A heme oxygenase-1 transducer model of degenerative and developmental brain disorders.
Identifieur interne : 000542 ( PubMed/Curation ); précédent : 000541; suivant : 000543A heme oxygenase-1 transducer model of degenerative and developmental brain disorders.
Auteurs : Hyman M. Schipper [Canada] ; Wei Song [Canada]Source :
- International journal of molecular sciences [ 1422-0067 ] ; 2015.
English descriptors
- KwdEn :
- MESH :
- chemical , genetics : Heme Oxygenase-1.
- genetics : Alzheimer Disease, Parkinson Disease.
- metabolism : Alzheimer Disease, Heme Oxygenase-1, Iron, Parkinson Disease.
- therapy : Alzheimer Disease, Parkinson Disease.
- Animals, Humans, Signal Transduction.
Abstract
Heme oxygenase-1 (HO-1) is a 32 kDa protein which catalyzes the breakdown of heme to free iron, carbon monoxide and biliverdin. The Hmox1 promoter contains numerous consensus sequences that render the gene exquisitely sensitive to induction by diverse pro-oxidant and inflammatory stimuli. In "stressed" astroglia, HO-1 hyperactivity promotes mitochondrial iron sequestration and macroautophagy and may thereby contribute to the pathological iron deposition and bioenergetic failure documented in Alzheimer disease, Parkinson disease and certain neurodevelopmental conditions. Glial HO-1 expression may also impact neuroplasticity and cell survival by modulating brain sterol metabolism and the proteasomal degradation of neurotoxic proteins. The glial HO-1 response may represent a pivotal transducer of noxious environmental and endogenous stressors into patterns of neural damage and repair characteristic of many human degenerative and developmental CNS disorders.
DOI: 10.3390/ijms16035400
PubMed: 25761244
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pubmed:25761244Le document en format XML
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Schipper</name><affiliation wicri:level="1"><nlm:affiliation>Bloomfield Centre for Research in Aging, Lady Davis Institute for Medical Research, Jewish General Hospital, Montreal, QC H3T1E2, Canada. hyman.schipper@mcgill.ca.</nlm:affiliation><country xml:lang="fr">Canada</country><wicri:regionArea>Bloomfield Centre for Research in Aging, Lady Davis Institute for Medical Research, Jewish General Hospital, Montreal, QC H3T1E2</wicri:regionArea></affiliation></author><author><name sortKey="Song, Wei" sort="Song, Wei" uniqKey="Song W" first="Wei" last="Song">Wei Song</name><affiliation wicri:level="1"><nlm:affiliation>Bloomfield Centre for Research in Aging, Lady Davis Institute for Medical Research, Jewish General Hospital, Montreal, QC H3T1E2, Canada. wsong39@yahoo.com.</nlm:affiliation><country xml:lang="fr">Canada</country><wicri:regionArea>Bloomfield Centre for Research in Aging, Lady Davis Institute for Medical Research, Jewish General Hospital, Montreal, QC H3T1E2</wicri:regionArea></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2015">2015</date><idno type="RBID">pubmed:25761244</idno><idno type="pmid">25761244</idno><idno type="doi">10.3390/ijms16035400</idno><idno type="wicri:Area/PubMed/Corpus">000542</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">000542</idno><idno type="wicri:Area/PubMed/Curation">000542</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Curation">000542</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">A heme oxygenase-1 transducer model of degenerative and developmental brain disorders.</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="1"><nlm:affiliation>Bloomfield Centre for Research in Aging, Lady Davis Institute for Medical Research, Jewish General Hospital, Montreal, QC H3T1E2, Canada. hyman.schipper@mcgill.ca.</nlm:affiliation><country xml:lang="fr">Canada</country><wicri:regionArea>Bloomfield Centre for Research in Aging, Lady Davis Institute for Medical Research, Jewish General Hospital, Montreal, QC H3T1E2</wicri:regionArea></affiliation></author><author><name sortKey="Song, Wei" sort="Song, Wei" uniqKey="Song W" first="Wei" last="Song">Wei Song</name><affiliation wicri:level="1"><nlm:affiliation>Bloomfield Centre for Research in Aging, Lady Davis Institute for Medical Research, Jewish General Hospital, Montreal, QC H3T1E2, Canada. wsong39@yahoo.com.</nlm:affiliation><country xml:lang="fr">Canada</country><wicri:regionArea>Bloomfield Centre for Research in Aging, Lady Davis Institute for Medical Research, Jewish General Hospital, Montreal, QC H3T1E2</wicri:regionArea></affiliation></author></analytic><series><title level="j">International journal of molecular sciences</title><idno type="eISSN">1422-0067</idno><imprint><date when="2015" type="published">2015</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Alzheimer Disease (genetics)</term><term>Alzheimer Disease (metabolism)</term><term>Alzheimer Disease (therapy)</term><term>Animals</term><term>Heme Oxygenase-1 (genetics)</term><term>Heme Oxygenase-1 (metabolism)</term><term>Humans</term><term>Iron (metabolism)</term><term>Parkinson Disease (genetics)</term><term>Parkinson Disease (metabolism)</term><term>Parkinson Disease (therapy)</term><term>Signal Transduction</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Heme Oxygenase-1</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Alzheimer Disease</term><term>Parkinson Disease</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Alzheimer Disease</term><term>Heme Oxygenase-1</term><term>Iron</term><term>Parkinson Disease</term></keywords><keywords scheme="MESH" qualifier="therapy" xml:lang="en"><term>Alzheimer Disease</term><term>Parkinson Disease</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Humans</term><term>Signal Transduction</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Heme oxygenase-1 (HO-1) is a 32 kDa protein which catalyzes the breakdown of heme to free iron, carbon monoxide and biliverdin. The Hmox1 promoter contains numerous consensus sequences that render the gene exquisitely sensitive to induction by diverse pro-oxidant and inflammatory stimuli. In "stressed" astroglia, HO-1 hyperactivity promotes mitochondrial iron sequestration and macroautophagy and may thereby contribute to the pathological iron deposition and bioenergetic failure documented in Alzheimer disease, Parkinson disease and certain neurodevelopmental conditions. Glial HO-1 expression may also impact neuroplasticity and cell survival by modulating brain sterol metabolism and the proteasomal degradation of neurotoxic proteins. The glial HO-1 response may represent a pivotal transducer of noxious environmental and endogenous stressors into patterns of neural damage and repair characteristic of many human degenerative and developmental CNS disorders.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">25761244</PMID><DateCreated><Year>2015</Year><Month>03</Month><Day>12</Day></DateCreated><DateCompleted><Year>2015</Year><Month>11</Month><Day>25</Day></DateCompleted><DateRevised><Year>2017</Year><Month>02</Month><Day>20</Day></DateRevised><Article PubModel="Electronic"><Journal><ISSN IssnType="Electronic">1422-0067</ISSN><JournalIssue CitedMedium="Internet"><Volume>16</Volume><Issue>3</Issue><PubDate><Year>2015</Year><Month>Mar</Month><Day>09</Day></PubDate></JournalIssue><Title>International journal of molecular sciences</Title><ISOAbbreviation>Int J Mol Sci</ISOAbbreviation></Journal><ArticleTitle>A heme oxygenase-1 transducer model of degenerative and developmental brain disorders.</ArticleTitle><Pagination><MedlinePgn>5400-19</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.3390/ijms16035400</ELocationID><Abstract><AbstractText>Heme oxygenase-1 (HO-1) is a 32 kDa protein which catalyzes the breakdown of heme to free iron, carbon monoxide and biliverdin. The Hmox1 promoter contains numerous consensus sequences that render the gene exquisitely sensitive to induction by diverse pro-oxidant and inflammatory stimuli. In "stressed" astroglia, HO-1 hyperactivity promotes mitochondrial iron sequestration and macroautophagy and may thereby contribute to the pathological iron deposition and bioenergetic failure documented in Alzheimer disease, Parkinson disease and certain neurodevelopmental conditions. Glial HO-1 expression may also impact neuroplasticity and cell survival by modulating brain sterol metabolism and the proteasomal degradation of neurotoxic proteins. The glial HO-1 response may represent a pivotal transducer of noxious environmental and endogenous stressors into patterns of neural damage and repair characteristic of many human degenerative and developmental CNS disorders.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Schipper</LastName><ForeName>Hyman M</ForeName><Initials>HM</Initials><AffiliationInfo><Affiliation>Bloomfield Centre for Research in Aging, Lady Davis Institute for Medical Research, Jewish General Hospital, Montreal, QC H3T1E2, Canada. hyman.schipper@mcgill.ca.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>Department of Neurology & Neurosurgery and Department of Medicine, McGill University and Jewish General Hospital, Montreal, QC H3T1E2, Canada. hyman.schipper@mcgill.ca.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Song</LastName><ForeName>Wei</ForeName><Initials>W</Initials><AffiliationInfo><Affiliation>Bloomfield Centre for Research in 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Version="1">19360540</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>Biochim Biophys Acta. 1996 Jul 18;1275(1-2):5-9</RefSource><PMID Version="1">8688451</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>J Alzheimers Dis. 2011;26(2):299-313</RefSource><PMID Version="1">21613741</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>J Neurosci. 1991 Jul;11(7):2170-6</RefSource><PMID Version="1">1712380</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>Leg Med (Tokyo). 2003 Mar;5 Suppl 1:S360-6</RefSource><PMID Version="1">12935634</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>J Neurochem. 1998 May;70(5):2057-69</RefSource><PMID Version="1">9572292</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>Mutat Res. 1992 Sep;275(3-6):195-208</RefSource><PMID Version="1">1383761</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>J Neurochem. 1999 Mar;72(3):1187-203</RefSource><PMID Version="1">10037492</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>J Histochem Cytochem. 1992 Dec;40(12):1887-97</RefSource><PMID Version="1">1453006</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>J Cell Physiol. 2006 Mar;206(3):655-63</RefSource><PMID Version="1">16222706</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>Ann Neurol. 1991 Oct;30(4):563-71</RefSource><PMID Version="1">1665052</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>Proc Natl Acad Sci U S A. 2001 Sep 25;98(20):10996-1002</RefSource><PMID Version="1">11572959</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>J Neurochem. 2009 Jul;110(2):469-85</RefSource><PMID Version="1">19457088</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>Brain Res. 2002 Nov 1;954(1):51-9</RefSource><PMID Version="1">12393232</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>Mol Brain. 2009;2:29</RefSource><PMID Version="1">19754977</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>Free Radic Biol Med. 2007 Mar 15;42(6):864-71</RefSource><PMID Version="1">17320768</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>Free Radic Biol Med. 2012 Jun 1-15;52(11-12):2292-301</RefSource><PMID Version="1">22549002</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>Free Radic Res. 2002 Dec;36(12):1307-13</RefSource><PMID Version="1">12607822</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>Exp Neurol. 2014 Apr;254:78-89</RefSource><PMID Version="1">24440642</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>Genomics. 1994 Sep 15;23(2):471-6</RefSource><PMID Version="1">7835898</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>J Neurochem. 2009 Jan;108(1):72-81</RefSource><PMID Version="1">19046352</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>J Cereb Blood Flow Metab. 2007 May;27(5):1010-21</RefSource><PMID Version="1">17047682</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>Cell Mol Biol (Noisy-le-grand). 2000 May;46(3):587-96</RefSource><PMID Version="1">10872745</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>J Biol Chem. 2000 Feb 25;275(8):5395-9</RefSource><PMID Version="1">10681514</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>Exp Gerontol. 2002 Dec;37(12):1389-400</RefSource><PMID Version="1">12559408</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>Clin Schizophr Relat Psychoses. 2010 Jul;4(2):124-37</RefSource><PMID Version="1">20643635</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>J Biol Chem. 2007 Jul 13;282(28):20621-33</RefSource><PMID Version="1">17430897</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>J Neurosci Res. 2007 Aug 1;85(10):2186-95</RefSource><PMID Version="1">17526019</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>Neurotox Res. 1999 Sep;1(1):57-70</RefSource><PMID Version="1">12835114</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>Exp Neurol. 1997 Oct;147(2):221-8</RefSource><PMID Version="1">9344547</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>J Nucl Med. 1994 Jan;35(1):1-6</RefSource><PMID Version="1">8271029</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>Mol Psychiatry. 2004 Jul;9(7):684-97, 643</RefSource><PMID Version="1">15098003</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>J Neurosci Res. 2005 Apr 15;80(2):268-78</RefSource><PMID Version="1">15751016</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>Biochim Biophys Acta. 1993 Oct 3;1158(2):189-93</RefSource><PMID Version="1">8399320</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>Science. 1993 Jan 15;259(5093):381-4</RefSource><PMID Version="1">7678352</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>Neuroscience. 2006 Sep 15;141(4):1703-8</RefSource><PMID Version="1">16828975</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>J Neurosci Res. 1999 Jun 15;56(6):652-8</RefSource><PMID Version="1">10374820</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>Prog Neurobiol. 2011 Jan;93(1):23-58</RefSource><PMID Version="1">20955757</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>Curr Med Chem. 2001 Jun;8(7):721-38</RefSource><PMID Version="1">11375746</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>Neurobiol Aging. 1998 Jan-Feb;19(1 Suppl):S47-51</RefSource><PMID Version="1">9562468</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>J Neuropsychiatry Clin Neurosci. 1992 Winter;4(1):36-41</RefSource><PMID Version="1">1627959</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>J Neurochem. 2009 Jul;110(2):719-33</RefSource><PMID Version="1">19457084</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>Ann Neurol. 2003;53 Suppl 3:S26-36; discussion S36-8</RefSource><PMID Version="1">12666096</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>Free Radic Biol Med. 2000 Jan 15;28(2):289-309</RefSource><PMID Version="1">11281297</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>Ageing Res Rev. 2004 Jul;3(3):265-301</RefSource><PMID Version="1">15231237</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>Ann Neurol. 1997 Jul;42(1):85-94</RefSource><PMID Version="1">9225689</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>J Neurochem. 2000 Jul;75(1):304-13</RefSource><PMID Version="1">10854275</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>J Neurochem. 1999 May;72(5):1802-11</RefSource><PMID Version="1">10217256</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>Philos Trans R Soc Lond B Biol Sci. 1991 Apr 29;332(1262):15-24</RefSource><PMID Version="1">1677205</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>Circ Res. 1985 Jul;57(1):142-51</RefSource><PMID Version="1">2988819</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>Exp Neurol. 1998 Mar;150(1):60-8</RefSource><PMID Version="1">9514830</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>J Neurochem. 2009 Aug;110(4):1241-53</RefSource><PMID Version="1">19522732</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>Glia. 1995 Oct;15(2):203-6</RefSource><PMID Version="1">8567072</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>J Biol Chem. 1993 Oct 15;268(29):21939-45</RefSource><PMID Version="1">8408050</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>Free Radic Biol Med. 2006 Apr 15;40(8):1332-9</RefSource><PMID Version="1">16631523</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>Biochim Biophys Acta. 1999 Feb 9;1410(2):171-82</RefSource><PMID Version="1">10076025</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>J Neurochem. 2012 Oct;123(2):325-36</RefSource><PMID Version="1">22881289</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>J Neurochem. 2001 Jun;77(5):1386-95</RefSource><PMID Version="1">11389189</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>Brain Res. 1996 Oct 14;736(1-2):68-75</RefSource><PMID Version="1">8930310</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>Neuron. 1991 Apr;6(4):487-98</RefSource><PMID Version="1">1673054</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>J Neural Transm (Vienna). 1998;105(8-9):855-70</RefSource><PMID Version="1">9869323</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>AJNR Am J Neuroradiol. 1995 Jan;16(1):61-8</RefSource><PMID Version="1">7900603</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>Neuroscience. 2014 Nov 7;280:40-9</RefSource><PMID Version="1">25218961</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>Brain Res Brain Res Rev. 1999 Apr;29(2-3):265-95</RefSource><PMID Version="1">10209236</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>Glia. 1995 May;14(1):55-64</RefSource><PMID Version="1">7615346</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>Pediatrics. 1993 Mar;91(3):537-9</RefSource><PMID Version="1">8441555</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>Nature. 2007 Jul 5;448(7149):39-43</RefSource><PMID Version="1">17572664</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>Brain Res Brain Res Rev. 1995 Sep;21(2):195-218</RefSource><PMID Version="1">8866675</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>Physiol Rev. 2006 Apr;86(2):583-650</RefSource><PMID Version="1">16601269</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>Neurobiol Dis. 2014 Feb;62:144-59</RefSource><PMID Version="1">24095978</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>Free Radic Biol Med. 2004 Dec 15;37(12):1995-2011</RefSource><PMID Version="1">15544918</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>J Cell Physiol. 2000 Oct;185(1):80-6</RefSource><PMID Version="1">10942521</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>J Neurochem. 2009 May;109(3):776-91</RefSource><PMID Version="1">19250338</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>J Neurosci. 2012 Aug 8;32(32):10841-53</RefSource><PMID Version="1">22875919</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>Science. 1987 Feb 27;235(4792):1043-6</RefSource><PMID Version="1">3029864</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>Semin Perinatol. 2004 Oct;28(5):365-8</RefSource><PMID Version="1">15686268</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>Proc Natl Acad Sci U S A. 2007 Aug 7;104(32):12982-7</RefSource><PMID Version="1">17652171</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>Biochim Biophys Acta. 1994 Aug 11;1223(1):9-14</RefSource><PMID Version="1">8061058</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>Proc Natl Acad Sci U S A. 1999 Mar 2;96(5):2445-50</RefSource><PMID Version="1">10051662</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>J Neurosci. 2001 May 1;21(9):3017-23</RefSource><PMID Version="1">11312286</PMID></CommentsCorrections></CommentsCorrectionsList><MeshHeadingList><MeshHeading><DescriptorName UI="D000544" MajorTopicYN="N">Alzheimer Disease</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName><QualifierName UI="Q000628" MajorTopicYN="N">therapy</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D051547" MajorTopicYN="N">Heme Oxygenase-1</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D007501" MajorTopicYN="N">Iron</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010300" MajorTopicYN="N">Parkinson Disease</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName><QualifierName UI="Q000628" MajorTopicYN="N">therapy</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D015398" MajorTopicYN="Y">Signal Transduction</DescriptorName></MeshHeading></MeshHeadingList><OtherID Source="NLM">PMC4394483</OtherID></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2014</Year><Month>12</Month><Day>11</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2015</Year><Month>01</Month><Day>28</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2015</Year><Month>02</Month><Day>22</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2015</Year><Month>3</Month><Day>12</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2015</Year><Month>3</Month><Day>12</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2015</Year><Month>12</Month><Day>15</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>epublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">25761244</ArticleId><ArticleId IdType="pii">ijms16035400</ArticleId><ArticleId IdType="doi">10.3390/ijms16035400</ArticleId><ArticleId IdType="pmc">PMC4394483</ArticleId></ArticleIdList></PubmedData></pubmed></record>Pour manipuler ce 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