Mitochondrial iron sequestration in dopamine-challenged astroglia : Role of heme oxygenase-1 and the permeability transition pore
Identifieur interne : 000D59 ( PascalFrancis/Corpus ); précédent : 000D58; suivant : 000D60Mitochondrial iron sequestration in dopamine-challenged astroglia : Role of heme oxygenase-1 and the permeability transition pore
Auteurs : H. M. Schipper ; L. Bernier ; K. Mehindate ; D. FrankelSource :
- Journal of neurochemistry [ 0022-3042 ] ; 1999.
Descripteurs français
- Pascal (Inist)
English descriptors
- KwdEn :
Abstract
Little is currently known concerning the mechanisms responsible for the excessive deposition of redox-active iron in the substantia nigra of subjects with Parkinson's disease (PD). In the present study, we demonstrate that dopamine promotes the selective sequestration of non-transferrin-derived iron by the mitochondrial compartment of cultured rat astroglia and that the mechanism underlying this novel dopamine effect is oxidative in nature. We also provide evidence that up-regulation of the stress protein heme oxygenase-1 (HO-1) is both necessary and sufficient for mitochondrial iron trapping in dopamine-challenged astroglia. Finally, we show that opening of the mitochondrial transition pore (MTP) mediates the influx of non-transferrin-derived iron into mitochondria of dopamine-stimulated and HO-1-transfected astroglia. Our findings provide an explanation for the pathological iron sequestration, mitochondrial insufficiency, and amplification of oxidative injury reported in the brains of PD subjects. Pharmacological blockade of transition metal trapping by "stressed" astroglial mitochondria (e.g., using HO-1 inhibitors or modulators of the MTP) may afford effective neuroprotection in patients with PD and other neurological afflictions.
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Format Inist (serveur)
NO : | PASCAL 99-0315872 INIST |
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ET : | Mitochondrial iron sequestration in dopamine-challenged astroglia : Role of heme oxygenase-1 and the permeability transition pore |
AU : | SCHIPPER (H. M.); BERNIER (L.); MEHINDATE (K.); FRANKEL (D.) |
AF : | Bloomfield Centre for Research in Aging, Lady Davis Institute for Medical Research, Sir Mortimer B. Davis-Jewish General Hospital/Montreal, Quebec/Canada (1 aut., 2 aut., 3 aut., 4 aut.); Departments of Neurology and Neurosurgery and Medicine (Geriatrics), McGill University/Montreal, Quebec/Canada (1 aut., 4 aut.) |
DT : | Publication en série; Niveau analytique |
SO : | Journal of neurochemistry; ISSN 0022-3042; Coden JONRA9; Etats-Unis; Da. 1999; Vol. 72; No. 5; Pp. 1802-1811; Bibl. 1 p.1/4 |
LA : | Anglais |
EA : | Little is currently known concerning the mechanisms responsible for the excessive deposition of redox-active iron in the substantia nigra of subjects with Parkinson's disease (PD). In the present study, we demonstrate that dopamine promotes the selective sequestration of non-transferrin-derived iron by the mitochondrial compartment of cultured rat astroglia and that the mechanism underlying this novel dopamine effect is oxidative in nature. We also provide evidence that up-regulation of the stress protein heme oxygenase-1 (HO-1) is both necessary and sufficient for mitochondrial iron trapping in dopamine-challenged astroglia. Finally, we show that opening of the mitochondrial transition pore (MTP) mediates the influx of non-transferrin-derived iron into mitochondria of dopamine-stimulated and HO-1-transfected astroglia. Our findings provide an explanation for the pathological iron sequestration, mitochondrial insufficiency, and amplification of oxidative injury reported in the brains of PD subjects. Pharmacological blockade of transition metal trapping by "stressed" astroglial mitochondria (e.g., using HO-1 inhibitors or modulators of the MTP) may afford effective neuroprotection in patients with PD and other neurological afflictions. |
CC : | 002B17G |
FD : | Fer; Dopamine; Heme oxygenase (decyclizing); Astrocyte; Perméabilité; Mitochondrie; Parkinson maladie; Rat; Stress oxydatif; In vitro |
FG : | Oxidoreductases; Enzyme; Neurotransmetteur; Catécholamine; Névroglie; Système nerveux pathologie; Système nerveux central pathologie; Encéphale pathologie; Extrapyramidal syndrome; Maladie dégénérative; Rodentia; Mammalia; Vertebrata |
ED : | Iron; Dopamine; Heme oxygenase (decyclizing); Astrocyte; Permeability; Mitochondria; Parkinson disease; Rat; Oxidative stress; In vitro |
EG : | Oxidoreductases; Enzyme; Neurotransmitter; Catecholamine; Neuroglia; Nervous system diseases; Central nervous system disease; Cerebral disorder; Extrapyramidal syndrome; Degenerative disease; Rodentia; Mammalia; Vertebrata |
SD : | Hierro; Dopamina; Heme oxygenase (decyclizing); Astrocito; Permeabilidad; Mitocondria; Parkinson enfermedad; Rata; Stress oxidativo; In vitro |
LO : | INIST-4037.354000083535430030 |
ID : | 99-0315872 |
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Pascal:99-0315872Le document en format XML
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<front><div type="abstract" xml:lang="en">Little is currently known concerning the mechanisms responsible for the excessive deposition of redox-active iron in the substantia nigra of subjects with Parkinson's disease (PD). In the present study, we demonstrate that dopamine promotes the selective sequestration of non-transferrin-derived iron by the mitochondrial compartment of cultured rat astroglia and that the mechanism underlying this novel dopamine effect is oxidative in nature. We also provide evidence that up-regulation of the stress protein heme oxygenase-1 (HO-1) is both necessary and sufficient for mitochondrial iron trapping in dopamine-challenged astroglia. Finally, we show that opening of the mitochondrial transition pore (MTP) mediates the influx of non-transferrin-derived iron into mitochondria of dopamine-stimulated and HO-1-transfected astroglia. Our findings provide an explanation for the pathological iron sequestration, mitochondrial insufficiency, and amplification of oxidative injury reported in the brains of PD subjects. Pharmacological blockade of transition metal trapping by "stressed" astroglial mitochondria (e.g., using HO-1 inhibitors or modulators of the MTP) may afford effective neuroprotection in patients with PD and other neurological afflictions.</div>
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<s5>40</s5>
</fC07>
<fC07 i1="08" i2="X" l="ENG"><s0>Cerebral disorder</s0>
<s5>40</s5>
</fC07>
<fC07 i1="08" i2="X" l="SPA"><s0>Encéfalo patología</s0>
<s5>40</s5>
</fC07>
<fC07 i1="09" i2="X" l="FRE"><s0>Extrapyramidal syndrome</s0>
<s5>41</s5>
</fC07>
<fC07 i1="09" i2="X" l="ENG"><s0>Extrapyramidal syndrome</s0>
<s5>41</s5>
</fC07>
<fC07 i1="09" i2="X" l="SPA"><s0>Extrapiramidal síndrome</s0>
<s5>41</s5>
</fC07>
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<s5>42</s5>
</fC07>
<fC07 i1="10" i2="X" l="ENG"><s0>Degenerative disease</s0>
<s5>42</s5>
</fC07>
<fC07 i1="10" i2="X" l="SPA"><s0>Enfermedad degenerativa</s0>
<s5>42</s5>
</fC07>
<fC07 i1="11" i2="X" l="FRE"><s0>Rodentia</s0>
<s2>NS</s2>
</fC07>
<fC07 i1="11" i2="X" l="ENG"><s0>Rodentia</s0>
<s2>NS</s2>
</fC07>
<fC07 i1="11" i2="X" l="SPA"><s0>Rodentia</s0>
<s2>NS</s2>
</fC07>
<fC07 i1="12" i2="X" l="FRE"><s0>Mammalia</s0>
<s2>NS</s2>
</fC07>
<fC07 i1="12" i2="X" l="ENG"><s0>Mammalia</s0>
<s2>NS</s2>
</fC07>
<fC07 i1="12" i2="X" l="SPA"><s0>Mammalia</s0>
<s2>NS</s2>
</fC07>
<fC07 i1="13" i2="X" l="FRE"><s0>Vertebrata</s0>
<s2>NS</s2>
</fC07>
<fC07 i1="13" i2="X" l="ENG"><s0>Vertebrata</s0>
<s2>NS</s2>
</fC07>
<fC07 i1="13" i2="X" l="SPA"><s0>Vertebrata</s0>
<s2>NS</s2>
</fC07>
<fN21><s1>200</s1>
</fN21>
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<server><NO>PASCAL 99-0315872 INIST</NO>
<ET>Mitochondrial iron sequestration in dopamine-challenged astroglia : Role of heme oxygenase-1 and the permeability transition pore</ET>
<AU>SCHIPPER (H. M.); BERNIER (L.); MEHINDATE (K.); FRANKEL (D.)</AU>
<AF>Bloomfield Centre for Research in Aging, Lady Davis Institute for Medical Research, Sir Mortimer B. Davis-Jewish General Hospital/Montreal, Quebec/Canada (1 aut., 2 aut., 3 aut., 4 aut.); Departments of Neurology and Neurosurgery and Medicine (Geriatrics), McGill University/Montreal, Quebec/Canada (1 aut., 4 aut.)</AF>
<DT>Publication en série; Niveau analytique</DT>
<SO>Journal of neurochemistry; ISSN 0022-3042; Coden JONRA9; Etats-Unis; Da. 1999; Vol. 72; No. 5; Pp. 1802-1811; Bibl. 1 p.1/4</SO>
<LA>Anglais</LA>
<EA>Little is currently known concerning the mechanisms responsible for the excessive deposition of redox-active iron in the substantia nigra of subjects with Parkinson's disease (PD). In the present study, we demonstrate that dopamine promotes the selective sequestration of non-transferrin-derived iron by the mitochondrial compartment of cultured rat astroglia and that the mechanism underlying this novel dopamine effect is oxidative in nature. We also provide evidence that up-regulation of the stress protein heme oxygenase-1 (HO-1) is both necessary and sufficient for mitochondrial iron trapping in dopamine-challenged astroglia. Finally, we show that opening of the mitochondrial transition pore (MTP) mediates the influx of non-transferrin-derived iron into mitochondria of dopamine-stimulated and HO-1-transfected astroglia. Our findings provide an explanation for the pathological iron sequestration, mitochondrial insufficiency, and amplification of oxidative injury reported in the brains of PD subjects. Pharmacological blockade of transition metal trapping by "stressed" astroglial mitochondria (e.g., using HO-1 inhibitors or modulators of the MTP) may afford effective neuroprotection in patients with PD and other neurological afflictions.</EA>
<CC>002B17G</CC>
<FD>Fer; Dopamine; Heme oxygenase (decyclizing); Astrocyte; Perméabilité; Mitochondrie; Parkinson maladie; Rat; Stress oxydatif; In vitro</FD>
<FG>Oxidoreductases; Enzyme; Neurotransmetteur; Catécholamine; Névroglie; Système nerveux pathologie; Système nerveux central pathologie; Encéphale pathologie; Extrapyramidal syndrome; Maladie dégénérative; Rodentia; Mammalia; Vertebrata</FG>
<ED>Iron; Dopamine; Heme oxygenase (decyclizing); Astrocyte; Permeability; Mitochondria; Parkinson disease; Rat; Oxidative stress; In vitro</ED>
<EG>Oxidoreductases; Enzyme; Neurotransmitter; Catecholamine; Neuroglia; Nervous system diseases; Central nervous system disease; Cerebral disorder; Extrapyramidal syndrome; Degenerative disease; Rodentia; Mammalia; Vertebrata</EG>
<SD>Hierro; Dopamina; Heme oxygenase (decyclizing); Astrocito; Permeabilidad; Mitocondria; Parkinson enfermedad; Rata; Stress oxidativo; In vitro</SD>
<LO>INIST-4037.354000083535430030</LO>
<ID>99-0315872</ID>
</server>
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