Protein Targets of Oxidative Damage in Human Neurodegenerative Diseases with Abnormal Protein Aggregates
Identifieur interne : 000F18 ( Main/Corpus ); précédent : 000F17; suivant : 000F19Protein Targets of Oxidative Damage in Human Neurodegenerative Diseases with Abnormal Protein Aggregates
Auteurs : Anna Martínez ; Manuel Portero-Otin ; Reinald Pamplona ; Isidre FerrerSource :
- Brain Pathology [ 1015-6305 ] ; 2010-03.
English descriptors
- KwdEn :
Abstract
Human neurodegenerative diseases with abnormal protein aggregates are associated with aberrant post‐translational modifications, solubility, aggregation and fibril formation of selected proteins which cannot be degraded by cytosolic proteases, ubiquitin–protesome system and autophagy, and, therefore, accumulate in cells and extracellular compartments as residual debris. In addition to the accumulation of “primary” proteins, several other mechanisms are involved in the degenerative process and probably may explain crucial aspects such as the timing, selective cellular vulnerability and progression of the disease in particular individuals. One of these mechanisms is oxidative stress, which occurs in the vast majority of, if not all, degenerative diseases of the nervous system. The present review covers most of the protein targets that have been recognized as modified proteins mainly using bidimensional gel electrophoresis, Western blotting with oxidative and nitrosative markers, and identified by mass spectrometry in Alzheimer disease; certain tauopathies such as progressive supranuclear palsy, Pick disease, argyrophilic grain disease and frontotemporal lobar degeneration linked to mutations in tau protein, for example, FTLD‐tau, Parkinson disease and related α‐synucleinopathies; Huntington disease; and amyotrophic lateral sclerosis, together with related animal and cellular models. Vulnerable proteins can be mostly grouped in defined metabolic pathways covering glycolysis and energy metabolism, cytoskeletal, chaperoning, cellular stress responses, and members of the ubiquitin–proteasome system. Available information points to the fact that vital metabolic pathways are hampered by protein oxidative damage in several human degenerative diseases and that oxidative damage occurs at very early stages of the disease. Yet parallel functional studies are limited and further work is needed to document whether protein oxidation results in loss of activity and impaired performance. A better understanding of proteins susceptible to oxidation and nitration may serve to define damaged metabolic networks at early stages of disease and to advance therapeutic interventions to attenuate disease progression.
Url:
DOI: 10.1111/j.1750-3639.2009.00326.x
Links to Exploration step
ISTEX:D96CAE48E9E1163F85C9132476ADC895E080088ELe document en format XML
<record><TEI wicri:istexFullTextTei="biblStruct"><teiHeader><fileDesc><titleStmt><title xml:lang="en">Protein Targets of Oxidative Damage in Human Neurodegenerative Diseases with Abnormal Protein Aggregates</title><author><name sortKey="Martinez, Anna" sort="Martinez, Anna" uniqKey="Martinez A" first="Anna" last="Martínez">Anna Martínez</name><affiliation><mods:affiliation>Institut de Neuropatologia, Institut d'Investigacio de Bellvitge‐Hospital Universitari de Bellvitge, Universitat de Barcelona, Hospitalet de LLobregat, Centro de Inbvestigación Biomédica en Red de Enfermedades Neurodegenerativas, Spain.</mods:affiliation></affiliation></author><author><name sortKey="Portero Tin, Manuel" sort="Portero Tin, Manuel" uniqKey="Portero Tin M" first="Manuel" last="Portero-Otin">Manuel Portero-Otin</name><affiliation><mods:affiliation>Departament de Medicina Experimental, Universitat de Lleida‐Institut de Recerca Biomedica de Lleida, Lleida, Spain.</mods:affiliation></affiliation></author><author><name sortKey="Pamplona, Reinald" sort="Pamplona, Reinald" uniqKey="Pamplona R" first="Reinald" last="Pamplona">Reinald Pamplona</name><affiliation><mods:affiliation>Departament de Medicina Experimental, Universitat de Lleida‐Institut de Recerca Biomedica de Lleida, Lleida, Spain.</mods:affiliation></affiliation></author><author><name sortKey="Ferrer, Isidre" sort="Ferrer, Isidre" uniqKey="Ferrer I" first="Isidre" last="Ferrer">Isidre Ferrer</name><affiliation><mods:affiliation>Institut de Neuropatologia, Institut d'Investigacio de Bellvitge‐Hospital Universitari de Bellvitge, Universitat de Barcelona, Hospitalet de LLobregat, Centro de Inbvestigación Biomédica en Red de Enfermedades Neurodegenerativas, Spain.</mods:affiliation></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">ISTEX</idno><idno type="RBID">ISTEX:D96CAE48E9E1163F85C9132476ADC895E080088E</idno><date when="2010" year="2010">2010</date><idno type="doi">10.1111/j.1750-3639.2009.00326.x</idno><idno type="url">https://api.istex.fr/document/D96CAE48E9E1163F85C9132476ADC895E080088E/fulltext/pdf</idno><idno type="wicri:Area/Main/Corpus">000F18</idno></publicationStmt><sourceDesc><biblStruct><analytic><title level="a" type="main" xml:lang="en">Protein Targets of Oxidative Damage in Human Neurodegenerative Diseases with Abnormal Protein Aggregates</title><author><name sortKey="Martinez, Anna" sort="Martinez, Anna" uniqKey="Martinez A" first="Anna" last="Martínez">Anna Martínez</name><affiliation><mods:affiliation>Institut de Neuropatologia, Institut d'Investigacio de Bellvitge‐Hospital Universitari de Bellvitge, Universitat de Barcelona, Hospitalet de LLobregat, Centro de Inbvestigación Biomédica en Red de Enfermedades Neurodegenerativas, Spain.</mods:affiliation></affiliation></author><author><name sortKey="Portero Tin, Manuel" sort="Portero Tin, Manuel" uniqKey="Portero Tin M" first="Manuel" last="Portero-Otin">Manuel Portero-Otin</name><affiliation><mods:affiliation>Departament de Medicina Experimental, Universitat de Lleida‐Institut de Recerca Biomedica de Lleida, Lleida, Spain.</mods:affiliation></affiliation></author><author><name sortKey="Pamplona, Reinald" sort="Pamplona, Reinald" uniqKey="Pamplona R" first="Reinald" last="Pamplona">Reinald Pamplona</name><affiliation><mods:affiliation>Departament de Medicina Experimental, Universitat de Lleida‐Institut de Recerca Biomedica de Lleida, Lleida, Spain.</mods:affiliation></affiliation></author><author><name sortKey="Ferrer, Isidre" sort="Ferrer, Isidre" uniqKey="Ferrer I" first="Isidre" last="Ferrer">Isidre Ferrer</name><affiliation><mods:affiliation>Institut de Neuropatologia, Institut d'Investigacio de Bellvitge‐Hospital Universitari de Bellvitge, Universitat de Barcelona, Hospitalet de LLobregat, Centro de Inbvestigación Biomédica en Red de Enfermedades Neurodegenerativas, Spain.</mods:affiliation></affiliation></author></analytic><monogr></monogr><series><title level="j">Brain Pathology</title><idno type="ISSN">1015-6305</idno><idno type="eISSN">1750-3639</idno><imprint><publisher>Blackwell Publishing Ltd</publisher><pubPlace>Oxford, UK</pubPlace><date type="published" when="2010-03">2010-03</date><biblScope unit="volume">20</biblScope><biblScope unit="issue">2</biblScope><biblScope unit="page" from="281">281</biblScope><biblScope unit="page" to="297">297</biblScope></imprint><idno type="ISSN">1015-6305</idno></series><idno type="istex">D96CAE48E9E1163F85C9132476ADC895E080088E</idno><idno type="DOI">10.1111/j.1750-3639.2009.00326.x</idno><idno type="ArticleID">BPA326</idno></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">1015-6305</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Alzheimer disease</term><term>Huntington disease</term><term>Parkinson disease</term><term>amyotrophic lateral sclerosis</term><term>cytoskeleton</term><term>energy metabolism</term><term>mitochondria</term><term>neurodegeneration</term><term>nitration</term><term>oxidative stress</term><term>tauopathies</term></keywords></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Human neurodegenerative diseases with abnormal protein aggregates are associated with aberrant post‐translational modifications, solubility, aggregation and fibril formation of selected proteins which cannot be degraded by cytosolic proteases, ubiquitin–protesome system and autophagy, and, therefore, accumulate in cells and extracellular compartments as residual debris. In addition to the accumulation of “primary” proteins, several other mechanisms are involved in the degenerative process and probably may explain crucial aspects such as the timing, selective cellular vulnerability and progression of the disease in particular individuals. One of these mechanisms is oxidative stress, which occurs in the vast majority of, if not all, degenerative diseases of the nervous system. The present review covers most of the protein targets that have been recognized as modified proteins mainly using bidimensional gel electrophoresis, Western blotting with oxidative and nitrosative markers, and identified by mass spectrometry in Alzheimer disease; certain tauopathies such as progressive supranuclear palsy, Pick disease, argyrophilic grain disease and frontotemporal lobar degeneration linked to mutations in tau protein, for example, FTLD‐tau, Parkinson disease and related α‐synucleinopathies; Huntington disease; and amyotrophic lateral sclerosis, together with related animal and cellular models. Vulnerable proteins can be mostly grouped in defined metabolic pathways covering glycolysis and energy metabolism, cytoskeletal, chaperoning, cellular stress responses, and members of the ubiquitin–proteasome system. Available information points to the fact that vital metabolic pathways are hampered by protein oxidative damage in several human degenerative diseases and that oxidative damage occurs at very early stages of the disease. Yet parallel functional studies are limited and further work is needed to document whether protein oxidation results in loss of activity and impaired performance. A better understanding of proteins susceptible to oxidation and nitration may serve to define damaged metabolic networks at early stages of disease and to advance therapeutic interventions to attenuate disease progression.</div></front></TEI><istex><corpusName>wiley</corpusName><author><json:item><name>Anna Martínez</name><affiliations><json:string>Institut de Neuropatologia, Institut d'Investigacio de Bellvitge‐Hospital Universitari de Bellvitge, Universitat de Barcelona, Hospitalet de LLobregat, Centro de Inbvestigación Biomédica en Red de Enfermedades Neurodegenerativas, Spain.</json:string></affiliations></json:item><json:item><name>Manuel Portero‐Otin</name><affiliations><json:string>Departament de Medicina Experimental, Universitat de Lleida‐Institut de Recerca Biomedica de Lleida, Lleida, Spain.</json:string></affiliations></json:item><json:item><name>Reinald Pamplona</name><affiliations><json:string>Departament de Medicina Experimental, Universitat de Lleida‐Institut de Recerca Biomedica de Lleida, Lleida, Spain.</json:string></affiliations></json:item><json:item><name>Isidre Ferrer</name><affiliations><json:string>Institut de Neuropatologia, Institut d'Investigacio de Bellvitge‐Hospital Universitari de Bellvitge, Universitat de Barcelona, Hospitalet de LLobregat, Centro de Inbvestigación Biomédica en Red de Enfermedades Neurodegenerativas, Spain.</json:string></affiliations></json:item></author><subject><json:item><lang><json:string>eng</json:string></lang><value>Alzheimer disease</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>amyotrophic lateral sclerosis</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>cytoskeleton</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>energy metabolism</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>Huntington disease</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>mitochondria</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>neurodegeneration</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>nitration</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>oxidative stress</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>Parkinson disease</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>tauopathies</value></json:item></subject><articleId><json:string>BPA326</json:string></articleId><language><json:string>eng</json:string></language><abstract>Human neurodegenerative diseases with abnormal protein aggregates are associated with aberrant post‐translational modifications, solubility, aggregation and fibril formation of selected proteins which cannot be degraded by cytosolic proteases, ubiquitin–protesome system and autophagy, and, therefore, accumulate in cells and extracellular compartments as residual debris. In addition to the accumulation of “primary” proteins, several other mechanisms are involved in the degenerative process and probably may explain crucial aspects such as the timing, selective cellular vulnerability and progression of the disease in particular individuals. One of these mechanisms is oxidative stress, which occurs in the vast majority of, if not all, degenerative diseases of the nervous system. The present review covers most of the protein targets that have been recognized as modified proteins mainly using bidimensional gel electrophoresis, Western blotting with oxidative and nitrosative markers, and identified by mass spectrometry in Alzheimer disease; certain tauopathies such as progressive supranuclear palsy, Pick disease, argyrophilic grain disease and frontotemporal lobar degeneration linked to mutations in tau protein, for example, FTLD‐tau, Parkinson disease and related α‐synucleinopathies; Huntington disease; and amyotrophic lateral sclerosis, together with related animal and cellular models. Vulnerable proteins can be mostly grouped in defined metabolic pathways covering glycolysis and energy metabolism, cytoskeletal, chaperoning, cellular stress responses, and members of the ubiquitin–proteasome system. Available information points to the fact that vital metabolic pathways are hampered by protein oxidative damage in several human degenerative diseases and that oxidative damage occurs at very early stages of the disease. Yet parallel functional studies are limited and further work is needed to document whether protein oxidation results in loss of activity and impaired performance. A better understanding of proteins susceptible to oxidation and nitration may serve to define damaged metabolic networks at early stages of disease and to advance therapeutic interventions to attenuate disease progression.</abstract><qualityIndicators><score>8</score><pdfVersion>1.3</pdfVersion><pdfPageSize>595.276 x 782.362 pts</pdfPageSize><refBibsNative>true</refBibsNative><keywordCount>11</keywordCount><abstractCharCount>2227</abstractCharCount><pdfWordCount>10324</pdfWordCount><pdfCharCount>75087</pdfCharCount><pdfPageCount>17</pdfPageCount><abstractWordCount>297</abstractWordCount></qualityIndicators><title>Protein Targets of Oxidative Damage in Human Neurodegenerative Diseases with Abnormal Protein Aggregates</title><genre><json:string>review-article</json:string></genre><host><volume>20</volume><publisherId><json:string>BPA</json:string></publisherId><pages><total>17</total><last>297</last><first>281</first></pages><issn><json:string>1015-6305</json:string></issn><issue>2</issue><genre><json:string>Journal</json:string></genre><language><json:string>unknown</json:string></language><eissn><json:string>1750-3639</json:string></eissn><title>Brain Pathology</title><doi><json:string>10.1111/(ISSN)1750-3639</json:string></doi></host><publicationDate>2010</publicationDate><copyrightDate>2010</copyrightDate><doi><json:string>10.1111/j.1750-3639.2009.00326.x</json:string></doi><id>D96CAE48E9E1163F85C9132476ADC895E080088E</id><fulltext><json:item><original>true</original><mimetype>application/pdf</mimetype><extension>pdf</extension><uri>https://api.istex.fr/document/D96CAE48E9E1163F85C9132476ADC895E080088E/fulltext/pdf</uri></json:item><json:item><original>false</original><mimetype>application/zip</mimetype><extension>zip</extension><uri>https://api.istex.fr/document/D96CAE48E9E1163F85C9132476ADC895E080088E/fulltext/zip</uri></json:item><istex:fulltextTEI uri="https://api.istex.fr/document/D96CAE48E9E1163F85C9132476ADC895E080088E/fulltext/tei"><teiHeader><fileDesc><titleStmt><title level="a" type="main" xml:lang="en">Protein Targets of Oxidative Damage in Human Neurodegenerative Diseases with Abnormal Protein Aggregates</title></titleStmt><publicationStmt><authority>ISTEX</authority><publisher>Blackwell Publishing Ltd</publisher><pubPlace>Oxford, UK</pubPlace><availability><p>WILEY</p></availability><date>2010</date></publicationStmt><sourceDesc><biblStruct type="inbook"><analytic><title level="a" type="main" xml:lang="en">Protein Targets of Oxidative Damage in Human Neurodegenerative Diseases with Abnormal Protein Aggregates</title><author><persName><forename type="first">Anna</forename><surname>Martínez</surname></persName><affiliation>Institut de Neuropatologia, Institut d'Investigacio de Bellvitge‐Hospital Universitari de Bellvitge, Universitat de Barcelona, Hospitalet de LLobregat, Centro de Inbvestigación Biomédica en Red de Enfermedades Neurodegenerativas, Spain.</affiliation></author><author><persName><forename type="first">Manuel</forename><surname>Portero‐Otin</surname></persName><affiliation>Departament de Medicina Experimental, Universitat de Lleida‐Institut de Recerca Biomedica de Lleida, Lleida, Spain.</affiliation></author><author><persName><forename type="first">Reinald</forename><surname>Pamplona</surname></persName><affiliation>Departament de Medicina Experimental, Universitat de Lleida‐Institut de Recerca Biomedica de Lleida, Lleida, Spain.</affiliation></author><author><persName><forename type="first">Isidre</forename><surname>Ferrer</surname></persName><note type="correspondence"><p>Correspondence: Isidro Ferrer, MD, Institut Neuropatologia, Servei Anatomia Patològica, IDIBELL‐Hospital Universitari de Bellvitge, Carrer Feixa LLarga sn, 08907 Hospitalet de LLobregat, Spain (E‐mail: )</p></note><affiliation>Institut de Neuropatologia, Institut d'Investigacio de Bellvitge‐Hospital Universitari de Bellvitge, Universitat de Barcelona, Hospitalet de LLobregat, Centro de Inbvestigación Biomédica en Red de Enfermedades Neurodegenerativas, Spain.</affiliation></author></analytic><monogr><title level="j">Brain Pathology</title><idno type="pISSN">1015-6305</idno><idno type="eISSN">1750-3639</idno><idno type="DOI">10.1111/(ISSN)1750-3639</idno><imprint><publisher>Blackwell Publishing Ltd</publisher><pubPlace>Oxford, UK</pubPlace><date type="published" when="2010-03"></date><biblScope unit="volume">20</biblScope><biblScope unit="issue">2</biblScope><biblScope unit="page" from="281">281</biblScope><biblScope unit="page" to="297">297</biblScope></imprint></monogr><idno type="istex">D96CAE48E9E1163F85C9132476ADC895E080088E</idno><idno type="DOI">10.1111/j.1750-3639.2009.00326.x</idno><idno type="ArticleID">BPA326</idno></biblStruct></sourceDesc></fileDesc><profileDesc><creation><date>2010</date></creation><langUsage><language ident="en">en</language></langUsage><abstract xml:lang="en"><p>Human neurodegenerative diseases with abnormal protein aggregates are associated with aberrant post‐translational modifications, solubility, aggregation and fibril formation of selected proteins which cannot be degraded by cytosolic proteases, ubiquitin–protesome system and autophagy, and, therefore, accumulate in cells and extracellular compartments as residual debris. In addition to the accumulation of “primary” proteins, several other mechanisms are involved in the degenerative process and probably may explain crucial aspects such as the timing, selective cellular vulnerability and progression of the disease in particular individuals. One of these mechanisms is oxidative stress, which occurs in the vast majority of, if not all, degenerative diseases of the nervous system. The present review covers most of the protein targets that have been recognized as modified proteins mainly using bidimensional gel electrophoresis, Western blotting with oxidative and nitrosative markers, and identified by mass spectrometry in Alzheimer disease; certain tauopathies such as progressive supranuclear palsy, Pick disease, argyrophilic grain disease and frontotemporal lobar degeneration linked to mutations in tau protein, for example, FTLD‐tau, Parkinson disease and related α‐synucleinopathies; Huntington disease; and amyotrophic lateral sclerosis, together with related animal and cellular models. Vulnerable proteins can be mostly grouped in defined metabolic pathways covering glycolysis and energy metabolism, cytoskeletal, chaperoning, cellular stress responses, and members of the ubiquitin–proteasome system. Available information points to the fact that vital metabolic pathways are hampered by protein oxidative damage in several human degenerative diseases and that oxidative damage occurs at very early stages of the disease. Yet parallel functional studies are limited and further work is needed to document whether protein oxidation results in loss of activity and impaired performance. A better understanding of proteins susceptible to oxidation and nitration may serve to define damaged metabolic networks at early stages of disease and to advance therapeutic interventions to attenuate disease progression.</p></abstract><textClass xml:lang="en"><keywords scheme="keyword"><list><head>Keywords</head><item><term>Alzheimer disease</term></item><item><term>amyotrophic lateral sclerosis</term></item><item><term>cytoskeleton</term></item><item><term>energy metabolism</term></item><item><term>Huntington disease</term></item><item><term>mitochondria</term></item><item><term>neurodegeneration</term></item><item><term>nitration</term></item><item><term>oxidative stress</term></item><item><term>Parkinson disease</term></item><item><term>tauopathies</term></item></list></keywords></textClass></profileDesc><revisionDesc><change when="2010-03">Published</change></revisionDesc></teiHeader></istex:fulltextTEI><json:item><original>false</original><mimetype>text/plain</mimetype><extension>txt</extension><uri>https://api.istex.fr/document/D96CAE48E9E1163F85C9132476ADC895E080088E/fulltext/txt</uri></json:item></fulltext><metadata><istex:metadataXml wicri:clean="Wiley, elements deleted: body"><istex:xmlDeclaration>version="1.0" encoding="UTF-8" standalone="yes"</istex:xmlDeclaration><istex:document><component version="2.0" type="serialArticle" xml:lang="en"><header><publicationMeta level="product"><publisherInfo><publisherName>Blackwell Publishing Ltd</publisherName><publisherLoc>Oxford, UK</publisherLoc></publisherInfo><doi origin="wiley" registered="yes">10.1111/(ISSN)1750-3639</doi><issn type="print">1015-6305</issn><issn type="electronic">1750-3639</issn><idGroup><id type="product" value="BPA"></id><id type="publisherDivision" value="ST"></id></idGroup><titleGroup><title type="main" sort="BRAIN PATHOLOGY">Brain Pathology</title></titleGroup></publicationMeta><publicationMeta level="part" position="03002"><doi origin="wiley">10.1111/bpa.2010.20.issue-2</doi><numberingGroup><numbering type="journalVolume" number="20">20</numbering><numbering type="journalIssue" number="2">2</numbering></numberingGroup><coverDate startDate="2010-03">March 2010</coverDate></publicationMeta><publicationMeta level="unit" type="reviewArticle" position="2" status="forIssue"><doi origin="wiley">10.1111/j.1750-3639.2009.00326.x</doi><idGroup><id type="unit" value="BPA326"></id></idGroup><countGroup><count type="pageTotal" number="17"></count></countGroup><titleGroup><title type="tocHeading1">REVIEW ARTICLE</title></titleGroup><copyright>© 2009 The Authors. Journal Compilation © 2009 International Society of Neuropathology</copyright><eventGroup><event type="firstOnline" date="2009-08-06"></event><event type="publishedOnlineFinalForm" date="2010-02-02"></event><event type="xmlConverted" agent="Converter:BPG_TO_WML3G version:2.3.2 mode:FullText source:FullText result:FullText" date="2010-03-07"></event><event type="xmlConverted" agent="Converter:WILEY_ML3G_TO_WILEY_ML3GV2 version:3.8.8" date="2014-01-08"></event><event type="xmlConverted" agent="Converter:WML3G_To_WML3G version:4.1.7 mode:FullText,remove_FC" date="2014-10-15"></event></eventGroup><numberingGroup><numbering type="pageFirst" number="281">281</numbering><numbering type="pageLast" number="297">297</numbering></numberingGroup><correspondenceTo>Isidro Ferrer, MD, Institut Neuropatologia, Servei Anatomia Patològica, IDIBELL‐Hospital Universitari de Bellvitge, Carrer Feixa LLarga sn, 08907 Hospitalet de LLobregat, Spain (E‐mail: <email>8082ifa@gmail.com</email>)</correspondenceTo><linkGroup><link type="toTypesetVersion" href="file:BPA.BPA326.pdf"></link></linkGroup></publicationMeta><contentMeta><unparsedEditorialHistory>Received 15 July 2009; accepted 17 July 2009.</unparsedEditorialHistory><countGroup><count type="figureTotal" number="0"></count><count type="tableTotal" number="3"></count><count type="formulaTotal" number="0"></count><count type="referenceTotal" number="130"></count><count type="wordTotal" number="10815"></count><count type="linksPubMed" number="0"></count><count type="linksCrossRef" number="0"></count></countGroup><titleGroup><title type="main">Protein Targets of Oxidative Damage in Human Neurodegenerative Diseases with Abnormal Protein Aggregates</title><title type="shortAuthors">Martínez <i>et al</i></title><title type="short">Targets of Oxidative Damage in Neurodegenarative Diseases</title></titleGroup><creators><creator creatorRole="author" xml:id="cr1" affiliationRef="#a1"><personName><givenNames>Anna</givenNames><familyName>Martínez</familyName></personName></creator><creator creatorRole="author" xml:id="cr2" affiliationRef="#a2"><personName><givenNames>Manuel</givenNames><familyName>Portero‐Otin</familyName></personName></creator><creator creatorRole="author" xml:id="cr3" affiliationRef="#a2"><personName><givenNames>Reinald</givenNames><familyName>Pamplona</familyName></personName></creator><creator creatorRole="author" xml:id="cr4" affiliationRef="#a1" corresponding="yes"><personName><givenNames>Isidre</givenNames><familyName>Ferrer</familyName></personName></creator></creators><affiliationGroup><affiliation xml:id="a1" countryCode="ES"><unparsedAffiliation>Institut de Neuropatologia, Institut d'Investigacio de Bellvitge‐Hospital Universitari de Bellvitge, Universitat de Barcelona, Hospitalet de LLobregat, Centro de Inbvestigación Biomédica en Red de Enfermedades Neurodegenerativas, Spain.</unparsedAffiliation></affiliation><affiliation xml:id="a2" countryCode="ES"><unparsedAffiliation>Departament de Medicina Experimental, Universitat de Lleida‐Institut de Recerca Biomedica de Lleida, Lleida, Spain.</unparsedAffiliation></affiliation></affiliationGroup><keywordGroup xml:lang="en"><keyword xml:id="k1">Alzheimer disease</keyword><keyword xml:id="k2">amyotrophic lateral sclerosis</keyword><keyword xml:id="k3">cytoskeleton</keyword><keyword xml:id="k4">energy metabolism</keyword><keyword xml:id="k5">Huntington disease</keyword><keyword xml:id="k6">mitochondria</keyword><keyword xml:id="k7">neurodegeneration</keyword><keyword xml:id="k8">nitration</keyword><keyword xml:id="k9">oxidative stress</keyword><keyword xml:id="k10">Parkinson disease</keyword><keyword xml:id="k11">tauopathies</keyword></keywordGroup><supportingInformation><p><b>Table S1.</b> Alzheimer disease.</p><p><b>Table S2.</b> Tauopathies.</p><p><b>Table S3.</b> Parkinson disease and related α‐synucleinopathies.</p><p>Please note: Wiley‐Blackwell are not responsible for the content or functionality of any supporting materials supplied by the authors. Any queries (other than missing material) should be directed to the corresponding author for the article.</p><supportingInfoItem><mediaResource alt="supporting info item" href="urn-x:wiley:10156305:media:bpa326:BPA_326_sm_table_1"></mediaResource><caption>Supporting info item</caption></supportingInfoItem><supportingInfoItem><mediaResource alt="supporting info item" href="urn-x:wiley:10156305:media:bpa326:BPA_326_sm_table_2"></mediaResource><caption>Supporting info item</caption></supportingInfoItem><supportingInfoItem><mediaResource alt="supporting info item" href="urn-x:wiley:10156305:media:bpa326:BPA_326_sm_table_3"></mediaResource><caption>Supporting info item</caption></supportingInfoItem></supportingInformation><abstractGroup><abstract type="main" xml:lang="en"><title type="main">Abstract</title><p>Human neurodegenerative diseases with abnormal protein aggregates are associated with aberrant post‐translational modifications, solubility, aggregation and fibril formation of selected proteins which cannot be degraded by cytosolic proteases, ubiquitin–protesome system and autophagy, and, therefore, accumulate in cells and extracellular compartments as residual debris. In addition to the accumulation of “primary” proteins, several other mechanisms are involved in the degenerative process and probably may explain crucial aspects such as the timing, selective cellular vulnerability and progression of the disease in particular individuals. One of these mechanisms is oxidative stress, which occurs in the vast majority of, if not all, degenerative diseases of the nervous system. The present review covers most of the protein targets that have been recognized as modified proteins mainly using bidimensional gel electrophoresis, Western blotting with oxidative and nitrosative markers, and identified by mass spectrometry in Alzheimer disease; certain tauopathies such as progressive supranuclear palsy, Pick disease, argyrophilic grain disease and frontotemporal lobar degeneration linked to mutations in tau protein, for example, FTLD‐tau, Parkinson disease and related α‐synucleinopathies; Huntington disease; and amyotrophic lateral sclerosis, together with related animal and cellular models. Vulnerable proteins can be mostly grouped in defined metabolic pathways covering glycolysis and energy metabolism, cytoskeletal, chaperoning, cellular stress responses, and members of the ubiquitin–proteasome system. Available information points to the fact that vital metabolic pathways are hampered by protein oxidative damage in several human degenerative diseases and that oxidative damage occurs at very early stages of the disease. Yet parallel functional studies are limited and further work is needed to document whether protein oxidation results in loss of activity and impaired performance. A better understanding of proteins susceptible to oxidation and nitration may serve to define damaged metabolic networks at early stages of disease and to advance therapeutic interventions to attenuate disease progression.</p></abstract></abstractGroup></contentMeta></header></component></istex:document></istex:metadataXml><mods version="3.6"><titleInfo lang="en"><title>Protein Targets of Oxidative Damage in Human Neurodegenerative Diseases with Abnormal Protein Aggregates</title></titleInfo><titleInfo type="abbreviated"><title>Targets of Oxidative Damage in Neurodegenarative Diseases</title></titleInfo><titleInfo type="alternative" contentType="CDATA" lang="en"><title>Protein Targets of Oxidative Damage in Human Neurodegenerative Diseases with Abnormal Protein Aggregates</title></titleInfo><name type="personal"><namePart type="given">Anna</namePart><namePart type="family">Martínez</namePart><affiliation>Institut de Neuropatologia, Institut d'Investigacio de Bellvitge‐Hospital Universitari de Bellvitge, Universitat de Barcelona, Hospitalet de LLobregat, Centro de Inbvestigación Biomédica en Red de Enfermedades Neurodegenerativas, Spain.</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Manuel</namePart><namePart type="family">Portero‐Otin</namePart><affiliation>Departament de Medicina Experimental, Universitat de Lleida‐Institut de Recerca Biomedica de Lleida, Lleida, Spain.</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Reinald</namePart><namePart type="family">Pamplona</namePart><affiliation>Departament de Medicina Experimental, Universitat de Lleida‐Institut de Recerca Biomedica de Lleida, Lleida, Spain.</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Isidre</namePart><namePart type="family">Ferrer</namePart><affiliation>Institut de Neuropatologia, Institut d'Investigacio de Bellvitge‐Hospital Universitari de Bellvitge, Universitat de Barcelona, Hospitalet de LLobregat, Centro de Inbvestigación Biomédica en Red de Enfermedades Neurodegenerativas, Spain.</affiliation><description>Correspondence: Isidro Ferrer, MD, Institut Neuropatologia, Servei Anatomia Patològica, IDIBELL‐Hospital Universitari de Bellvitge, Carrer Feixa LLarga sn, 08907 Hospitalet de LLobregat, Spain (E‐mail: )</description><role><roleTerm type="text">author</roleTerm></role></name><typeOfResource>text</typeOfResource><genre type="review-article" displayLabel="reviewArticle"></genre><originInfo><publisher>Blackwell Publishing Ltd</publisher><place><placeTerm type="text">Oxford, UK</placeTerm></place><dateIssued encoding="w3cdtf">2010-03</dateIssued><edition>Received 15 July 2009; accepted 17 July 2009.</edition><copyrightDate encoding="w3cdtf">2010</copyrightDate></originInfo><language><languageTerm type="code" authority="rfc3066">en</languageTerm><languageTerm type="code" authority="iso639-2b">eng</languageTerm></language><physicalDescription><internetMediaType>text/html</internetMediaType><extent unit="tables">3</extent><extent unit="references">130</extent><extent unit="words">10815</extent></physicalDescription><abstract lang="en">Human neurodegenerative diseases with abnormal protein aggregates are associated with aberrant post‐translational modifications, solubility, aggregation and fibril formation of selected proteins which cannot be degraded by cytosolic proteases, ubiquitin–protesome system and autophagy, and, therefore, accumulate in cells and extracellular compartments as residual debris. In addition to the accumulation of “primary” proteins, several other mechanisms are involved in the degenerative process and probably may explain crucial aspects such as the timing, selective cellular vulnerability and progression of the disease in particular individuals. One of these mechanisms is oxidative stress, which occurs in the vast majority of, if not all, degenerative diseases of the nervous system. The present review covers most of the protein targets that have been recognized as modified proteins mainly using bidimensional gel electrophoresis, Western blotting with oxidative and nitrosative markers, and identified by mass spectrometry in Alzheimer disease; certain tauopathies such as progressive supranuclear palsy, Pick disease, argyrophilic grain disease and frontotemporal lobar degeneration linked to mutations in tau protein, for example, FTLD‐tau, Parkinson disease and related α‐synucleinopathies; Huntington disease; and amyotrophic lateral sclerosis, together with related animal and cellular models. Vulnerable proteins can be mostly grouped in defined metabolic pathways covering glycolysis and energy metabolism, cytoskeletal, chaperoning, cellular stress responses, and members of the ubiquitin–proteasome system. Available information points to the fact that vital metabolic pathways are hampered by protein oxidative damage in several human degenerative diseases and that oxidative damage occurs at very early stages of the disease. Yet parallel functional studies are limited and further work is needed to document whether protein oxidation results in loss of activity and impaired performance. A better understanding of proteins susceptible to oxidation and nitration may serve to define damaged metabolic networks at early stages of disease and to advance therapeutic interventions to attenuate disease progression.</abstract><subject lang="en"><genre>Keywords</genre><topic>Alzheimer disease</topic><topic>amyotrophic lateral sclerosis</topic><topic>cytoskeleton</topic><topic>energy metabolism</topic><topic>Huntington disease</topic><topic>mitochondria</topic><topic>neurodegeneration</topic><topic>nitration</topic><topic>oxidative stress</topic><topic>Parkinson disease</topic><topic>tauopathies</topic></subject><relatedItem type="host"><titleInfo><title>Brain Pathology</title></titleInfo><genre type="Journal">journal</genre><note type="content"> Table S1. Alzheimer disease. Table S2. Tauopathies. Table S3. Parkinson disease and related α‐synucleinopathies. Please note: Wiley‐Blackwell are not responsible for the content or functionality of any supporting materials supplied by the authors. Any queries (other than missing material) should be directed to the corresponding author for the article. Table S1. Alzheimer disease. Table S2. Tauopathies. Table S3. Parkinson disease and related α‐synucleinopathies. Please note: Wiley‐Blackwell are not responsible for the content or functionality of any supporting materials supplied by the authors. Any queries (other than missing material) should be directed to the corresponding author for the article. Table S1. Alzheimer disease. Table S2. Tauopathies. Table S3. Parkinson disease and related α‐synucleinopathies. Please note: Wiley‐Blackwell are not responsible for the content or functionality of any supporting materials supplied by the authors. Any queries (other than missing material) should be directed to the corresponding author for the article. Table S1. Alzheimer disease. Table S2. Tauopathies. Table S3. Parkinson disease and related α‐synucleinopathies. Please note: Wiley‐Blackwell are not responsible for the content or functionality of any supporting materials supplied by the authors. Any queries (other than missing material) should be directed to the corresponding author for the article.Supporting Info Item: Supporting info item - Supporting info item - Supporting info item - </note><identifier type="ISSN">1015-6305</identifier><identifier type="eISSN">1750-3639</identifier><identifier type="DOI">10.1111/(ISSN)1750-3639</identifier><identifier type="PublisherID">BPA</identifier><part><date>2010</date><detail type="volume"><caption>vol.</caption><number>20</number></detail><detail type="issue"><caption>no.</caption><number>2</number></detail><extent unit="pages"><start>281</start><end>297</end><total>17</total></extent></part></relatedItem><identifier type="istex">D96CAE48E9E1163F85C9132476ADC895E080088E</identifier><identifier type="DOI">10.1111/j.1750-3639.2009.00326.x</identifier><identifier type="ArticleID">BPA326</identifier><accessCondition type="use and reproduction" contentType="copyright">© 2009 The Authors. Journal Compilation © 2009 International Society of Neuropathology</accessCondition><recordInfo><recordContentSource>WILEY</recordContentSource><recordOrigin>Blackwell Publishing Ltd</recordOrigin></recordInfo></mods></metadata><serie></serie></istex></record>Pour manipuler ce document sous Unix (Dilib)
EXPLOR_STEP=$WICRI_ROOT/Wicri/Sante/explor/ParkinsonV1/Data/Main/Corpus
HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 000F18 | SxmlIndent | more
Ou
HfdSelect -h $EXPLOR_AREA/Data/Main/Corpus/biblio.hfd -nk 000F18 | SxmlIndent | more
Pour mettre un lien sur cette page dans le réseau Wicri
{{Explor lien
|wiki= Wicri/Sante
|area= ParkinsonV1
|flux= Main
|étape= Corpus
|type= RBID
|clé= ISTEX:D96CAE48E9E1163F85C9132476ADC895E080088E
|texte= Protein Targets of Oxidative Damage in Human Neurodegenerative Diseases with Abnormal Protein Aggregates
}}
| This area was generated with Dilib version V0.6.23. |  |