Comparative biochemistry of tau in progressive supranuclear palsy, corticobasal degeneration, FTDP-17 and Pick's disease.
Identifieur interne : 004364 ( Main/Merge ); précédent : 004363; suivant : 004365Comparative biochemistry of tau in progressive supranuclear palsy, corticobasal degeneration, FTDP-17 and Pick's disease.
Auteurs : L. Buée [France] ; A. DelacourteSource :
- Brain pathology (Zurich, Switzerland) [ 1015-6305 ] ; 1999.
English descriptors
- KwdEn :
- Alzheimer Disease (metabolism), Chromosomes, Human, Pair 17 (genetics), Genetic Linkage, Humans, Microtubule-Associated Proteins (analysis), Nerve Degeneration (metabolism), Parkinson Disease (metabolism), Pick Disease of the Brain (metabolism), Supranuclear Palsy, Progressive (metabolism), tau Proteins (analysis).
- MESH :
- chemical , analysis : Microtubule-Associated Proteins, tau Proteins.
- genetics : Chromosomes, Human, Pair 17.
- metabolism : Alzheimer Disease, Nerve Degeneration, Parkinson Disease, Pick Disease of the Brain, Supranuclear Palsy, Progressive.
- Genetic Linkage, Humans.
Abstract
Neurodegenerative disorders referred to as tauopathies have cellular hyperphosphorylated tau protein aggregates in the absence of amyloid deposits. Comparative biochemistry of tau aggregates shows that they differ in both phosphorylation and content of tau isoforms. The six tau isoforms found in human brain contain either three (3R) or four microtubule-binding domains (4R). In Alzheimer's disease, all six tau isoforms are abnormally phosphorylated and aggregate into paired helical filaments. They are detected by immunoblotting as a major tau triplet (tau55, 64 and 69). In corticobasal degeneration and progressive supranuclear palsy, only 4R-tau isoforms aggregate into twisted and straight filaments respectively. They appear as a major tau doublet (tau64 and 69). Finally, in Pick's disease, only 3R-tau isoforms aggregate into random coiled filaments. They are characterized by another major tau doublet (tau55 and 64). These differences in tau isoforms may be related to either the degeneration of particular cell populations in a given disorder or aberrant cell trafficking of particular tau isoforms. Finally, recent findings provide a direct link between a genetic defect in tau and its abnormal aggregation into filaments in fronto-temporal dementia with Parkinsonism linked to chromosome 17, demonstrating that tau aggregation is sufficient for nerve cell degeneration. Thus, tau mutations and polymorphisms may also be instrumental in many neurodegenerative disorders.
PubMed: 10517507
Links toward previous steps (curation, corpus...)
- to stream PubMed, to step Corpus: 001370
- to stream PubMed, to step Curation: 001329
- to stream PubMed, to step Checkpoint: 001329
- to stream Ncbi, to step Merge: 000068
- to stream Ncbi, to step Curation: 000068
- to stream Ncbi, to step Checkpoint: 000068
Links to Exploration step
pubmed:10517507Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Comparative biochemistry of tau in progressive supranuclear palsy, corticobasal degeneration, FTDP-17 and Pick's disease.</title>
<author><name sortKey="Buee, L" sort="Buee, L" uniqKey="Buee L" first="L" last="Buée">L. Buée</name>
<affiliation wicri:level="3"><nlm:affiliation>INSERM U422, F-59045 Lille, France. buee@lille.inserm.fr</nlm:affiliation>
<country xml:lang="fr">France</country>
<wicri:regionArea>INSERM U422, F-59045 Lille</wicri:regionArea>
<placeName><region type="region" nuts="2">Hauts-de-France</region>
<region type="old region" nuts="2">Nord-Pas-de-Calais</region>
<settlement type="city">Lille</settlement>
</placeName>
</affiliation>
</author>
<author><name sortKey="Delacourte, A" sort="Delacourte, A" uniqKey="Delacourte A" first="A" last="Delacourte">A. Delacourte</name>
</author>
</titleStmt>
<publicationStmt><idno type="wicri:source">PubMed</idno>
<date when="1999">1999</date>
<idno type="RBID">pubmed:10517507</idno>
<idno type="pmid">10517507</idno>
<idno type="wicri:Area/PubMed/Corpus">001370</idno>
<idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">001370</idno>
<idno type="wicri:Area/PubMed/Curation">001329</idno>
<idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Curation">001329</idno>
<idno type="wicri:Area/PubMed/Checkpoint">001329</idno>
<idno type="wicri:explorRef" wicri:stream="Checkpoint" wicri:step="PubMed">001329</idno>
<idno type="wicri:Area/Ncbi/Merge">000068</idno>
<idno type="wicri:Area/Ncbi/Curation">000068</idno>
<idno type="wicri:Area/Ncbi/Checkpoint">000068</idno>
<idno type="wicri:doubleKey">1015-6305:1999:Buee L:comparative:biochemistry:of</idno>
<idno type="wicri:Area/Main/Merge">004364</idno>
</publicationStmt>
<sourceDesc><biblStruct><analytic><title xml:lang="en">Comparative biochemistry of tau in progressive supranuclear palsy, corticobasal degeneration, FTDP-17 and Pick's disease.</title>
<author><name sortKey="Buee, L" sort="Buee, L" uniqKey="Buee L" first="L" last="Buée">L. Buée</name>
<affiliation wicri:level="3"><nlm:affiliation>INSERM U422, F-59045 Lille, France. buee@lille.inserm.fr</nlm:affiliation>
<country xml:lang="fr">France</country>
<wicri:regionArea>INSERM U422, F-59045 Lille</wicri:regionArea>
<placeName><region type="region" nuts="2">Hauts-de-France</region>
<region type="old region" nuts="2">Nord-Pas-de-Calais</region>
<settlement type="city">Lille</settlement>
</placeName>
</affiliation>
</author>
<author><name sortKey="Delacourte, A" sort="Delacourte, A" uniqKey="Delacourte A" first="A" last="Delacourte">A. Delacourte</name>
</author>
</analytic>
<series><title level="j">Brain pathology (Zurich, Switzerland)</title>
<idno type="ISSN">1015-6305</idno>
<imprint><date when="1999" type="published">1999</date>
</imprint>
</series>
</biblStruct>
</sourceDesc>
</fileDesc>
<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Alzheimer Disease (metabolism)</term>
<term>Chromosomes, Human, Pair 17 (genetics)</term>
<term>Genetic Linkage</term>
<term>Humans</term>
<term>Microtubule-Associated Proteins (analysis)</term>
<term>Nerve Degeneration (metabolism)</term>
<term>Parkinson Disease (metabolism)</term>
<term>Pick Disease of the Brain (metabolism)</term>
<term>Supranuclear Palsy, Progressive (metabolism)</term>
<term>tau Proteins (analysis)</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="analysis" xml:lang="en"><term>Microtubule-Associated Proteins</term>
<term>tau Proteins</term>
</keywords>
<keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Chromosomes, Human, Pair 17</term>
</keywords>
<keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Alzheimer Disease</term>
<term>Nerve Degeneration</term>
<term>Parkinson Disease</term>
<term>Pick Disease of the Brain</term>
<term>Supranuclear Palsy, Progressive</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Genetic Linkage</term>
<term>Humans</term>
</keywords>
</textClass>
</profileDesc>
</teiHeader>
<front><div type="abstract" xml:lang="en">Neurodegenerative disorders referred to as tauopathies have cellular hyperphosphorylated tau protein aggregates in the absence of amyloid deposits. Comparative biochemistry of tau aggregates shows that they differ in both phosphorylation and content of tau isoforms. The six tau isoforms found in human brain contain either three (3R) or four microtubule-binding domains (4R). In Alzheimer's disease, all six tau isoforms are abnormally phosphorylated and aggregate into paired helical filaments. They are detected by immunoblotting as a major tau triplet (tau55, 64 and 69). In corticobasal degeneration and progressive supranuclear palsy, only 4R-tau isoforms aggregate into twisted and straight filaments respectively. They appear as a major tau doublet (tau64 and 69). Finally, in Pick's disease, only 3R-tau isoforms aggregate into random coiled filaments. They are characterized by another major tau doublet (tau55 and 64). These differences in tau isoforms may be related to either the degeneration of particular cell populations in a given disorder or aberrant cell trafficking of particular tau isoforms. Finally, recent findings provide a direct link between a genetic defect in tau and its abnormal aggregation into filaments in fronto-temporal dementia with Parkinsonism linked to chromosome 17, demonstrating that tau aggregation is sufficient for nerve cell degeneration. Thus, tau mutations and polymorphisms may also be instrumental in many neurodegenerative disorders.</div>
</front>
</TEI>
</record>
Pour manipuler ce document sous Unix (Dilib)
EXPLOR_STEP=$WICRI_ROOT/Wicri/Sante/explor/ParkinsonFranceV1/Data/Main/Merge
HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 004364 | SxmlIndent | more
Ou
HfdSelect -h $EXPLOR_AREA/Data/Main/Merge/biblio.hfd -nk 004364 | SxmlIndent | more
Pour mettre un lien sur cette page dans le réseau Wicri
{{Explor lien |wiki= Wicri/Sante |area= ParkinsonFranceV1 |flux= Main |étape= Merge |type= RBID |clé= pubmed:10517507 |texte= Comparative biochemistry of tau in progressive supranuclear palsy, corticobasal degeneration, FTDP-17 and Pick's disease. }}
Pour générer des pages wiki
HfdIndexSelect -h $EXPLOR_AREA/Data/Main/Merge/RBID.i -Sk "pubmed:10517507" \ | HfdSelect -Kh $EXPLOR_AREA/Data/Main/Merge/biblio.hfd \ | NlmPubMed2Wicri -a ParkinsonFranceV1
![]() | This area was generated with Dilib version V0.6.29. | ![]() |