Heme oxygenase-1 and neurodegeneration: expanding frontiers of engagement
Identifieur interne : 002098 ( Main/Exploration ); précédent : 002097; suivant : 002099Heme oxygenase-1 and neurodegeneration: expanding frontiers of engagement
Auteurs : Hyman M. Schipper [Canada] ; WEI SONG [Canada] ; Hillel Zukor [Canada] ; Jacob R. Hascalovici [Canada] ; David Zeligman [Canada]Source :
- Journal of neurochemistry [ 0022-3042 ] ; 2009.
Descripteurs français
- Pascal (Inist)
- Wicri :
English descriptors
- KwdEn :
Abstract
The heme oxygenases (HOs), responsible for the degradation of heme to biliverdin/bilirubin, free iron and CO, have been heavily implicated in mammalian CNS aging and disease. In normal brain, the expression of HO-2 is constitutive, abundant and fairly ubiquitous, whereas HO-1 mRNA and protein are confined to small populations of scattered neurons and neuroglia. In contradistinction to HO-2, the ho-1 gene (Hmox1) is exquisitely sensitive to induction by a wide range of pro-oxidant and other stressors. In Alzheimer disease and mild cognitive impairment, immunoreactive HO-1 protein is over-expressed in neurons and astrocytes of the cerebral cortex and hippocampus relative to age-matched, cognitively intact controls and co-Iocalizes to senile plaques, neurofibrillary tangles, and corpora amylacea. In Parkinson disease, HO-1 is markedly over-expressed in astrocytes of the substantia nigra and decorates Lewy bodies in affected dopaminergic neurons. HMOX1 is also up-regulated in glial cells surrounding human cerebral infarcts, hemorrhages and contusions, within multiple sclerosis plaques, and in other degenerative and inflammatory human CNS disorders. Heme-derived free ferrous iron, CO, and biliverdin/bilirubin are biologically active substances that have been shown to either ameliorate or exacerbate neural injury contingent upon specific disease models employed, the intensity and duration of HO-1 expression and the nature of the prevailing redox microenvironment. In 'stressed' astroglia, HO-1 hyperactivity promotes mitochondrial sequestration of non-transferrin iron and macroautophagy and may thereby contribute to the pathological iron deposition and bioenergetic failure amply documented in Alzheimer disease, Parkinson disease and other aging-related neurodegenerative disorders. Glial HO-1 expression may also impact cell survival and neuroplasticity in these conditions by modulating brain sterol metabolism and proteosomal degradation of neurotoxic protein aggregates.
Affiliations:
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Schipper</name><affiliation wicri:level="4"><inist:fA14 i1="01"><s1>Centre for Neurotranslational Research, Lady Davis Institute for Medical Research, Jewish General Hospital, Department of Neurology & Neurosurgery, McGill University</s1><s2>Montreal, Quebec</s2><s3>CAN</s3><sZ>1 aut.</sZ><sZ>2 aut.</sZ><sZ>3 aut.</sZ><sZ>4 aut.</sZ><sZ>5 aut.</sZ></inist:fA14><country>Canada</country><placeName><settlement type="city">Montréal</settlement><region type="state">Québec</region></placeName><orgName type="university">Université McGill</orgName></affiliation></author><author><name sortKey="Wei Song" sort="Wei Song" uniqKey="Wei Song" last="Wei Song">WEI SONG</name><affiliation wicri:level="4"><inist:fA14 i1="01"><s1>Centre for Neurotranslational Research, Lady Davis Institute for Medical Research, Jewish General Hospital, Department of Neurology & Neurosurgery, McGill University</s1><s2>Montreal, Quebec</s2><s3>CAN</s3><sZ>1 aut.</sZ><sZ>2 aut.</sZ><sZ>3 aut.</sZ><sZ>4 aut.</sZ><sZ>5 aut.</sZ></inist:fA14><country>Canada</country><placeName><settlement type="city">Montréal</settlement><region type="state">Québec</region></placeName><orgName type="university">Université McGill</orgName></affiliation></author><author><name sortKey="Zukor, Hillel" sort="Zukor, Hillel" uniqKey="Zukor H" first="Hillel" last="Zukor">Hillel Zukor</name><affiliation wicri:level="4"><inist:fA14 i1="01"><s1>Centre for Neurotranslational Research, Lady Davis Institute for Medical Research, Jewish General Hospital, Department of Neurology & Neurosurgery, McGill University</s1><s2>Montreal, Quebec</s2><s3>CAN</s3><sZ>1 aut.</sZ><sZ>2 aut.</sZ><sZ>3 aut.</sZ><sZ>4 aut.</sZ><sZ>5 aut.</sZ></inist:fA14><country>Canada</country><placeName><settlement type="city">Montréal</settlement><region type="state">Québec</region></placeName><orgName type="university">Université McGill</orgName></affiliation></author><author><name sortKey="Hascalovici, Jacob R" sort="Hascalovici, Jacob R" uniqKey="Hascalovici J" first="Jacob R." last="Hascalovici">Jacob R. Hascalovici</name><affiliation wicri:level="4"><inist:fA14 i1="01"><s1>Centre for Neurotranslational Research, Lady Davis Institute for Medical Research, Jewish General Hospital, Department of Neurology & Neurosurgery, McGill University</s1><s2>Montreal, Quebec</s2><s3>CAN</s3><sZ>1 aut.</sZ><sZ>2 aut.</sZ><sZ>3 aut.</sZ><sZ>4 aut.</sZ><sZ>5 aut.</sZ></inist:fA14><country>Canada</country><placeName><settlement type="city">Montréal</settlement><region type="state">Québec</region></placeName><orgName type="university">Université McGill</orgName></affiliation></author><author><name sortKey="Zeligman, David" sort="Zeligman, David" uniqKey="Zeligman D" first="David" last="Zeligman">David Zeligman</name><affiliation wicri:level="4"><inist:fA14 i1="01"><s1>Centre for Neurotranslational Research, Lady Davis Institute for Medical Research, Jewish General Hospital, Department of Neurology & Neurosurgery, McGill University</s1><s2>Montreal, Quebec</s2><s3>CAN</s3><sZ>1 aut.</sZ><sZ>2 aut.</sZ><sZ>3 aut.</sZ><sZ>4 aut.</sZ><sZ>5 aut.</sZ></inist:fA14><country>Canada</country><placeName><settlement type="city">Montréal</settlement><region type="state">Québec</region></placeName><orgName type="university">Université McGill</orgName></affiliation></author></analytic><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></series></biblStruct></sourceDesc><seriesStmt><title level="j" type="main">Journal of neurochemistry</title><title level="j" type="abbreviated">J. neurochem.</title><idno type="ISSN">0022-3042</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Alzheimer disease</term><term>Astrocyte</term><term>Central nervous system</term><term>Cognitive disorder</term><term>Dopaminergic neuron</term><term>Encephalon</term><term>Gene</term><term>Heme</term><term>Human</term><term>Induction</term><term>Iron</term><term>Oxidant</term><term>Oxidative stress</term><term>Protein</term><term>mild cognitive impairment</term></keywords><keywords scheme="Pascal" xml:lang="fr"><term>Hème</term><term>Fer</term><term>Système nerveux central</term><term>Encéphale</term><term>Protéine</term><term>Neurone dopaminergique</term><term>Gène</term><term>Induction</term><term>Démence d'Alzheimer</term><term>Oxydant</term><term>Stress oxydatif</term><term>Déficit cognitif léger</term><term>Trouble cognitif</term><term>Astrocyte</term><term>Homme</term></keywords><keywords scheme="Wicri" type="topic" xml:lang="fr"><term>Fer</term><term>Homme</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The heme oxygenases (HOs), responsible for the degradation of heme to biliverdin/bilirubin, free iron and CO, have been heavily implicated in mammalian CNS aging and disease. In normal brain, the expression of HO-2 is constitutive, abundant and fairly ubiquitous, whereas HO-1 mRNA and protein are confined to small populations of scattered neurons and neuroglia. In contradistinction to HO-2, the ho-1 gene (Hmox1) is exquisitely sensitive to induction by a wide range of pro-oxidant and other stressors. In Alzheimer disease and mild cognitive impairment, immunoreactive HO-1 protein is over-expressed in neurons and astrocytes of the cerebral cortex and hippocampus relative to age-matched, cognitively intact controls and co-Iocalizes to senile plaques, neurofibrillary tangles, and corpora amylacea. In Parkinson disease, HO-1 is markedly over-expressed in astrocytes of the substantia nigra and decorates Lewy bodies in affected dopaminergic neurons. HMOX1 is also up-regulated in glial cells surrounding human cerebral infarcts, hemorrhages and contusions, within multiple sclerosis plaques, and in other degenerative and inflammatory human CNS disorders. Heme-derived free ferrous iron, CO, and biliverdin/bilirubin are biologically active substances that have been shown to either ameliorate or exacerbate neural injury contingent upon specific disease models employed, the intensity and duration of HO-1 expression and the nature of the prevailing redox microenvironment. In 'stressed' astroglia, HO-1 hyperactivity promotes mitochondrial sequestration of non-transferrin iron and macroautophagy and may thereby contribute to the pathological iron deposition and bioenergetic failure amply documented in Alzheimer disease, Parkinson disease and other aging-related neurodegenerative disorders. Glial HO-1 expression may also impact cell survival and neuroplasticity in these conditions by modulating brain sterol metabolism and proteosomal degradation of neurotoxic protein aggregates.</div></front></TEI><affiliations><list><country><li>Canada</li></country><region><li>Québec</li></region><settlement><li>Montréal</li></settlement><orgName><li>Université McGill</li></orgName></list><tree><country name="Canada"><region name="Québec"><name sortKey="Schipper, Hyman M" sort="Schipper, Hyman M" uniqKey="Schipper H" first="Hyman M." last="Schipper">Hyman M. Schipper</name></region><name sortKey="Hascalovici, Jacob R" sort="Hascalovici, Jacob R" uniqKey="Hascalovici J" first="Jacob R." last="Hascalovici">Jacob R. Hascalovici</name><name sortKey="Wei Song" sort="Wei Song" uniqKey="Wei Song" last="Wei Song">WEI SONG</name><name sortKey="Zeligman, David" sort="Zeligman, David" uniqKey="Zeligman D" first="David" last="Zeligman">David Zeligman</name><name sortKey="Zukor, Hillel" sort="Zukor, Hillel" uniqKey="Zukor H" first="Hillel" last="Zukor">Hillel Zukor</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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