Is Bax a mitochondrial mediator in apoptotic death of dopaminergic neurons in Parkinson's disease?
Identifieur interne : 001256 ( PubMed/Corpus ); précédent : 001255; suivant : 001257Is Bax a mitochondrial mediator in apoptotic death of dopaminergic neurons in Parkinson's disease?
Auteurs : A. Hartmann ; P P Michel ; J D Troadec ; A. Mouatt-Prigent ; B A Faucheux ; M. Ruberg ; Y. Agid ; E C HirschSource :
- Journal of neurochemistry [ 0022-3042 ] ; 2001.
English descriptors
- KwdEn :
- 1-Methyl-4-phenylpyridinium (pharmacology), Adult, Aged, Animals, Apoptosis (physiology), Brain (metabolism), Brain (pathology), Cells, Cultured, Dopamine (metabolism), Embryo, Mammalian, Humans, Intracellular Membranes (drug effects), Intracellular Membranes (metabolism), Lewy Bodies (metabolism), Lewy Bodies (pathology), Mesencephalon (cytology), Mesencephalon (metabolism), Mitochondria (metabolism), Neurons (drug effects), Neurons (metabolism), Neurons (pathology), Parkinson Disease (metabolism), Parkinson Disease (pathology), Proto-Oncogene Proteins (metabolism), Proto-Oncogene Proteins c-bcl-2, Rats, Rats, Wistar, Reference Values, Substantia Nigra (metabolism), Substantia Nigra (pathology), Tyrosine 3-Monooxygenase (metabolism), bcl-2-Associated X Protein.
- MESH :
- chemical , metabolism : Dopamine, Proto-Oncogene Proteins, Tyrosine 3-Monooxygenase.
- chemical , pharmacology : 1-Methyl-4-phenylpyridinium.
- cytology : Mesencephalon.
- drug effects : Intracellular Membranes, Neurons.
- metabolism : Brain, Intracellular Membranes, Lewy Bodies, Mesencephalon, Mitochondria, Neurons, Parkinson Disease, Substantia Nigra.
- pathology : Brain, Lewy Bodies, Neurons, Parkinson Disease, Substantia Nigra.
- physiology : Apoptosis.
- Adult, Aged, Animals, Cells, Cultured, Embryo, Mammalian, Humans, Proto-Oncogene Proteins c-bcl-2, Rats, Rats, Wistar, Reference Values, bcl-2-Associated X Protein.
Abstract
Bax is a proapoptotic member of the Bcl-2 family of proteins. It is believed to exert its action primarily by facilitating the release of cytochrome c from the mitochondrial intermembrane space into the cytosol, leading to caspase activation and cell death. Because alterations in mitochondrial respiratory function, caspase activation and cell death with morphologic features compatible with apoptosis have been observed post mortem in the brain of patients with Parkinson's disease, we tried to clarify the potential role of Bax in this process in an immunohistochemical study on normal and Parkinson's disease post-mortem brain and primary mesencephalic cell cultures treated with MPP(+). We found that Bax is expressed ubiquitously by dopaminergic (DA) neurons in post-mortem brain of normal and Parkinson's disease subjects as well as in vitro. Using an antibody to Bax inserted into the outer mitochondrial membrane as an index of Bax activation, no significant differences were observed between control and Parkinson's disease subjects, regardless of the mesencephalic subregion analysed. However, in Parkinson's disease subjects, the percentage of Bax-positive melanized SNpc neurons containing Lewy bodies, suggestive of DA neuronal suffering, was significantly higher than the overall percentage of Bax-positive neurons among melanized neurons. Furthermore, all melanized SNpc neurons in Parkinson's disease subjects with activated caspase-3 were also immunoreactive for Bax, suggesting that Bax anchored in the outer mitochondrial membrane of melanized SNpc neurons showing signs of neuronal suffering or apoptosis is increased compared with DA neurons that are apparently unaltered. Surprisingly, MPP(+) treatment of tyrosine hydroxylase (TH)-positive neurons in primary mesencephalic cultures did not cause redistribution of Bax, although cytochrome c was released from the mitochondria and nuclear condensation/fragmentation was induced. Taken together, these findings suggest that in the human pathology, Bax may be a cofactor in caspase activation, but our in vitro data fail to indicate a central role for Bax in apoptotic death of DA neurons in an experimental Parkinson's disease paradigm.
PubMed: 11259496
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Mouatt-Prigent</name></author><author><name sortKey="Faucheux, B A" sort="Faucheux, B A" uniqKey="Faucheux B" first="B A" last="Faucheux">B A Faucheux</name></author><author><name sortKey="Ruberg, M" sort="Ruberg, M" uniqKey="Ruberg M" first="M" last="Ruberg">M. Ruberg</name></author><author><name sortKey="Agid, Y" sort="Agid, Y" uniqKey="Agid Y" first="Y" last="Agid">Y. Agid</name></author><author><name sortKey="Hirsch, E C" sort="Hirsch, E C" uniqKey="Hirsch E" first="E C" last="Hirsch">E C Hirsch</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2001">2001</date><idno type="RBID">pubmed:11259496</idno><idno type="pmid">11259496</idno><idno type="wicri:Area/PubMed/Corpus">001256</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">001256</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Is Bax a mitochondrial mediator in apoptotic death of dopaminergic neurons in Parkinson's disease?</title><author><name sortKey="Hartmann, A" sort="Hartmann, A" uniqKey="Hartmann A" first="A" last="Hartmann">A. Hartmann</name><affiliation><nlm:affiliation>INSERM U289, Hôpital de la Salpêtrière, Paris, France.</nlm:affiliation></affiliation></author><author><name sortKey="Michel, P P" sort="Michel, P P" uniqKey="Michel P" first="P P" last="Michel">P P Michel</name></author><author><name sortKey="Troadec, J D" sort="Troadec, J D" uniqKey="Troadec J" first="J D" last="Troadec">J D Troadec</name></author><author><name sortKey="Mouatt Prigent, A" sort="Mouatt Prigent, A" uniqKey="Mouatt Prigent A" first="A" last="Mouatt-Prigent">A. Mouatt-Prigent</name></author><author><name sortKey="Faucheux, B A" sort="Faucheux, B A" uniqKey="Faucheux B" first="B A" last="Faucheux">B A Faucheux</name></author><author><name sortKey="Ruberg, M" sort="Ruberg, M" uniqKey="Ruberg M" first="M" last="Ruberg">M. Ruberg</name></author><author><name sortKey="Agid, Y" sort="Agid, Y" uniqKey="Agid Y" first="Y" last="Agid">Y. Agid</name></author><author><name sortKey="Hirsch, E C" sort="Hirsch, E C" uniqKey="Hirsch E" first="E C" last="Hirsch">E C Hirsch</name></author></analytic><series><title level="j">Journal of neurochemistry</title><idno type="ISSN">0022-3042</idno><imprint><date when="2001" type="published">2001</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>1-Methyl-4-phenylpyridinium (pharmacology)</term><term>Adult</term><term>Aged</term><term>Animals</term><term>Apoptosis (physiology)</term><term>Brain (metabolism)</term><term>Brain (pathology)</term><term>Cells, Cultured</term><term>Dopamine (metabolism)</term><term>Embryo, Mammalian</term><term>Humans</term><term>Intracellular Membranes (drug effects)</term><term>Intracellular Membranes (metabolism)</term><term>Lewy Bodies (metabolism)</term><term>Lewy Bodies (pathology)</term><term>Mesencephalon (cytology)</term><term>Mesencephalon (metabolism)</term><term>Mitochondria (metabolism)</term><term>Neurons (drug effects)</term><term>Neurons (metabolism)</term><term>Neurons (pathology)</term><term>Parkinson Disease (metabolism)</term><term>Parkinson Disease (pathology)</term><term>Proto-Oncogene Proteins (metabolism)</term><term>Proto-Oncogene Proteins c-bcl-2</term><term>Rats</term><term>Rats, Wistar</term><term>Reference Values</term><term>Substantia Nigra (metabolism)</term><term>Substantia Nigra (pathology)</term><term>Tyrosine 3-Monooxygenase (metabolism)</term><term>bcl-2-Associated X Protein</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Dopamine</term><term>Proto-Oncogene Proteins</term><term>Tyrosine 3-Monooxygenase</term></keywords><keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>1-Methyl-4-phenylpyridinium</term></keywords><keywords scheme="MESH" qualifier="cytology" xml:lang="en"><term>Mesencephalon</term></keywords><keywords scheme="MESH" qualifier="drug effects" xml:lang="en"><term>Intracellular Membranes</term><term>Neurons</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Brain</term><term>Intracellular Membranes</term><term>Lewy Bodies</term><term>Mesencephalon</term><term>Mitochondria</term><term>Neurons</term><term>Parkinson Disease</term><term>Substantia Nigra</term></keywords><keywords scheme="MESH" qualifier="pathology" xml:lang="en"><term>Brain</term><term>Lewy Bodies</term><term>Neurons</term><term>Parkinson Disease</term><term>Substantia Nigra</term></keywords><keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>Apoptosis</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Adult</term><term>Aged</term><term>Animals</term><term>Cells, Cultured</term><term>Embryo, Mammalian</term><term>Humans</term><term>Proto-Oncogene Proteins c-bcl-2</term><term>Rats</term><term>Rats, Wistar</term><term>Reference Values</term><term>bcl-2-Associated X Protein</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Bax is a proapoptotic member of the Bcl-2 family of proteins. It is believed to exert its action primarily by facilitating the release of cytochrome c from the mitochondrial intermembrane space into the cytosol, leading to caspase activation and cell death. Because alterations in mitochondrial respiratory function, caspase activation and cell death with morphologic features compatible with apoptosis have been observed post mortem in the brain of patients with Parkinson's disease, we tried to clarify the potential role of Bax in this process in an immunohistochemical study on normal and Parkinson's disease post-mortem brain and primary mesencephalic cell cultures treated with MPP(+). We found that Bax is expressed ubiquitously by dopaminergic (DA) neurons in post-mortem brain of normal and Parkinson's disease subjects as well as in vitro. Using an antibody to Bax inserted into the outer mitochondrial membrane as an index of Bax activation, no significant differences were observed between control and Parkinson's disease subjects, regardless of the mesencephalic subregion analysed. However, in Parkinson's disease subjects, the percentage of Bax-positive melanized SNpc neurons containing Lewy bodies, suggestive of DA neuronal suffering, was significantly higher than the overall percentage of Bax-positive neurons among melanized neurons. Furthermore, all melanized SNpc neurons in Parkinson's disease subjects with activated caspase-3 were also immunoreactive for Bax, suggesting that Bax anchored in the outer mitochondrial membrane of melanized SNpc neurons showing signs of neuronal suffering or apoptosis is increased compared with DA neurons that are apparently unaltered. Surprisingly, MPP(+) treatment of tyrosine hydroxylase (TH)-positive neurons in primary mesencephalic cultures did not cause redistribution of Bax, although cytochrome c was released from the mitochondria and nuclear condensation/fragmentation was induced. Taken together, these findings suggest that in the human pathology, Bax may be a cofactor in caspase activation, but our in vitro data fail to indicate a central role for Bax in apoptotic death of DA neurons in an experimental Parkinson's disease paradigm.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">11259496</PMID><DateCreated><Year>2001</Year><Month>03</Month><Day>22</Day></DateCreated><DateCompleted><Year>2001</Year><Month>04</Month><Day>12</Day></DateCompleted><DateRevised><Year>2013</Year><Month>11</Month><Day>21</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0022-3042</ISSN><JournalIssue CitedMedium="Print"><Volume>76</Volume><Issue>6</Issue><PubDate><Year>2001</Year><Month>Mar</Month></PubDate></JournalIssue><Title>Journal of neurochemistry</Title><ISOAbbreviation>J. Neurochem.</ISOAbbreviation></Journal><ArticleTitle>Is Bax a mitochondrial mediator in apoptotic death of dopaminergic neurons in Parkinson's disease?</ArticleTitle><Pagination><MedlinePgn>1785-93</MedlinePgn></Pagination><Abstract><AbstractText>Bax is a proapoptotic member of the Bcl-2 family of proteins. It is believed to exert its action primarily by facilitating the release of cytochrome c from the mitochondrial intermembrane space into the cytosol, leading to caspase activation and cell death. Because alterations in mitochondrial respiratory function, caspase activation and cell death with morphologic features compatible with apoptosis have been observed post mortem in the brain of patients with Parkinson's disease, we tried to clarify the potential role of Bax in this process in an immunohistochemical study on normal and Parkinson's disease post-mortem brain and primary mesencephalic cell cultures treated with MPP(+). We found that Bax is expressed ubiquitously by dopaminergic (DA) neurons in post-mortem brain of normal and Parkinson's disease subjects as well as in vitro. Using an antibody to Bax inserted into the outer mitochondrial membrane as an index of Bax activation, no significant differences were observed between control and Parkinson's disease subjects, regardless of the mesencephalic subregion analysed. However, in Parkinson's disease subjects, the percentage of Bax-positive melanized SNpc neurons containing Lewy bodies, suggestive of DA neuronal suffering, was significantly higher than the overall percentage of Bax-positive neurons among melanized neurons. Furthermore, all melanized SNpc neurons in Parkinson's disease subjects with activated caspase-3 were also immunoreactive for Bax, suggesting that Bax anchored in the outer mitochondrial membrane of melanized SNpc neurons showing signs of neuronal suffering or apoptosis is increased compared with DA neurons that are apparently unaltered. Surprisingly, MPP(+) treatment of tyrosine hydroxylase (TH)-positive neurons in primary mesencephalic cultures did not cause redistribution of Bax, although cytochrome c was released from the mitochondria and nuclear condensation/fragmentation was induced. Taken together, these findings suggest that in the human pathology, Bax may be a cofactor in caspase activation, but our in vitro data fail to indicate a central role for Bax in apoptotic death of DA neurons in an experimental Parkinson's disease paradigm.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Hartmann</LastName><ForeName>A</ForeName><Initials>A</Initials><AffiliationInfo><Affiliation>INSERM U289, Hôpital de la Salpêtrière, Paris, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Michel</LastName><ForeName>P P</ForeName><Initials>PP</Initials></Author><Author ValidYN="Y"><LastName>Troadec</LastName><ForeName>J D</ForeName><Initials>JD</Initials></Author><Author ValidYN="Y"><LastName>Mouatt-Prigent</LastName><ForeName>A</ForeName><Initials>A</Initials></Author><Author ValidYN="Y"><LastName>Faucheux</LastName><ForeName>B A</ForeName><Initials>BA</Initials></Author><Author ValidYN="Y"><LastName>Ruberg</LastName><ForeName>M</ForeName><Initials>M</Initials></Author><Author ValidYN="Y"><LastName>Agid</LastName><ForeName>Y</ForeName><Initials>Y</Initials></Author><Author ValidYN="Y"><LastName>Hirsch</LastName><ForeName>E C</ForeName><Initials>EC</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>J Neurochem</MedlineTA><NlmUniqueID>2985190R</NlmUniqueID><ISSNLinking>0022-3042</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C494826">BAX protein, human</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C494828">Bax protein, 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MajorTopicYN="N">cytology</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008928" MajorTopicYN="N">Mitochondria</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D009474" MajorTopicYN="N">Neurons</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName><QualifierName UI="Q000473" MajorTopicYN="N">pathology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010300" MajorTopicYN="N">Parkinson Disease</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName><QualifierName UI="Q000473" MajorTopicYN="Y">pathology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011518" MajorTopicYN="N">Proto-Oncogene Proteins</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D019253" MajorTopicYN="Y">Proto-Oncogene Proteins c-bcl-2</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D051381" MajorTopicYN="N">Rats</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D017208" MajorTopicYN="N">Rats, Wistar</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D012016" MajorTopicYN="N">Reference Values</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D013378" MajorTopicYN="N">Substantia Nigra</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName><QualifierName UI="Q000473" MajorTopicYN="N">pathology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D014446" MajorTopicYN="N">Tyrosine 3-Monooxygenase</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D051028" MajorTopicYN="N">bcl-2-Associated X Protein</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>2001</Year><Month>3</Month><Day>22</Day><Hour>10</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2001</Year><Month>4</Month><Day>17</Day><Hour>10</Hour><Minute>1</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2001</Year><Month>3</Month><Day>22</Day><Hour>10</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">11259496</ArticleId></ArticleIdList></PubmedData></pubmed></record>Pour manipuler ce document sous Unix (Dilib)
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