Heme oxygenase-1 and neurodegeneration: expanding frontiers of engagement.
Identifieur interne : 000A89 ( Ncbi/Merge ); précédent : 000A88; suivant : 000A90Heme oxygenase-1 and neurodegeneration: expanding frontiers of engagement.
Auteurs : Hyman M. Schipper [Canada] ; Wei Song ; Hillel Zukor ; Jacob R. Hascalovici ; David ZeligmanSource :
- Journal of neurochemistry [ 1471-4159 ] ; 2009.
English descriptors
- KwdEn :
- Animals, Heme Oxygenase-1 (biosynthesis), Heme Oxygenase-1 (genetics), Humans, Nerve Degeneration (enzymology), Nerve Degeneration (genetics), Nerve Degeneration (pathology), Neurodegenerative Diseases (enzymology), Neurodegenerative Diseases (genetics), Neurodegenerative Diseases (pathology), Signal Transduction (genetics).
- MESH :
- chemical , biosynthesis : Heme Oxygenase-1.
- chemical , genetics : Heme Oxygenase-1.
- enzymology : Nerve Degeneration, Neurodegenerative Diseases.
- genetics : Nerve Degeneration, Neurodegenerative Diseases, Signal Transduction.
- pathology : Nerve Degeneration, Neurodegenerative Diseases.
- Animals, Humans.
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-localizes 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.
DOI: 10.1111/j.1471-4159.2009.06160.x
PubMed: 19457088
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Schipper</name><affiliation wicri:level="4"><nlm:affiliation>Centre for Neurotranslational Research, Lady Davis Institute for Medical Research, Jewish General Hospital, Department of Neurology & Neurosurgery, McGill University, Montreal, Quebec, Canada. hyman.schipper@mcgill.ca</nlm:affiliation><country xml:lang="fr">Canada</country><wicri:regionArea>Centre for Neurotranslational Research, Lady Davis Institute for Medical Research, Jewish General Hospital, Department of Neurology & Neurosurgery, McGill University, Montreal, Quebec</wicri:regionArea><orgName type="university">Université McGill</orgName><placeName><settlement type="city">Montréal</settlement><region type="state">Québec</region></placeName></affiliation></author><author><name sortKey="Song, Wei" sort="Song, Wei" uniqKey="Song W" first="Wei" last="Song">Wei Song</name></author><author><name sortKey="Zukor, Hillel" sort="Zukor, Hillel" uniqKey="Zukor H" first="Hillel" last="Zukor">Hillel Zukor</name></author><author><name sortKey="Hascalovici, Jacob R" sort="Hascalovici, Jacob R" uniqKey="Hascalovici J" first="Jacob R" last="Hascalovici">Jacob R. Hascalovici</name></author><author><name sortKey="Zeligman, David" sort="Zeligman, David" uniqKey="Zeligman D" first="David" last="Zeligman">David Zeligman</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2009">2009</date><idno type="RBID">pubmed:19457088</idno><idno type="pmid">19457088</idno><idno type="doi">10.1111/j.1471-4159.2009.06160.x</idno><idno type="wicri:Area/PubMed/Corpus">000E64</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">000E64</idno><idno type="wicri:Area/PubMed/Curation">000E64</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Curation">000E64</idno><idno type="wicri:Area/PubMed/Checkpoint">000E64</idno><idno type="wicri:explorRef" wicri:stream="Checkpoint" wicri:step="PubMed">000E64</idno><idno type="wicri:Area/Ncbi/Merge">000A89</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Heme oxygenase-1 and neurodegeneration: expanding frontiers of engagement.</title><author><name sortKey="Schipper, Hyman M" sort="Schipper, Hyman M" uniqKey="Schipper H" first="Hyman M" last="Schipper">Hyman M. Schipper</name><affiliation wicri:level="4"><nlm:affiliation>Centre for Neurotranslational Research, Lady Davis Institute for Medical Research, Jewish General Hospital, Department of Neurology & Neurosurgery, McGill University, Montreal, Quebec, Canada. hyman.schipper@mcgill.ca</nlm:affiliation><country xml:lang="fr">Canada</country><wicri:regionArea>Centre for Neurotranslational Research, Lady Davis Institute for Medical Research, Jewish General Hospital, Department of Neurology & Neurosurgery, McGill University, Montreal, Quebec</wicri:regionArea><orgName type="university">Université McGill</orgName><placeName><settlement type="city">Montréal</settlement><region type="state">Québec</region></placeName></affiliation></author><author><name sortKey="Song, Wei" sort="Song, Wei" uniqKey="Song W" first="Wei" last="Song">Wei Song</name></author><author><name sortKey="Zukor, Hillel" sort="Zukor, Hillel" uniqKey="Zukor H" first="Hillel" last="Zukor">Hillel Zukor</name></author><author><name sortKey="Hascalovici, Jacob R" sort="Hascalovici, Jacob R" uniqKey="Hascalovici J" first="Jacob R" last="Hascalovici">Jacob R. Hascalovici</name></author><author><name sortKey="Zeligman, David" sort="Zeligman, David" uniqKey="Zeligman D" first="David" last="Zeligman">David Zeligman</name></author></analytic><series><title level="j">Journal of neurochemistry</title><idno type="eISSN">1471-4159</idno><imprint><date when="2009" type="published">2009</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Animals</term><term>Heme Oxygenase-1 (biosynthesis)</term><term>Heme Oxygenase-1 (genetics)</term><term>Humans</term><term>Nerve Degeneration (enzymology)</term><term>Nerve Degeneration (genetics)</term><term>Nerve Degeneration (pathology)</term><term>Neurodegenerative Diseases (enzymology)</term><term>Neurodegenerative Diseases (genetics)</term><term>Neurodegenerative Diseases (pathology)</term><term>Signal Transduction (genetics)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="biosynthesis" xml:lang="en"><term>Heme Oxygenase-1</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Heme Oxygenase-1</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Nerve Degeneration</term><term>Neurodegenerative Diseases</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Nerve Degeneration</term><term>Neurodegenerative Diseases</term><term>Signal Transduction</term></keywords><keywords scheme="MESH" qualifier="pathology" xml:lang="en"><term>Nerve Degeneration</term><term>Neurodegenerative Diseases</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Humans</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-localizes 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><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">19457088</PMID><DateCreated><Year>2009</Year><Month>07</Month><Day>08</Day></DateCreated><DateCompleted><Year>2009</Year><Month>07</Month><Day>31</Day></DateCompleted><DateRevised><Year>2016</Year><Month>11</Month><Day>25</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1471-4159</ISSN><JournalIssue CitedMedium="Internet"><Volume>110</Volume><Issue>2</Issue><PubDate><Year>2009</Year><Month>Jul</Month></PubDate></JournalIssue><Title>Journal of neurochemistry</Title><ISOAbbreviation>J. Neurochem.</ISOAbbreviation></Journal><ArticleTitle>Heme oxygenase-1 and neurodegeneration: expanding frontiers of engagement.</ArticleTitle><Pagination><MedlinePgn>469-85</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1111/j.1471-4159.2009.06160.x</ELocationID><Abstract><AbstractText>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-localizes 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.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Schipper</LastName><ForeName>Hyman M</ForeName><Initials>HM</Initials><AffiliationInfo><Affiliation>Centre for Neurotranslational Research, Lady Davis Institute for Medical Research, Jewish General Hospital, Department of Neurology & Neurosurgery, McGill University, Montreal, Quebec, Canada. hyman.schipper@mcgill.ca</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Song</LastName><ForeName>Wei</ForeName><Initials>W</Initials></Author><Author ValidYN="Y"><LastName>Zukor</LastName><ForeName>Hillel</ForeName><Initials>H</Initials></Author><Author ValidYN="Y"><LastName>Hascalovici</LastName><ForeName>Jacob R</ForeName><Initials>JR</Initials></Author><Author ValidYN="Y"><LastName>Zeligman</LastName><ForeName>David</ForeName><Initials>D</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType><PublicationType UI="D016454">Review</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2009</Year><Month>05</Month><Day>11</Day></ArticleDate></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>J Neurochem</MedlineTA><NlmUniqueID>2985190R</NlmUniqueID><ISSNLinking>0022-3042</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>EC 1.14.14.18</RegistryNumber><NameOfSubstance UI="D051547">Heme Oxygenase-1</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D051547" MajorTopicYN="N">Heme Oxygenase-1</DescriptorName><QualifierName UI="Q000096" MajorTopicYN="Y">biosynthesis</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D009410" MajorTopicYN="N">Nerve Degeneration</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000473" MajorTopicYN="N">pathology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D019636" MajorTopicYN="N">Neurodegenerative Diseases</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000473" MajorTopicYN="N">pathology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D015398" MajorTopicYN="N">Signal Transduction</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading></MeshHeadingList><NumberOfReferences>187</NumberOfReferences></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="entrez"><Year>2009</Year><Month>5</Month><Day>22</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2009</Year><Month>5</Month><Day>22</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2009</Year><Month>8</Month><Day>1</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">19457088</ArticleId><ArticleId IdType="pii">JNC6160</ArticleId><ArticleId IdType="doi">10.1111/j.1471-4159.2009.06160.x</ArticleId></ArticleIdList></PubmedData></pubmed><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><noCountry><name sortKey="Hascalovici, Jacob R" sort="Hascalovici, Jacob R" uniqKey="Hascalovici J" first="Jacob R" last="Hascalovici">Jacob R. Hascalovici</name><name sortKey="Song, Wei" sort="Song, Wei" uniqKey="Song W" first="Wei" last="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></noCountry><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></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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