Cellular prion protein electron microscopy: attempts/limits and clues to a synaptic trait. Implications in neurodegeneration process.
Identifieur interne : 000811 ( Ncbi/Curation ); précédent : 000810; suivant : 000812Cellular prion protein electron microscopy: attempts/limits and clues to a synaptic trait. Implications in neurodegeneration process.
Auteurs : Jean-Guy Fournier [France]Source :
- Cell and tissue research [ 0302-766X ] ; 2008.
English descriptors
- KwdEn :
- Animals, Histocytological Preparation Techniques (methods), Humans, Microscopy, Electron (methods), Microscopy, Immunoelectron (methods), Models, Neurological, PrPC Proteins (physiology), PrPC Proteins (ultrastructure), PrPSc Proteins (metabolism), Prion Diseases (etiology), Prion Diseases (physiopathology), Synapses (physiology).
- MESH :
- chemical , metabolism : PrPSc Proteins.
- chemical , physiology : PrPC Proteins.
- etiology : Prion Diseases.
- methods : Histocytological Preparation Techniques, Microscopy, Electron, Microscopy, Immunoelectron.
- physiology : Synapses.
- physiopathology : Prion Diseases.
- chemical , ultrastructure : PrPC Proteins.
- Animals, Humans, Models, Neurological.
Abstract
Prion diseases are caused by an infectious agent constituted by a rogue protein called prion (PrP Sc) of neuronal origin (PrP c) and are exemplified by Creutzfeldt-Jakob disease in humans and bovine spongiform encephalopathy in cattle. Considerable efforts have been made to understand the cerebral damage caused by these diseases but a clear comprehensive view cannot be achieved without defining the neurophysiological function of PrP c. This lack of information is in part attributable to our ignorance of the precise localization of PrP c in the brain neuronal cell. One relevant option to explore this aspect is to undertake PrP immunohistochemistry at the electron-microscopy level, knowing that this challenge raises major technical constraints. In describing the attempts and restrictions of the various approaches used, we review here the efforts that have been invested in this particular field of prionology. The common result emerging from these contributions is that the synapse could be the site at which PrP c exerts its critical activity. This location suggests, in the perspective of synaptic regulation, that PrP c can be assigned multiple biological functions and supports the novel concept that prion-like changes are involved in long-term memory formation. The synaptic trait of PrP c and PrP Sc suggests that synapse loss is the key event in neuronal death. Interestingly, synaptic alterations are also considered to be predominant in the pathophysiological mechanism in Alzheimer, Parkinson and Huntington diseases. All these brain disorders, characterized by the formation of a specific amyloid protein of synaptic origin, can be classified under the heading of amyloidogenic synaptopathies.
DOI: 10.1007/s00441-007-0565-5
PubMed: 18236081
Links toward previous steps (curation, corpus...)
- to stream PubMed, to step Corpus: Pour aller vers cette notice dans l'étape Curation :000D03
- to stream PubMed, to step Curation: Pour aller vers cette notice dans l'étape Curation :000C63
- to stream PubMed, to step Checkpoint: Pour aller vers cette notice dans l'étape Curation :000C63
- to stream Ncbi, to step Merge: Pour aller vers cette notice dans l'étape Curation :000811
Links to Exploration step
pubmed:18236081Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Cellular prion protein electron microscopy: attempts/limits and clues to a synaptic trait. Implications in neurodegeneration process.</title>
<author><name sortKey="Fournier, Jean Guy" sort="Fournier, Jean Guy" uniqKey="Fournier J" first="Jean-Guy" last="Fournier">Jean-Guy Fournier</name>
<affiliation wicri:level="3"><nlm:affiliation>SEPIA/DSV/DRM/CEA, 18 Route Panorama, 92260, Fontenay aux Roses, France. jean-guy.fournier@cea.fr</nlm:affiliation>
<country xml:lang="fr">France</country>
<wicri:regionArea>SEPIA/DSV/DRM/CEA, 18 Route Panorama, 92260, Fontenay aux Roses</wicri:regionArea>
<placeName><region type="region" nuts="2">Île-de-France</region>
<settlement type="city">Fontenay aux Roses</settlement>
</placeName>
</affiliation>
</author>
</titleStmt>
<publicationStmt><idno type="wicri:source">PubMed</idno>
<date when="2008">2008</date>
<idno type="RBID">pubmed:18236081</idno>
<idno type="pmid">18236081</idno>
<idno type="doi">10.1007/s00441-007-0565-5</idno>
<idno type="wicri:Area/PubMed/Corpus">000D03</idno>
<idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">000D03</idno>
<idno type="wicri:Area/PubMed/Curation">000C63</idno>
<idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Curation">000C63</idno>
<idno type="wicri:Area/PubMed/Checkpoint">000C63</idno>
<idno type="wicri:explorRef" wicri:stream="Checkpoint" wicri:step="PubMed">000C63</idno>
<idno type="wicri:Area/Ncbi/Merge">000811</idno>
<idno type="wicri:Area/Ncbi/Curation">000811</idno>
</publicationStmt>
<sourceDesc><biblStruct><analytic><title xml:lang="en">Cellular prion protein electron microscopy: attempts/limits and clues to a synaptic trait. Implications in neurodegeneration process.</title>
<author><name sortKey="Fournier, Jean Guy" sort="Fournier, Jean Guy" uniqKey="Fournier J" first="Jean-Guy" last="Fournier">Jean-Guy Fournier</name>
<affiliation wicri:level="3"><nlm:affiliation>SEPIA/DSV/DRM/CEA, 18 Route Panorama, 92260, Fontenay aux Roses, France. jean-guy.fournier@cea.fr</nlm:affiliation>
<country xml:lang="fr">France</country>
<wicri:regionArea>SEPIA/DSV/DRM/CEA, 18 Route Panorama, 92260, Fontenay aux Roses</wicri:regionArea>
<placeName><region type="region" nuts="2">Île-de-France</region>
<settlement type="city">Fontenay aux Roses</settlement>
</placeName>
</affiliation>
</author>
</analytic>
<series><title level="j">Cell and tissue research</title>
<idno type="ISSN">0302-766X</idno>
<imprint><date when="2008" type="published">2008</date>
</imprint>
</series>
</biblStruct>
</sourceDesc>
</fileDesc>
<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Animals</term>
<term>Histocytological Preparation Techniques (methods)</term>
<term>Humans</term>
<term>Microscopy, Electron (methods)</term>
<term>Microscopy, Immunoelectron (methods)</term>
<term>Models, Neurological</term>
<term>PrPC Proteins (physiology)</term>
<term>PrPC Proteins (ultrastructure)</term>
<term>PrPSc Proteins (metabolism)</term>
<term>Prion Diseases (etiology)</term>
<term>Prion Diseases (physiopathology)</term>
<term>Synapses (physiology)</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>PrPSc Proteins</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="physiology" xml:lang="en"><term>PrPC Proteins</term>
</keywords>
<keywords scheme="MESH" qualifier="etiology" xml:lang="en"><term>Prion Diseases</term>
</keywords>
<keywords scheme="MESH" qualifier="methods" xml:lang="en"><term>Histocytological Preparation Techniques</term>
<term>Microscopy, Electron</term>
<term>Microscopy, Immunoelectron</term>
</keywords>
<keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>Synapses</term>
</keywords>
<keywords scheme="MESH" qualifier="physiopathology" xml:lang="en"><term>Prion Diseases</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="ultrastructure" xml:lang="en"><term>PrPC Proteins</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Animals</term>
<term>Humans</term>
<term>Models, Neurological</term>
</keywords>
</textClass>
</profileDesc>
</teiHeader>
<front><div type="abstract" xml:lang="en">Prion diseases are caused by an infectious agent constituted by a rogue protein called prion (PrP Sc) of neuronal origin (PrP c) and are exemplified by Creutzfeldt-Jakob disease in humans and bovine spongiform encephalopathy in cattle. Considerable efforts have been made to understand the cerebral damage caused by these diseases but a clear comprehensive view cannot be achieved without defining the neurophysiological function of PrP c. This lack of information is in part attributable to our ignorance of the precise localization of PrP c in the brain neuronal cell. One relevant option to explore this aspect is to undertake PrP immunohistochemistry at the electron-microscopy level, knowing that this challenge raises major technical constraints. In describing the attempts and restrictions of the various approaches used, we review here the efforts that have been invested in this particular field of prionology. The common result emerging from these contributions is that the synapse could be the site at which PrP c exerts its critical activity. This location suggests, in the perspective of synaptic regulation, that PrP c can be assigned multiple biological functions and supports the novel concept that prion-like changes are involved in long-term memory formation. The synaptic trait of PrP c and PrP Sc suggests that synapse loss is the key event in neuronal death. Interestingly, synaptic alterations are also considered to be predominant in the pathophysiological mechanism in Alzheimer, Parkinson and Huntington diseases. All these brain disorders, characterized by the formation of a specific amyloid protein of synaptic origin, can be classified under the heading of amyloidogenic synaptopathies.</div>
</front>
</TEI>
</record>
Pour manipuler ce document sous Unix (Dilib)
EXPLOR_STEP=$WICRI_ROOT/Wicri/Sante/explor/ParkinsonFranceV1/Data/Ncbi/Curation
HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 000811 | SxmlIndent | more
Ou
HfdSelect -h $EXPLOR_AREA/Data/Ncbi/Curation/biblio.hfd -nk 000811 | SxmlIndent | more
Pour mettre un lien sur cette page dans le réseau Wicri
{{Explor lien |wiki= Wicri/Sante |area= ParkinsonFranceV1 |flux= Ncbi |étape= Curation |type= RBID |clé= pubmed:18236081 |texte= Cellular prion protein electron microscopy: attempts/limits and clues to a synaptic trait. Implications in neurodegeneration process. }}
Pour générer des pages wiki
HfdIndexSelect -h $EXPLOR_AREA/Data/Ncbi/Curation/RBID.i -Sk "pubmed:18236081" \ | HfdSelect -Kh $EXPLOR_AREA/Data/Ncbi/Curation/biblio.hfd \ | NlmPubMed2Wicri -a ParkinsonFranceV1
![]() | This area was generated with Dilib version V0.6.29. | ![]() |