Protein aggregation and prionopathies.
Identifieur interne : 000555 ( PubMed/Corpus ); précédent : 000554; suivant : 000556Protein aggregation and prionopathies.
Auteurs : M. Renner ; R. MelkiSource :
- Pathologie-biologie [ 1768-3114 ] ; 2014.
English descriptors
- KwdEn :
- Aging, Alzheimer Disease (prevention & control), Amyotrophic Lateral Sclerosis (metabolism), Amyotrophic Lateral Sclerosis (pathology), Animals, Autophagy, Biopolymers, Clinical Trials, Phase II as Topic, Disease Models, Animal, Drug Evaluation, Preclinical, Endocytosis, Humans, Inclusion Bodies (chemistry), Inclusion Bodies (pathology), Mice, Nerve Tissue Proteins (chemistry), Neurodegenerative Diseases (metabolism), Neurodegenerative Diseases (pathology), Neurofibrillary Tangles (chemistry), Neurofibrillary Tangles (pathology), Plaque, Amyloid (chemistry), Plaque, Amyloid (pathology), Polysaccharides (therapeutic use), Prion Diseases (metabolism), Prion Diseases (pathology), Prion Diseases (veterinary), Prions (chemistry), Protein Aggregation, Pathological (metabolism), Protein Aggregation, Pathological (pathology), Protein Conformation, Solubility.
- MESH :
- chemical , chemistry : Nerve Tissue Proteins, Prions.
- chemical , therapeutic use : Polysaccharides.
- chemical : Biopolymers.
- chemistry : Inclusion Bodies, Neurofibrillary Tangles, Plaque, Amyloid.
- metabolism : Amyotrophic Lateral Sclerosis, Neurodegenerative Diseases, Prion Diseases, Protein Aggregation, Pathological.
- pathology : Amyotrophic Lateral Sclerosis, Inclusion Bodies, Neurodegenerative Diseases, Neurofibrillary Tangles, Plaque, Amyloid, Prion Diseases, Protein Aggregation, Pathological.
- prevention & control : Alzheimer Disease.
- veterinary : Prion Diseases.
- Aging, Animals, Autophagy, Clinical Trials, Phase II as Topic, Disease Models, Animal, Drug Evaluation, Preclinical, Endocytosis, Humans, Mice, Protein Conformation, Solubility.
Abstract
Prion protein and prion-like proteins share a number of characteristics. From the molecular point of view, they are constitutive proteins that aggregate following conformational changes into insoluble particles. These particles escape the cellular clearance machinery and amplify by recruiting the soluble for of their constituting proteins. The resulting protein aggregates are responsible for a number of neurodegenerative diseases such as Creutzfeldt-Jacob, Alzheimer, Parkinson and Huntington diseases. In addition, there are increasing evidences supporting the inter-cellular trafficking of these aggregates, meaning that they are "transmissible" between cells. There are also evidences that brain homogenates from individuals developing Alzheimer and Parkinson diseases propagate the disease in recipient model animals in a manner similar to brain extracts of patients developing Creutzfeldt-Jacob's disease. Thus, the propagation of protein aggregates from cell to cell may be a generic phenomenon that contributes to the evolution of neurodegenerative diseases, which has important consequences on human health issues. Moreover, although the distribution of protein aggregates is characteristic for each disease, new evidences indicate the possibility of overlaps and crosstalk between the different disorders. Despite the increasing evidences that support prion or prion-like propagation of protein aggregates, there are many unanswered questions regarding the mechanisms of toxicity and this is a field of intensive research nowadays.
DOI: 10.1016/j.patbio.2014.01.003
PubMed: 24698014
Links to Exploration step
pubmed:24698014Le document en format XML
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Melki</name><affiliation><nlm:affiliation>Laboratoire d'enzymologie et biochimie structurales, CNRS UPR 3082, bâtiment 34, avenue de la Terrasse, 91198 Gif-sur-Yvette, France.</nlm:affiliation></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2014">2014</date><idno type="RBID">pubmed:24698014</idno><idno type="pmid">24698014</idno><idno type="doi">10.1016/j.patbio.2014.01.003</idno><idno type="wicri:Area/PubMed/Corpus">000555</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">000555</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Protein aggregation and prionopathies.</title><author><name sortKey="Renner, M" sort="Renner, M" uniqKey="Renner M" first="M" last="Renner">M. Renner</name><affiliation><nlm:affiliation>Biologie cellulaire de la synapse, institut de biologie de l'École normale supérieure (IBENS), Inserm U1024 - CNRS 8197, 46, rue d'Ulm, 75005 Paris, France. Electronic address: renner@biologie.ens.fr.</nlm:affiliation></affiliation></author><author><name sortKey="Melki, R" sort="Melki, R" uniqKey="Melki R" first="R" last="Melki">R. Melki</name><affiliation><nlm:affiliation>Laboratoire d'enzymologie et biochimie structurales, CNRS UPR 3082, bâtiment 34, avenue de la Terrasse, 91198 Gif-sur-Yvette, France.</nlm:affiliation></affiliation></author></analytic><series><title level="j">Pathologie-biologie</title><idno type="eISSN">1768-3114</idno><imprint><date when="2014" type="published">2014</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Aging</term><term>Alzheimer Disease (prevention & control)</term><term>Amyotrophic Lateral Sclerosis (metabolism)</term><term>Amyotrophic Lateral Sclerosis (pathology)</term><term>Animals</term><term>Autophagy</term><term>Biopolymers</term><term>Clinical Trials, Phase II as Topic</term><term>Disease Models, Animal</term><term>Drug Evaluation, Preclinical</term><term>Endocytosis</term><term>Humans</term><term>Inclusion Bodies (chemistry)</term><term>Inclusion Bodies (pathology)</term><term>Mice</term><term>Nerve Tissue Proteins (chemistry)</term><term>Neurodegenerative Diseases (metabolism)</term><term>Neurodegenerative Diseases (pathology)</term><term>Neurofibrillary Tangles (chemistry)</term><term>Neurofibrillary Tangles (pathology)</term><term>Plaque, Amyloid (chemistry)</term><term>Plaque, Amyloid (pathology)</term><term>Polysaccharides (therapeutic use)</term><term>Prion Diseases (metabolism)</term><term>Prion Diseases (pathology)</term><term>Prion Diseases (veterinary)</term><term>Prions (chemistry)</term><term>Protein Aggregation, Pathological (metabolism)</term><term>Protein Aggregation, Pathological (pathology)</term><term>Protein Conformation</term><term>Solubility</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Nerve Tissue Proteins</term><term>Prions</term></keywords><keywords scheme="MESH" type="chemical" qualifier="therapeutic use" xml:lang="en"><term>Polysaccharides</term></keywords><keywords scheme="MESH" type="chemical" xml:lang="en"><term>Biopolymers</term></keywords><keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>Inclusion Bodies</term><term>Neurofibrillary Tangles</term><term>Plaque, Amyloid</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Amyotrophic Lateral Sclerosis</term><term>Neurodegenerative Diseases</term><term>Prion Diseases</term><term>Protein Aggregation, Pathological</term></keywords><keywords scheme="MESH" qualifier="pathology" xml:lang="en"><term>Amyotrophic Lateral Sclerosis</term><term>Inclusion Bodies</term><term>Neurodegenerative Diseases</term><term>Neurofibrillary Tangles</term><term>Plaque, Amyloid</term><term>Prion Diseases</term><term>Protein Aggregation, Pathological</term></keywords><keywords scheme="MESH" qualifier="prevention & control" xml:lang="en"><term>Alzheimer Disease</term></keywords><keywords scheme="MESH" qualifier="veterinary" xml:lang="en"><term>Prion Diseases</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Aging</term><term>Animals</term><term>Autophagy</term><term>Clinical Trials, Phase II as Topic</term><term>Disease Models, Animal</term><term>Drug Evaluation, Preclinical</term><term>Endocytosis</term><term>Humans</term><term>Mice</term><term>Protein Conformation</term><term>Solubility</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Prion protein and prion-like proteins share a number of characteristics. From the molecular point of view, they are constitutive proteins that aggregate following conformational changes into insoluble particles. These particles escape the cellular clearance machinery and amplify by recruiting the soluble for of their constituting proteins. The resulting protein aggregates are responsible for a number of neurodegenerative diseases such as Creutzfeldt-Jacob, Alzheimer, Parkinson and Huntington diseases. In addition, there are increasing evidences supporting the inter-cellular trafficking of these aggregates, meaning that they are "transmissible" between cells. There are also evidences that brain homogenates from individuals developing Alzheimer and Parkinson diseases propagate the disease in recipient model animals in a manner similar to brain extracts of patients developing Creutzfeldt-Jacob's disease. Thus, the propagation of protein aggregates from cell to cell may be a generic phenomenon that contributes to the evolution of neurodegenerative diseases, which has important consequences on human health issues. Moreover, although the distribution of protein aggregates is characteristic for each disease, new evidences indicate the possibility of overlaps and crosstalk between the different disorders. Despite the increasing evidences that support prion or prion-like propagation of protein aggregates, there are many unanswered questions regarding the mechanisms of toxicity and this is a field of intensive research nowadays.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">24698014</PMID><DateCreated><Year>2014</Year><Month>06</Month><Day>20</Day></DateCreated><DateCompleted><Year>2015</Year><Month>02</Month><Day>23</Day></DateCompleted><DateRevised><Year>2014</Year><Month>06</Month><Day>20</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1768-3114</ISSN><JournalIssue CitedMedium="Internet"><Volume>62</Volume><Issue>3</Issue><PubDate><Year>2014</Year><Month>Jun</Month></PubDate></JournalIssue><Title>Pathologie-biologie</Title><ISOAbbreviation>Pathol. Biol.</ISOAbbreviation></Journal><ArticleTitle>Protein aggregation and prionopathies.</ArticleTitle><Pagination><MedlinePgn>162-8</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1016/j.patbio.2014.01.003</ELocationID><ELocationID EIdType="pii" ValidYN="Y">S0369-8114(14)00033-9</ELocationID><Abstract><AbstractText>Prion protein and prion-like proteins share a number of characteristics. From the molecular point of view, they are constitutive proteins that aggregate following conformational changes into insoluble particles. These particles escape the cellular clearance machinery and amplify by recruiting the soluble for of their constituting proteins. The resulting protein aggregates are responsible for a number of neurodegenerative diseases such as Creutzfeldt-Jacob, Alzheimer, Parkinson and Huntington diseases. In addition, there are increasing evidences supporting the inter-cellular trafficking of these aggregates, meaning that they are "transmissible" between cells. There are also evidences that brain homogenates from individuals developing Alzheimer and Parkinson diseases propagate the disease in recipient model animals in a manner similar to brain extracts of patients developing Creutzfeldt-Jacob's disease. Thus, the propagation of protein aggregates from cell to cell may be a generic phenomenon that contributes to the evolution of neurodegenerative diseases, which has important consequences on human health issues. Moreover, although the distribution of protein aggregates is characteristic for each disease, new evidences indicate the possibility of overlaps and crosstalk between the different disorders. Despite the increasing evidences that support prion or prion-like propagation of protein aggregates, there are many unanswered questions regarding the mechanisms of toxicity and this is a field of intensive research nowadays.</AbstractText><CopyrightInformation>Copyright © 2014 Elsevier Masson SAS. All rights reserved.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Renner</LastName><ForeName>M</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>Biologie cellulaire de la synapse, institut de biologie de l'École normale supérieure (IBENS), Inserm U1024 - CNRS 8197, 46, rue d'Ulm, 75005 Paris, France. Electronic address: renner@biologie.ens.fr.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Melki</LastName><ForeName>R</ForeName><Initials>R</Initials><AffiliationInfo><Affiliation>Laboratoire d'enzymologie et biochimie structurales, CNRS UPR 3082, bâtiment 34, avenue de la Terrasse, 91198 Gif-sur-Yvette, France.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D016454">Review</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2014</Year><Month>03</Month><Day>31</Day></ArticleDate></Article><MedlineJournalInfo><Country>France</Country><MedlineTA>Pathol Biol (Paris)</MedlineTA><NlmUniqueID>0265365</NlmUniqueID><ISSNLinking>0369-8114</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D001704">Biopolymers</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D009419">Nerve Tissue Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011134">Polysaccharides</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011328">Prions</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C486237">alzhemed</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000375" MajorTopicYN="N">Aging</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D000544" MajorTopicYN="N">Alzheimer Disease</DescriptorName><QualifierName UI="Q000517" MajorTopicYN="N">prevention & control</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D000690" MajorTopicYN="N">Amyotrophic Lateral Sclerosis</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName><QualifierName UI="Q000473" MajorTopicYN="N">pathology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D001343" MajorTopicYN="N">Autophagy</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D001704" MajorTopicYN="N">Biopolymers</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D017322" MajorTopicYN="N">Clinical Trials, Phase II as Topic</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004195" MajorTopicYN="N">Disease Models, Animal</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004353" MajorTopicYN="N">Drug Evaluation, Preclinical</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004705" MajorTopicYN="N">Endocytosis</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002479" MajorTopicYN="N">Inclusion Bodies</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000473" MajorTopicYN="N">pathology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D051379" MajorTopicYN="N">Mice</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D009419" MajorTopicYN="N">Nerve Tissue Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D019636" MajorTopicYN="N">Neurodegenerative Diseases</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName><QualifierName UI="Q000473" MajorTopicYN="N">pathology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D016874" MajorTopicYN="N">Neurofibrillary Tangles</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000473" MajorTopicYN="N">pathology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D058225" MajorTopicYN="N">Plaque, Amyloid</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000473" MajorTopicYN="N">pathology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011134" MajorTopicYN="N">Polysaccharides</DescriptorName><QualifierName UI="Q000627" MajorTopicYN="N">therapeutic use</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D017096" MajorTopicYN="N">Prion Diseases</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName><QualifierName UI="Q000473" MajorTopicYN="N">pathology</QualifierName><QualifierName UI="Q000662" MajorTopicYN="N">veterinary</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011328" MajorTopicYN="N">Prions</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D066263" MajorTopicYN="N">Protein Aggregation, Pathological</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName><QualifierName UI="Q000473" MajorTopicYN="N">pathology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011487" MajorTopicYN="N">Protein Conformation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D012995" MajorTopicYN="N">Solubility</DescriptorName></MeshHeading></MeshHeadingList><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">Agrégation des protéines</Keyword><Keyword MajorTopicYN="N">Alpha-synucleinopathies</Keyword><Keyword MajorTopicYN="N">Alpha-synucléinopathies</Keyword><Keyword MajorTopicYN="N">Alzheimer</Keyword><Keyword MajorTopicYN="N">Amyotrophic lateral sclerosis</Keyword><Keyword MajorTopicYN="N">Huntington</Keyword><Keyword MajorTopicYN="N">Parkinson</Keyword><Keyword MajorTopicYN="N">Prion</Keyword><Keyword MajorTopicYN="N">Protein aggregation</Keyword><Keyword MajorTopicYN="N">Sclérose latérale amyotrophique</Keyword><Keyword MajorTopicYN="N">Tauopathies</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2013</Year><Month>12</Month><Day>12</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2014</Year><Month>01</Month><Day>28</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2014</Year><Month>4</Month><Day>5</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2014</Year><Month>4</Month><Day>5</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2015</Year><Month>2</Month><Day>24</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">24698014</ArticleId><ArticleId 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