Altered expression of calcium- and apoptosis-regulating proteins in multiple system atrophy Purkinje cells.
Identifieur interne : 004027 ( PubMed/Corpus ); précédent : 004026; suivant : 004028Altered expression of calcium- and apoptosis-regulating proteins in multiple system atrophy Purkinje cells.
Auteurs : U. Wüllner ; M. Weller ; J. Kornhuber ; A. Bornemann ; J B Schulz ; P. Riederer ; T. KlockgetherSource :
- Movement disorders : official journal of the Movement Disorder Society [ 0885-3185 ] ; 2000.
English descriptors
- KwdEn :
- Apoptosis (physiology), Calbindins, Cell Nucleus (pathology), Cerebellum (pathology), Female, Humans, Male, Middle Aged, Multiple System Atrophy (pathology), Parvalbumins (analysis), Proto-Oncogene Proteins (analysis), Proto-Oncogene Proteins c-bcl-2 (analysis), Purkinje Cells (pathology), S100 Calcium Binding Protein G (analysis), bcl-2-Associated X Protein, bcl-X Protein.
- MESH :
- chemical , analysis : Parvalbumins, Proto-Oncogene Proteins, Proto-Oncogene Proteins c-bcl-2, S100 Calcium Binding Protein G.
- chemical : Calbindins, bcl-2-Associated X Protein, bcl-X Protein.
- pathology : Cell Nucleus, Cerebellum, Multiple System Atrophy, Purkinje Cells.
- physiology : Apoptosis.
- Female, Humans, Male, Middle Aged.
Abstract
The expression patterns of the calcium binding proteins calbindin and parvalbumin and of the apoptosis modulating proteins Bcl-2, Bax, and Bcl-x were studied in the cerebellum of patients with multiple system atrophy (MSA). Calbindin and parvalbumin immunoreactivity was markedly decreased in MSA Purkinje cells whereas Bax and Bcl-x protein expression was increased. Bcl-2 expression was restricted to a subpopulation of granule neurons, but no decrease of Bcl-2 was evident in MSA. Additional DNA end-labeling (ISEL) studies revealed only one possible apoptotic Purkinje cell nucleus, but nuclei in the cerebellar white matter, probably oligodendrocytes, in the cerebellum of patients with MSA. The present results suggest that a diminished calcium binding capacity of MSA Purkinje cells might lead to a change in the regulation of proteins of the bcl-2 family that could favor the pathologic initiation of apoptosis.
PubMed: 10752575
Links to Exploration step
pubmed:10752575Le document en format XML
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Bornemann</name></author><author><name sortKey="Schulz, J B" sort="Schulz, J B" uniqKey="Schulz J" first="J B" last="Schulz">J B Schulz</name></author><author><name sortKey="Riederer, P" sort="Riederer, P" uniqKey="Riederer P" first="P" last="Riederer">P. Riederer</name></author><author><name sortKey="Klockgether, T" sort="Klockgether, T" uniqKey="Klockgether T" first="T" last="Klockgether">T. Klockgether</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2000">2000</date><idno type="RBID">pubmed:10752575</idno><idno type="pmid">10752575</idno><idno type="wicri:Area/PubMed/Corpus">004027</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Altered expression of calcium- and apoptosis-regulating proteins in multiple system atrophy Purkinje cells.</title><author><name sortKey="Wullner, U" sort="Wullner, U" uniqKey="Wullner U" first="U" last="Wüllner">U. Wüllner</name><affiliation><nlm:affiliation>Department of Neurology, Rheinische Friedrich-Wilhelms-University, Bonn, Germany.</nlm:affiliation></affiliation></author><author><name sortKey="Weller, M" sort="Weller, M" uniqKey="Weller M" first="M" last="Weller">M. Weller</name></author><author><name sortKey="Kornhuber, J" sort="Kornhuber, J" uniqKey="Kornhuber J" first="J" last="Kornhuber">J. Kornhuber</name></author><author><name sortKey="Bornemann, A" sort="Bornemann, A" uniqKey="Bornemann A" first="A" last="Bornemann">A. Bornemann</name></author><author><name sortKey="Schulz, J B" sort="Schulz, J B" uniqKey="Schulz J" first="J B" last="Schulz">J B Schulz</name></author><author><name sortKey="Riederer, P" sort="Riederer, P" uniqKey="Riederer P" first="P" last="Riederer">P. Riederer</name></author><author><name sortKey="Klockgether, T" sort="Klockgether, T" uniqKey="Klockgether T" first="T" last="Klockgether">T. Klockgether</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>Apoptosis (physiology)</term><term>Calbindins</term><term>Cell Nucleus (pathology)</term><term>Cerebellum (pathology)</term><term>Female</term><term>Humans</term><term>Male</term><term>Middle Aged</term><term>Multiple System Atrophy (pathology)</term><term>Parvalbumins (analysis)</term><term>Proto-Oncogene Proteins (analysis)</term><term>Proto-Oncogene Proteins c-bcl-2 (analysis)</term><term>Purkinje Cells (pathology)</term><term>S100 Calcium Binding Protein G (analysis)</term><term>bcl-2-Associated X Protein</term><term>bcl-X Protein</term></keywords><keywords scheme="MESH" type="chemical" qualifier="analysis" xml:lang="en"><term>Parvalbumins</term><term>Proto-Oncogene Proteins</term><term>Proto-Oncogene Proteins c-bcl-2</term><term>S100 Calcium Binding Protein G</term></keywords><keywords scheme="MESH" type="chemical" xml:lang="en"><term>Calbindins</term><term>bcl-2-Associated X Protein</term><term>bcl-X Protein</term></keywords><keywords scheme="MESH" qualifier="pathology" xml:lang="en"><term>Cell Nucleus</term><term>Cerebellum</term><term>Multiple System Atrophy</term><term>Purkinje Cells</term></keywords><keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>Apoptosis</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Female</term><term>Humans</term><term>Male</term><term>Middle Aged</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The expression patterns of the calcium binding proteins calbindin and parvalbumin and of the apoptosis modulating proteins Bcl-2, Bax, and Bcl-x were studied in the cerebellum of patients with multiple system atrophy (MSA). Calbindin and parvalbumin immunoreactivity was markedly decreased in MSA Purkinje cells whereas Bax and Bcl-x protein expression was increased. Bcl-2 expression was restricted to a subpopulation of granule neurons, but no decrease of Bcl-2 was evident in MSA. Additional DNA end-labeling (ISEL) studies revealed only one possible apoptotic Purkinje cell nucleus, but nuclei in the cerebellar white matter, probably oligodendrocytes, in the cerebellum of patients with MSA. The present results suggest that a diminished calcium binding capacity of MSA Purkinje cells might lead to a change in the regulation of proteins of the bcl-2 family that could favor the pathologic initiation of apoptosis.</div></front></TEI><pubmed><MedlineCitation Owner="NLM" Status="MEDLINE"><PMID Version="1">10752575</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>2013</Year><Month>11</Month><Day>21</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. 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The present results suggest that a diminished calcium binding capacity of MSA Purkinje cells might lead to a change in the regulation of proteins of the bcl-2 family that could favor the pathologic initiation of apoptosis.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Wüllner</LastName><ForeName>U</ForeName><Initials>U</Initials><AffiliationInfo><Affiliation>Department of Neurology, Rheinische Friedrich-Wilhelms-University, Bonn, Germany.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Weller</LastName><ForeName>M</ForeName><Initials>M</Initials></Author><Author ValidYN="Y"><LastName>Kornhuber</LastName><ForeName>J</ForeName><Initials>J</Initials></Author><Author ValidYN="Y"><LastName>Bornemann</LastName><ForeName>A</ForeName><Initials>A</Initials></Author><Author ValidYN="Y"><LastName>Schulz</LastName><ForeName>J B</ForeName><Initials>JB</Initials></Author><Author 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MajorTopicYN="Y" UI="Q000473">pathology</QualifierName></MeshHeading><MeshHeading><DescriptorName MajorTopicYN="N" UI="D010320">Parvalbumins</DescriptorName><QualifierName MajorTopicYN="Y" UI="Q000032">analysis</QualifierName></MeshHeading><MeshHeading><DescriptorName MajorTopicYN="N" UI="D011518">Proto-Oncogene Proteins</DescriptorName><QualifierName MajorTopicYN="Y" UI="Q000032">analysis</QualifierName></MeshHeading><MeshHeading><DescriptorName MajorTopicYN="N" UI="D019253">Proto-Oncogene Proteins c-bcl-2</DescriptorName><QualifierName MajorTopicYN="Y" UI="Q000032">analysis</QualifierName></MeshHeading><MeshHeading><DescriptorName MajorTopicYN="N" UI="D011689">Purkinje Cells</DescriptorName><QualifierName MajorTopicYN="Y" UI="Q000473">pathology</QualifierName></MeshHeading><MeshHeading><DescriptorName MajorTopicYN="N" UI="D064030">S100 Calcium Binding Protein G</DescriptorName><QualifierName MajorTopicYN="Y" 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