Abnormal activity of membrane phospholipid synthetic enzymes in the brain of patients with Friedreich's ataxia and spinocerebellar atrophy type-1.
Identifieur interne : 004062 ( PubMed/Checkpoint ); précédent : 004061; suivant : 004063Abnormal activity of membrane phospholipid synthetic enzymes in the brain of patients with Friedreich's ataxia and spinocerebellar atrophy type-1.
Auteurs : B M Ross [Canada] ; K. Eder ; A. Moszczynska ; N. Mamalias ; J. Lamarche ; L. Ang ; M. Pandolfo ; G. Rouleau ; M. Kirchgessner ; S J KishSource :
- Movement disorders : official journal of the Movement Disorder Society [ 0885-3185 ] ; 2000.
English descriptors
- KwdEn :
- Adult, Brain (enzymology), Brain (pathology), Brain Mapping, Cerebellar Cortex (enzymology), Cerebellar Cortex (pathology), Cerebral Cortex (enzymology), Cerebral Cortex (pathology), Female, Friedreich Ataxia (diagnosis), Friedreich Ataxia (enzymology), Friedreich Ataxia (pathology), Humans, Male, Membrane Lipids (metabolism), Phosphatidylethanolamines (metabolism), Phospholipids (metabolism), Phosphotransferases (Alcohol Group Acceptor) (metabolism), Reference Values, Spinocerebellar Ataxias (diagnosis), Spinocerebellar Ataxias (enzymology), Spinocerebellar Ataxias (pathology).
- MESH :
- chemical , metabolism : Membrane Lipids, Phosphatidylethanolamines, Phospholipids, Phosphotransferases (Alcohol Group Acceptor).
- diagnosis : Friedreich Ataxia, Spinocerebellar Ataxias.
- enzymology : Brain, Cerebellar Cortex, Cerebral Cortex, Friedreich Ataxia, Spinocerebellar Ataxias.
- pathology : Brain, Cerebellar Cortex, Cerebral Cortex, Friedreich Ataxia, Spinocerebellar Ataxias.
- Adult, Brain Mapping, Female, Humans, Male, Reference Values.
Abstract
Much evidence, derived from biochemical studies of both blood and autopsied brain, has suggested that phospholipid metabolism is abnormal in patients with Friedreich's ataxia (FA), a disorder characterized by severe neuronal loss in the spinal cord and lower brain stem with no, or only modest, damage in other brain regions. To establish the cause of our recent finding of reduced brain levels of phospholipids in FA, we assayed activities of 10 phospholipid-metabolizing enzymes in the autopsied cerebellar cortex of patients with the disorder and, for comparison, in a group of patients with spinocerebellar ataxia type 1 (SCA-1), a disease characterized, unlike FA, by marked neuronal loss in the cerebellar cortex. Enzyme activities were also measured in four brain areas which are relatively unaffected morphologically in both FA and SCA-1. We found that ethanolamine kinase activity was increased in multiple brain regions of patients with FA (increased 31%-137%) and, more modestly, in SCA-1 (increased 39%-60%), suggesting a nonspecific enhancement of phosphoethanolamine production in both disorders. In contrast, the activity of phosphoethanolamine cytidylyltransferase (PECT), the rate-limiting enzyme of phosphatidylethanolamine synthesis, was significantly and markedly decreased by 35%-78% in the cerebellar, frontal, and occipital cortices of patients with FA but was normal in SCA-1. Reduced PECT activity in FA may explain the lower brain levels of phosphatidylethanolamine in the disorder. Moreover, because decreased PECT activity in FA occurs in brain regions having no, or only modest, morphologic damage, this may represent a systemic change consequent to the frataxin gene defect. Our data also suggest that therapeutic intervention in FA designed to increase synthesis of membrane phospholipids may warrant further investigation.
PubMed: 10752579
Affiliations:
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Eder</name></author><author><name sortKey="Moszczynska, A" sort="Moszczynska, A" uniqKey="Moszczynska A" first="A" last="Moszczynska">A. Moszczynska</name></author><author><name sortKey="Mamalias, N" sort="Mamalias, N" uniqKey="Mamalias N" first="N" last="Mamalias">N. Mamalias</name></author><author><name sortKey="Lamarche, J" sort="Lamarche, J" uniqKey="Lamarche J" first="J" last="Lamarche">J. Lamarche</name></author><author><name sortKey="Ang, L" sort="Ang, L" uniqKey="Ang L" first="L" last="Ang">L. Ang</name></author><author><name sortKey="Pandolfo, M" sort="Pandolfo, M" uniqKey="Pandolfo M" first="M" last="Pandolfo">M. Pandolfo</name></author><author><name sortKey="Rouleau, G" sort="Rouleau, G" uniqKey="Rouleau G" first="G" last="Rouleau">G. Rouleau</name></author><author><name sortKey="Kirchgessner, M" sort="Kirchgessner, M" uniqKey="Kirchgessner M" first="M" last="Kirchgessner">M. Kirchgessner</name></author><author><name sortKey="Kish, S J" sort="Kish, S J" uniqKey="Kish S" first="S J" last="Kish">S J Kish</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2000">2000</date><idno type="RBID">pubmed:10752579</idno><idno type="pmid">10752579</idno><idno type="wicri:Area/PubMed/Corpus">004023</idno><idno type="wicri:Area/PubMed/Curation">004023</idno><idno type="wicri:Area/PubMed/Checkpoint">004062</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Abnormal activity of membrane phospholipid synthetic enzymes in the brain of patients with Friedreich's ataxia and spinocerebellar atrophy type-1.</title><author><name sortKey="Ross, B M" sort="Ross, B M" uniqKey="Ross B" first="B M" last="Ross">B M Ross</name><affiliation wicri:level="4"><nlm:affiliation>Centre for Addiction and Mental Health, and Department of Psychiatry, University of Toronto, Ontario, Canada.</nlm:affiliation><country xml:lang="fr">Canada</country><wicri:regionArea>Centre for Addiction and Mental Health, and Department of Psychiatry, University of Toronto, Ontario</wicri:regionArea><orgName type="university">Université de Toronto</orgName><placeName><settlement type="city">Toronto</settlement><region type="state">Ontario</region></placeName></affiliation></author><author><name sortKey="Eder, K" sort="Eder, K" uniqKey="Eder K" first="K" last="Eder">K. Eder</name></author><author><name sortKey="Moszczynska, A" sort="Moszczynska, A" uniqKey="Moszczynska A" first="A" last="Moszczynska">A. Moszczynska</name></author><author><name sortKey="Mamalias, N" sort="Mamalias, N" uniqKey="Mamalias N" first="N" last="Mamalias">N. Mamalias</name></author><author><name sortKey="Lamarche, J" sort="Lamarche, J" uniqKey="Lamarche J" first="J" last="Lamarche">J. Lamarche</name></author><author><name sortKey="Ang, L" sort="Ang, L" uniqKey="Ang L" first="L" last="Ang">L. Ang</name></author><author><name sortKey="Pandolfo, M" sort="Pandolfo, M" uniqKey="Pandolfo M" first="M" last="Pandolfo">M. Pandolfo</name></author><author><name sortKey="Rouleau, G" sort="Rouleau, G" uniqKey="Rouleau G" first="G" last="Rouleau">G. Rouleau</name></author><author><name sortKey="Kirchgessner, M" sort="Kirchgessner, M" uniqKey="Kirchgessner M" first="M" last="Kirchgessner">M. Kirchgessner</name></author><author><name sortKey="Kish, S J" sort="Kish, S J" uniqKey="Kish S" first="S J" last="Kish">S J Kish</name></author></analytic><series><title level="j">Movement disorders : official journal of the Movement Disorder Society</title><idno type="ISSN">0885-3185</idno><imprint><date when="2000" type="published">2000</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Adult</term><term>Brain (enzymology)</term><term>Brain (pathology)</term><term>Brain Mapping</term><term>Cerebellar Cortex (enzymology)</term><term>Cerebellar Cortex (pathology)</term><term>Cerebral Cortex (enzymology)</term><term>Cerebral Cortex (pathology)</term><term>Female</term><term>Friedreich Ataxia (diagnosis)</term><term>Friedreich Ataxia (enzymology)</term><term>Friedreich Ataxia (pathology)</term><term>Humans</term><term>Male</term><term>Membrane Lipids (metabolism)</term><term>Phosphatidylethanolamines (metabolism)</term><term>Phospholipids (metabolism)</term><term>Phosphotransferases (Alcohol Group Acceptor) (metabolism)</term><term>Reference Values</term><term>Spinocerebellar Ataxias (diagnosis)</term><term>Spinocerebellar Ataxias (enzymology)</term><term>Spinocerebellar Ataxias (pathology)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Membrane Lipids</term><term>Phosphatidylethanolamines</term><term>Phospholipids</term><term>Phosphotransferases (Alcohol Group Acceptor)</term></keywords><keywords scheme="MESH" qualifier="diagnosis" xml:lang="en"><term>Friedreich Ataxia</term><term>Spinocerebellar Ataxias</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Brain</term><term>Cerebellar Cortex</term><term>Cerebral Cortex</term><term>Friedreich Ataxia</term><term>Spinocerebellar Ataxias</term></keywords><keywords scheme="MESH" qualifier="pathology" xml:lang="en"><term>Brain</term><term>Cerebellar Cortex</term><term>Cerebral Cortex</term><term>Friedreich Ataxia</term><term>Spinocerebellar Ataxias</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Adult</term><term>Brain Mapping</term><term>Female</term><term>Humans</term><term>Male</term><term>Reference Values</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Much evidence, derived from biochemical studies of both blood and autopsied brain, has suggested that phospholipid metabolism is abnormal in patients with Friedreich's ataxia (FA), a disorder characterized by severe neuronal loss in the spinal cord and lower brain stem with no, or only modest, damage in other brain regions. To establish the cause of our recent finding of reduced brain levels of phospholipids in FA, we assayed activities of 10 phospholipid-metabolizing enzymes in the autopsied cerebellar cortex of patients with the disorder and, for comparison, in a group of patients with spinocerebellar ataxia type 1 (SCA-1), a disease characterized, unlike FA, by marked neuronal loss in the cerebellar cortex. Enzyme activities were also measured in four brain areas which are relatively unaffected morphologically in both FA and SCA-1. We found that ethanolamine kinase activity was increased in multiple brain regions of patients with FA (increased 31%-137%) and, more modestly, in SCA-1 (increased 39%-60%), suggesting a nonspecific enhancement of phosphoethanolamine production in both disorders. In contrast, the activity of phosphoethanolamine cytidylyltransferase (PECT), the rate-limiting enzyme of phosphatidylethanolamine synthesis, was significantly and markedly decreased by 35%-78% in the cerebellar, frontal, and occipital cortices of patients with FA but was normal in SCA-1. Reduced PECT activity in FA may explain the lower brain levels of phosphatidylethanolamine in the disorder. Moreover, because decreased PECT activity in FA occurs in brain regions having no, or only modest, morphologic damage, this may represent a systemic change consequent to the frataxin gene defect. Our data also suggest that therapeutic intervention in FA designed to increase synthesis of membrane phospholipids may warrant further investigation.</div></front></TEI><pubmed><MedlineCitation Owner="NLM" Status="MEDLINE"><PMID Version="1">10752579</PMID><DateCreated><Year>2000</Year><Month>06</Month><Day>09</Day></DateCreated><DateCompleted><Year>2000</Year><Month>06</Month><Day>09</Day></DateCompleted><DateRevised><Year>2007</Year><Month>11</Month><Day>14</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0885-3185</ISSN><JournalIssue CitedMedium="Print"><Volume>15</Volume><Issue>2</Issue><PubDate><Year>2000</Year><Month>Mar</Month></PubDate></JournalIssue><Title>Movement disorders : official journal of the Movement Disorder Society</Title><ISOAbbreviation>Mov. Disord.</ISOAbbreviation></Journal><ArticleTitle>Abnormal activity of membrane phospholipid synthetic enzymes in the brain of patients with Friedreich's ataxia and spinocerebellar atrophy type-1.</ArticleTitle><Pagination><MedlinePgn>294-300</MedlinePgn></Pagination><Abstract><AbstractText>Much evidence, derived from biochemical studies of both blood and autopsied brain, has suggested that phospholipid metabolism is abnormal in patients with Friedreich's ataxia (FA), a disorder characterized by severe neuronal loss in the spinal cord and lower brain stem with no, or only modest, damage in other brain regions. To establish the cause of our recent finding of reduced brain levels of phospholipids in FA, we assayed activities of 10 phospholipid-metabolizing enzymes in the autopsied cerebellar cortex of patients with the disorder and, for comparison, in a group of patients with spinocerebellar ataxia type 1 (SCA-1), a disease characterized, unlike FA, by marked neuronal loss in the cerebellar cortex. Enzyme activities were also measured in four brain areas which are relatively unaffected morphologically in both FA and SCA-1. We found that ethanolamine kinase activity was increased in multiple brain regions of patients with FA (increased 31%-137%) and, more modestly, in SCA-1 (increased 39%-60%), suggesting a nonspecific enhancement of phosphoethanolamine production in both disorders. In contrast, the activity of phosphoethanolamine cytidylyltransferase (PECT), the rate-limiting enzyme of phosphatidylethanolamine synthesis, was significantly and markedly decreased by 35%-78% in the cerebellar, frontal, and occipital cortices of patients with FA but was normal in SCA-1. Reduced PECT activity in FA may explain the lower brain levels of phosphatidylethanolamine in the disorder. Moreover, because decreased PECT activity in FA occurs in brain regions having no, or only modest, morphologic damage, this may represent a systemic change consequent to the frataxin gene defect. Our data also suggest that therapeutic intervention in FA designed to increase synthesis of membrane phospholipids may warrant further investigation.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Ross</LastName><ForeName>B M</ForeName><Initials>BM</Initials><AffiliationInfo><Affiliation>Centre for Addiction and Mental Health, and Department of Psychiatry, University of Toronto, Ontario, Canada.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Eder</LastName><ForeName>K</ForeName><Initials>K</Initials></Author><Author ValidYN="Y"><LastName>Moszczynska</LastName><ForeName>A</ForeName><Initials>A</Initials></Author><Author ValidYN="Y"><LastName>Mamalias</LastName><ForeName>N</ForeName><Initials>N</Initials></Author><Author ValidYN="Y"><LastName>Lamarche</LastName><ForeName>J</ForeName><Initials>J</Initials></Author><Author ValidYN="Y"><LastName>Ang</LastName><ForeName>L</ForeName><Initials>L</Initials></Author><Author ValidYN="Y"><LastName>Pandolfo</LastName><ForeName>M</ForeName><Initials>M</Initials></Author><Author ValidYN="Y"><LastName>Rouleau</LastName><ForeName>G</ForeName><Initials>G</Initials></Author><Author ValidYN="Y"><LastName>Kirchgessner</LastName><ForeName>M</ForeName><Initials>M</Initials></Author><Author ValidYN="Y"><LastName>Kish</LastName><ForeName>S J</ForeName><Initials>SJ</Initials></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>26034</GrantID><Agency>PHS HHS</Agency><Country>United States</Country></Grant></GrantList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType><PublicationType UI="D013487">Research Support, U.S. Gov't, P.H.S.</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>UNITED STATES</Country><MedlineTA>Mov Disord</MedlineTA><NlmUniqueID>8610688</NlmUniqueID><ISSNLinking>0885-3185</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D008563">Membrane Lipids</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D010714">Phosphatidylethanolamines</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D010743">Phospholipids</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.7.1.-</RegistryNumber><NameOfSubstance UI="D017853">Phosphotransferases (Alcohol Group Acceptor)</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.7.1.82</RegistryNumber><NameOfSubstance UI="C020125">ethanolamine kinase</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName MajorTopicYN="N" UI="D000328">Adult</DescriptorName></MeshHeading><MeshHeading><DescriptorName MajorTopicYN="N" UI="D001921">Brain</DescriptorName><QualifierName MajorTopicYN="Y" UI="Q000201">enzymology</QualifierName><QualifierName MajorTopicYN="N" UI="Q000473">pathology</QualifierName></MeshHeading><MeshHeading><DescriptorName MajorTopicYN="N" UI="D001931">Brain Mapping</DescriptorName></MeshHeading><MeshHeading><DescriptorName MajorTopicYN="N" UI="D002525">Cerebellar Cortex</DescriptorName><QualifierName MajorTopicYN="N" UI="Q000201">enzymology</QualifierName><QualifierName MajorTopicYN="N" UI="Q000473">pathology</QualifierName></MeshHeading><MeshHeading><DescriptorName MajorTopicYN="N" UI="D002540">Cerebral Cortex</DescriptorName><QualifierName MajorTopicYN="N" UI="Q000201">enzymology</QualifierName><QualifierName MajorTopicYN="N" UI="Q000473">pathology</QualifierName></MeshHeading><MeshHeading><DescriptorName MajorTopicYN="N" UI="D005260">Female</DescriptorName></MeshHeading><MeshHeading><DescriptorName MajorTopicYN="N" UI="D005621">Friedreich Ataxia</DescriptorName><QualifierName MajorTopicYN="N" UI="Q000175">diagnosis</QualifierName><QualifierName MajorTopicYN="Y" UI="Q000201">enzymology</QualifierName><QualifierName MajorTopicYN="N" UI="Q000473">pathology</QualifierName></MeshHeading><MeshHeading><DescriptorName MajorTopicYN="N" UI="D006801">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName MajorTopicYN="N" UI="D008297">Male</DescriptorName></MeshHeading><MeshHeading><DescriptorName MajorTopicYN="N" UI="D008563">Membrane Lipids</DescriptorName><QualifierName MajorTopicYN="Y" UI="Q000378">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName MajorTopicYN="N" UI="D010714">Phosphatidylethanolamines</DescriptorName><QualifierName MajorTopicYN="N" UI="Q000378">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName MajorTopicYN="N" UI="D010743">Phospholipids</DescriptorName><QualifierName MajorTopicYN="Y" UI="Q000378">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName MajorTopicYN="N" UI="D017853">Phosphotransferases (Alcohol Group Acceptor)</DescriptorName><QualifierName MajorTopicYN="Y" UI="Q000378">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName MajorTopicYN="N" UI="D012016">Reference Values</DescriptorName></MeshHeading><MeshHeading><DescriptorName MajorTopicYN="N" UI="D020754">Spinocerebellar Ataxias</DescriptorName><QualifierName MajorTopicYN="N" UI="Q000175">diagnosis</QualifierName><QualifierName MajorTopicYN="Y" UI="Q000201">enzymology</QualifierName><QualifierName MajorTopicYN="N" UI="Q000473">pathology</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>2000</Year><Month>4</Month><Day>7</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2000</Year><Month>6</Month><Day>17</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2000</Year><Month>4</Month><Day>7</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">10752579</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Canada</li></country><region><li>Ontario</li></region><settlement><li>Toronto</li></settlement><orgName><li>Université de Toronto</li></orgName></list><tree><noCountry><name sortKey="Ang, L" sort="Ang, L" uniqKey="Ang L" first="L" last="Ang">L. Ang</name><name sortKey="Eder, K" sort="Eder, K" uniqKey="Eder K" first="K" last="Eder">K. Eder</name><name sortKey="Kirchgessner, M" sort="Kirchgessner, M" uniqKey="Kirchgessner M" first="M" last="Kirchgessner">M. Kirchgessner</name><name sortKey="Kish, S J" sort="Kish, S J" uniqKey="Kish S" first="S J" last="Kish">S J Kish</name><name sortKey="Lamarche, J" sort="Lamarche, J" uniqKey="Lamarche J" first="J" last="Lamarche">J. Lamarche</name><name sortKey="Mamalias, N" sort="Mamalias, N" uniqKey="Mamalias N" first="N" last="Mamalias">N. Mamalias</name><name sortKey="Moszczynska, A" sort="Moszczynska, A" uniqKey="Moszczynska A" first="A" last="Moszczynska">A. Moszczynska</name><name sortKey="Pandolfo, M" sort="Pandolfo, M" uniqKey="Pandolfo M" first="M" last="Pandolfo">M. Pandolfo</name><name sortKey="Rouleau, G" sort="Rouleau, G" uniqKey="Rouleau G" first="G" last="Rouleau">G. Rouleau</name></noCountry><country name="Canada"><region name="Ontario"><name sortKey="Ross, B M" sort="Ross, B M" uniqKey="Ross B" first="B M" last="Ross">B M Ross</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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