-mediated macroautophagy : a mechanism for unregulated iron deposition in aging and degenerating neural tissues

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