Quantitation of Alzheimer's amyloid peptide and identification of related amyloid proteins by dot-blot immunoassay
Identifieur interne : 001850 ( Istex/Corpus ); précédent : 001849; suivant : 001851Quantitation of Alzheimer's amyloid peptide and identification of related amyloid proteins by dot-blot immunoassay
Auteurs : Bruno Permanne ; Luc Buée ; Jean-Philippe David ; Catherine Fallet-Bianco ; Claude Di Menza ; André DelacourteSource :
- Brain Research [ 0006-8993 ] ; 1995.
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Abstract
In Alzheimer's disease, the main component of amyloid deposits is a 39–43 amino acid peptide referred to as amyloid peptide or A β. A crucial issue in the study of this disorder is to define the sequence of events that lead to amyloid deposition. In the present study, a new approach was developed that allows to specifically solubilize A β peptide trapped within amyloid deposits and to quantify its amount by dot-blot immunoassay. The present method also permits to isolate components tightly bound to A β and that are likely to catalyze its aggregation. Biochemical A β quantitation was performed in 4 Brodmann areas from 17 elderly individuals exhibiting different degrees of amyloidosis. In parallel, classical neuropathology was done by histochemical and immunohistochemical methods. A β amounts (pmol) were correlated to the number of amyloid deposits determined by neuropathology showing high statistical significance. Moreover, amyloid-binding proteins including apolipoprotein E and heparan sulfate proteoglycans were also found associated to A β in the amyloid preparation. The present biochemical procedure is a new and reliable method to quantify amyloid deposition in brain. Furthermore, it allows to detect amyloid-associated components such as apolipoprotein E, that may be involved in the pathological process of amyloidogenesis.
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DOI: 10.1016/0006-8993(95)00431-O
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Fax: (33) 2052-3794; or (33) 2062-2061.</mods:affiliation></affiliation><affiliation><mods:affiliation>INSERM U422, Place de Verdun, 59045 Lille Cedex, France</mods:affiliation></affiliation></author><author><name sortKey="David, Jean Philippe" sort="David, Jean Philippe" uniqKey="David J" first="Jean-Philippe" last="David">Jean-Philippe David</name><affiliation><mods:affiliation>INSERM U422, Place de Verdun, 59045 Lille Cedex, France</mods:affiliation></affiliation><affiliation><mods:affiliation>Hôpital Emile Roux, Avenue de Verdun, 94450 Limeil-Brévannes, France</mods:affiliation></affiliation></author><author><name sortKey="Fallet Bianco, Catherine" sort="Fallet Bianco, Catherine" uniqKey="Fallet Bianco C" first="Catherine" last="Fallet-Bianco">Catherine Fallet-Bianco</name><affiliation><mods:affiliation>Hôpital Emile Roux, Avenue de Verdun, 94450 Limeil-Brévannes, France</mods:affiliation></affiliation></author><author><name sortKey="Di Menza, Claude" sort="Di Menza, Claude" uniqKey="Di Menza C" first="Claude" last="Di Menza">Claude Di Menza</name><affiliation><mods:affiliation>Hôpital Emile Roux, Avenue de Verdun, 94450 Limeil-Brévannes, France</mods:affiliation></affiliation></author><author><name sortKey="Delacourte, Andre" sort="Delacourte, Andre" uniqKey="Delacourte A" first="André" last="Delacourte">André Delacourte</name><affiliation><mods:affiliation>INSERM U422, Place de Verdun, 59045 Lille Cedex, France</mods:affiliation></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">ISTEX</idno><idno type="RBID">ISTEX:B8401D072C64B3BB7B811CBB9F6126FB98E98D9F</idno><date when="1995" year="1995">1995</date><idno type="doi">10.1016/0006-8993(95)00431-O</idno><idno type="url">https://api.istex.fr/document/B8401D072C64B3BB7B811CBB9F6126FB98E98D9F/fulltext/pdf</idno><idno type="wicri:Area/Istex/Corpus">001850</idno><idno type="wicri:explorRef" wicri:stream="Istex" wicri:step="Corpus" wicri:corpus="ISTEX">001850</idno></publicationStmt><sourceDesc><biblStruct><analytic><title level="a" type="main" xml:lang="en">Quantitation of Alzheimer's amyloid peptide and identification of related amyloid proteins by dot-blot immunoassay</title><author><name sortKey="Permanne, Bruno" sort="Permanne, Bruno" uniqKey="Permanne B" first="Bruno" last="Permanne">Bruno Permanne</name><affiliation><mods:affiliation>INSERM U422, Place de Verdun, 59045 Lille Cedex, France</mods:affiliation></affiliation></author><author><name sortKey="Buee, Luc" sort="Buee, Luc" uniqKey="Buee L" first="Luc" last="Buée">Luc Buée</name><affiliation><mods:affiliation>Corresponding author. Fax: (33) 2052-3794; or (33) 2062-2061.</mods:affiliation></affiliation><affiliation><mods:affiliation>INSERM U422, Place de Verdun, 59045 Lille Cedex, France</mods:affiliation></affiliation></author><author><name sortKey="David, Jean Philippe" sort="David, Jean Philippe" uniqKey="David J" first="Jean-Philippe" last="David">Jean-Philippe David</name><affiliation><mods:affiliation>INSERM U422, Place de Verdun, 59045 Lille Cedex, France</mods:affiliation></affiliation><affiliation><mods:affiliation>Hôpital Emile Roux, Avenue de Verdun, 94450 Limeil-Brévannes, France</mods:affiliation></affiliation></author><author><name sortKey="Fallet Bianco, Catherine" sort="Fallet Bianco, Catherine" uniqKey="Fallet Bianco C" first="Catherine" last="Fallet-Bianco">Catherine Fallet-Bianco</name><affiliation><mods:affiliation>Hôpital Emile Roux, Avenue de Verdun, 94450 Limeil-Brévannes, France</mods:affiliation></affiliation></author><author><name sortKey="Di Menza, Claude" sort="Di Menza, Claude" uniqKey="Di Menza C" first="Claude" last="Di Menza">Claude Di Menza</name><affiliation><mods:affiliation>Hôpital Emile Roux, Avenue de Verdun, 94450 Limeil-Brévannes, France</mods:affiliation></affiliation></author><author><name sortKey="Delacourte, Andre" sort="Delacourte, Andre" uniqKey="Delacourte A" first="André" last="Delacourte">André Delacourte</name><affiliation><mods:affiliation>INSERM U422, Place de Verdun, 59045 Lille Cedex, France</mods:affiliation></affiliation></author></analytic><monogr></monogr><series><title level="j">Brain Research</title><title level="j" type="abbrev">BRES</title><idno type="ISSN">0006-8993</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="1995">1995</date><biblScope unit="volume">685</biblScope><biblScope unit="issue">1–2</biblScope><biblScope unit="page" from="154">154</biblScope><biblScope unit="page" to="162">162</biblScope></imprint><idno type="ISSN">0006-8993</idno></series><idno type="istex">B8401D072C64B3BB7B811CBB9F6126FB98E98D9F</idno><idno type="DOI">10.1016/0006-8993(95)00431-O</idno><idno type="PII">0006-8993(95)00431-O</idno><idno type="ArticleID">9500431O</idno></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0006-8993</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Aging</term><term>Amyloidosis</term><term>Apolipoprotein E</term><term>Neuropathology</term><term>Proteoglycans</term></keywords></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">In Alzheimer's disease, the main component of amyloid deposits is a 39–43 amino acid peptide referred to as amyloid peptide or A β. A crucial issue in the study of this disorder is to define the sequence of events that lead to amyloid deposition. In the present study, a new approach was developed that allows to specifically solubilize A β peptide trapped within amyloid deposits and to quantify its amount by dot-blot immunoassay. The present method also permits to isolate components tightly bound to A β and that are likely to catalyze its aggregation. Biochemical A β quantitation was performed in 4 Brodmann areas from 17 elderly individuals exhibiting different degrees of amyloidosis. In parallel, classical neuropathology was done by histochemical and immunohistochemical methods. A β amounts (pmol) were correlated to the number of amyloid deposits determined by neuropathology showing high statistical significance. Moreover, amyloid-binding proteins including apolipoprotein E and heparan sulfate proteoglycans were also found associated to A β in the amyloid preparation. The present biochemical procedure is a new and reliable method to quantify amyloid deposition in brain. Furthermore, it allows to detect amyloid-associated components such as apolipoprotein E, that may be involved in the pathological process of amyloidogenesis.</div></front></TEI><istex><corpusName>elsevier</corpusName><author><json:item><name>Bruno Permanne</name><affiliations><json:string>INSERM U422, Place de Verdun, 59045 Lille Cedex, France</json:string></affiliations></json:item><json:item><name>Luc Buée</name><affiliations><json:string>Corresponding author. Fax: (33) 2052-3794; or (33) 2062-2061.</json:string><json:string>INSERM U422, Place de Verdun, 59045 Lille Cedex, France</json:string></affiliations></json:item><json:item><name>Jean-Philippe David</name><affiliations><json:string>INSERM U422, Place de Verdun, 59045 Lille Cedex, France</json:string><json:string>Hôpital Emile Roux, Avenue de Verdun, 94450 Limeil-Brévannes, France</json:string></affiliations></json:item><json:item><name>Catherine Fallet-Bianco</name><affiliations><json:string>Hôpital Emile Roux, Avenue de Verdun, 94450 Limeil-Brévannes, France</json:string></affiliations></json:item><json:item><name>Claude Di Menza</name><affiliations><json:string>Hôpital Emile Roux, Avenue de Verdun, 94450 Limeil-Brévannes, France</json:string></affiliations></json:item><json:item><name>André Delacourte</name><affiliations><json:string>INSERM U422, Place de Verdun, 59045 Lille Cedex, France</json:string></affiliations></json:item></author><subject><json:item><lang><json:string>eng</json:string></lang><value>Aging</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>Amyloidosis</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>Apolipoprotein E</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>Neuropathology</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>Proteoglycans</value></json:item></subject><articleId><json:string>9500431O</json:string></articleId><language><json:string>eng</json:string></language><originalGenre><json:string>Full-length article</json:string></originalGenre><abstract>In Alzheimer's disease, the main component of amyloid deposits is a 39–43 amino acid peptide referred to as amyloid peptide or A β. A crucial issue in the study of this disorder is to define the sequence of events that lead to amyloid deposition. In the present study, a new approach was developed that allows to specifically solubilize A β peptide trapped within amyloid deposits and to quantify its amount by dot-blot immunoassay. The present method also permits to isolate components tightly bound to A β and that are likely to catalyze its aggregation. Biochemical A β quantitation was performed in 4 Brodmann areas from 17 elderly individuals exhibiting different degrees of amyloidosis. In parallel, classical neuropathology was done by histochemical and immunohistochemical methods. A β amounts (pmol) were correlated to the number of amyloid deposits determined by neuropathology showing high statistical significance. Moreover, amyloid-binding proteins including apolipoprotein E and heparan sulfate proteoglycans were also found associated to A β in the amyloid preparation. The present biochemical procedure is a new and reliable method to quantify amyloid deposition in brain. Furthermore, it allows to detect amyloid-associated components such as apolipoprotein E, that may be involved in the pathological process of amyloidogenesis.</abstract><qualityIndicators><score>7.412</score><pdfVersion>1.2</pdfVersion><pdfPageSize>591 x 807 pts</pdfPageSize><refBibsNative>true</refBibsNative><keywordCount>5</keywordCount><abstractCharCount>1346</abstractCharCount><pdfWordCount>5212</pdfWordCount><pdfCharCount>32333</pdfCharCount><pdfPageCount>9</pdfPageCount><abstractWordCount>201</abstractWordCount></qualityIndicators><title>Quantitation of Alzheimer's amyloid peptide and identification of related amyloid proteins by dot-blot immunoassay</title><pii><json:string>0006-8993(95)00431-O</json:string></pii><refBibs><json:item><author><json:item><name>C.R. Abraham</name></json:item><json:item><name>D.J. Selkoe</name></json:item><json:item><name>H. 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USA</title></serie><host><volume>685</volume><pii><json:string>S0006-8993(00)X0050-9</json:string></pii><pages><last>162</last><first>154</first></pages><issn><json:string>0006-8993</json:string></issn><issue>1–2</issue><genre><json:string>journal</json:string></genre><language><json:string>unknown</json:string></language><title>Brain Research</title><publicationDate>1995</publicationDate></host><categories><wos><json:string>science</json:string><json:string>neurosciences</json:string></wos><scienceMetrix><json:string>health sciences</json:string><json:string>clinical medicine</json:string><json:string>neurology & neurosurgery</json:string></scienceMetrix></categories><publicationDate>1995</publicationDate><copyrightDate>1995</copyrightDate><doi><json:string>10.1016/0006-8993(95)00431-O</json:string></doi><id>B8401D072C64B3BB7B811CBB9F6126FB98E98D9F</id><score>0.14092793</score><fulltext><json:item><extension>pdf</extension><original>true</original><mimetype>application/pdf</mimetype><uri>https://api.istex.fr/document/B8401D072C64B3BB7B811CBB9F6126FB98E98D9F/fulltext/pdf</uri></json:item><json:item><extension>zip</extension><original>false</original><mimetype>application/zip</mimetype><uri>https://api.istex.fr/document/B8401D072C64B3BB7B811CBB9F6126FB98E98D9F/fulltext/zip</uri></json:item><istex:fulltextTEI uri="https://api.istex.fr/document/B8401D072C64B3BB7B811CBB9F6126FB98E98D9F/fulltext/tei"><teiHeader><fileDesc><titleStmt><title level="a" type="main" xml:lang="en">Quantitation of Alzheimer's amyloid peptide and identification of related amyloid proteins by dot-blot immunoassay</title></titleStmt><publicationStmt><authority>ISTEX</authority><publisher>ELSEVIER</publisher><availability><p>ELSEVIER</p></availability><date>1995</date></publicationStmt><notesStmt><note type="content">Section title: Research report</note></notesStmt><sourceDesc><biblStruct type="inbook"><analytic><title level="a" type="main" xml:lang="en">Quantitation of Alzheimer's amyloid peptide and identification of related amyloid proteins by dot-blot immunoassay</title><author xml:id="author-1"><persName><forename type="first">Bruno</forename><surname>Permanne</surname></persName><affiliation>INSERM U422, Place de Verdun, 59045 Lille Cedex, France</affiliation></author><author xml:id="author-2"><persName><forename type="first">Luc</forename><surname>Buée</surname></persName><affiliation>Corresponding author. Fax: (33) 2052-3794; or (33) 2062-2061.</affiliation><affiliation>INSERM U422, Place de Verdun, 59045 Lille Cedex, France</affiliation></author><author xml:id="author-3"><persName><forename type="first">Jean-Philippe</forename><surname>David</surname></persName><affiliation>INSERM U422, Place de Verdun, 59045 Lille Cedex, France</affiliation><affiliation>Hôpital Emile Roux, Avenue de Verdun, 94450 Limeil-Brévannes, France</affiliation></author><author xml:id="author-4"><persName><forename type="first">Catherine</forename><surname>Fallet-Bianco</surname></persName><affiliation>Hôpital Emile Roux, Avenue de Verdun, 94450 Limeil-Brévannes, France</affiliation></author><author xml:id="author-5"><persName><forename type="first">Claude</forename><surname>Di Menza</surname></persName><affiliation>Hôpital Emile Roux, Avenue de Verdun, 94450 Limeil-Brévannes, France</affiliation></author><author xml:id="author-6"><persName><forename type="first">André</forename><surname>Delacourte</surname></persName><affiliation>INSERM U422, Place de Verdun, 59045 Lille Cedex, France</affiliation></author></analytic><monogr><title level="j">Brain Research</title><title level="j" type="abbrev">BRES</title><idno type="pISSN">0006-8993</idno><idno type="PII">S0006-8993(00)X0050-9</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="1995"></date><biblScope unit="volume">685</biblScope><biblScope unit="issue">1–2</biblScope><biblScope unit="page" from="154">154</biblScope><biblScope unit="page" to="162">162</biblScope></imprint></monogr><idno type="istex">B8401D072C64B3BB7B811CBB9F6126FB98E98D9F</idno><idno type="DOI">10.1016/0006-8993(95)00431-O</idno><idno type="PII">0006-8993(95)00431-O</idno><idno type="ArticleID">9500431O</idno></biblStruct></sourceDesc></fileDesc><profileDesc><creation><date>1995</date></creation><langUsage><language ident="en">en</language></langUsage><abstract xml:lang="en"><p>In Alzheimer's disease, the main component of amyloid deposits is a 39–43 amino acid peptide referred to as amyloid peptide or A β. A crucial issue in the study of this disorder is to define the sequence of events that lead to amyloid deposition. In the present study, a new approach was developed that allows to specifically solubilize A β peptide trapped within amyloid deposits and to quantify its amount by dot-blot immunoassay. The present method also permits to isolate components tightly bound to A β and that are likely to catalyze its aggregation. Biochemical A β quantitation was performed in 4 Brodmann areas from 17 elderly individuals exhibiting different degrees of amyloidosis. In parallel, classical neuropathology was done by histochemical and immunohistochemical methods. A β amounts (pmol) were correlated to the number of amyloid deposits determined by neuropathology showing high statistical significance. Moreover, amyloid-binding proteins including apolipoprotein E and heparan sulfate proteoglycans were also found associated to A β in the amyloid preparation. The present biochemical procedure is a new and reliable method to quantify amyloid deposition in brain. Furthermore, it allows to detect amyloid-associated components such as apolipoprotein E, that may be involved in the pathological process of amyloidogenesis.</p></abstract><textClass xml:lang="en"><keywords scheme="keyword"><list><head>Keywords</head><item><term>Aging</term></item><item><term>Amyloidosis</term></item><item><term>Apolipoprotein E</term></item><item><term>Neuropathology</term></item><item><term>Proteoglycans</term></item></list></keywords></textClass></profileDesc><revisionDesc><change when="1995">Published</change></revisionDesc></teiHeader></istex:fulltextTEI><json:item><extension>txt</extension><original>false</original><mimetype>text/plain</mimetype><uri>https://api.istex.fr/document/B8401D072C64B3BB7B811CBB9F6126FB98E98D9F/fulltext/txt</uri></json:item></fulltext><metadata><istex:metadataXml wicri:clean="Elsevier, elements deleted: tail"><istex:xmlDeclaration>version="1.0" encoding="UTF-8"</istex:xmlDeclaration><istex:docType PUBLIC="-//ES//DTD journal article DTD version 4.5.2//EN//XML" URI="art452.dtd" name="istex:docType"></istex:docType><istex:document><converted-article version="4.5.2" docsubtype="fla" xml:lang="en"><item-info><jid>BRES</jid><aid>9500431O</aid><ce:pii>0006-8993(95)00431-O</ce:pii><ce:doi>10.1016/0006-8993(95)00431-O</ce:doi><ce:copyright type="unknown" year="1995"></ce:copyright></item-info><head><ce:dochead><ce:textfn>Research report</ce:textfn></ce:dochead><ce:title>Quantitation of Alzheimer's amyloid peptide and identification of related amyloid proteins by dot-blot immunoassay</ce:title><ce:author-group><ce:author><ce:given-name>Bruno</ce:given-name><ce:surname>Permanne</ce:surname><ce:cross-ref refid="AFF1"><ce:sup loc="post">a</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>Luc</ce:given-name><ce:surname>Buée</ce:surname><ce:cross-ref refid="COR1"><ce:sup loc="post">∗</ce:sup></ce:cross-ref><ce:cross-ref refid="AFF1"><ce:sup loc="post">a</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>Jean-Philippe</ce:given-name><ce:surname>David</ce:surname><ce:cross-ref refid="AFF1"><ce:sup loc="post">a</ce:sup></ce:cross-ref><ce:cross-ref refid="AFF2"><ce:sup loc="post">b</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>Catherine</ce:given-name><ce:surname>Fallet-Bianco</ce:surname><ce:cross-ref refid="AFF2"><ce:sup loc="post">b</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>Claude</ce:given-name><ce:surname>Di Menza</ce:surname><ce:cross-ref refid="AFF2"><ce:sup loc="post">b</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>André</ce:given-name><ce:surname>Delacourte</ce:surname><ce:cross-ref refid="AFF1"><ce:sup loc="post">a</ce:sup></ce:cross-ref></ce:author><ce:affiliation id="AFF1"><ce:label>a</ce:label><ce:textfn>INSERM U422, Place de Verdun, 59045 Lille Cedex, France</ce:textfn></ce:affiliation><ce:affiliation id="AFF2"><ce:label>b</ce:label><ce:textfn>Hôpital Emile Roux, Avenue de Verdun, 94450 Limeil-Brévannes, France</ce:textfn></ce:affiliation><ce:correspondence id="COR1"><ce:label>∗</ce:label><ce:text>Corresponding author. Fax: (33) 2052-3794; or (33) 2062-2061.</ce:text></ce:correspondence></ce:author-group><ce:date-accepted day="21" month="3" year="1995"></ce:date-accepted><ce:abstract class="author"><ce:section-title>Abstract</ce:section-title><ce:abstract-sec><ce:simple-para view="all" id="simple-para.0010">In Alzheimer's disease, the main component of amyloid deposits is a 39–43 amino acid peptide referred to as amyloid peptide or A β. A crucial issue in the study of this disorder is to define the sequence of events that lead to amyloid deposition. In the present study, a new approach was developed that allows to specifically solubilize A β peptide trapped within amyloid deposits and to quantify its amount by dot-blot immunoassay. The present method also permits to isolate components tightly bound to A β and that are likely to catalyze its aggregation. Biochemical A β quantitation was performed in 4 Brodmann areas from 17 elderly individuals exhibiting different degrees of amyloidosis. In parallel, classical neuropathology was done by histochemical and immunohistochemical methods. A β amounts (pmol) were correlated to the number of amyloid deposits determined by neuropathology showing high statistical significance. Moreover, amyloid-binding proteins including apolipoprotein E and heparan sulfate proteoglycans were also found associated to A β in the amyloid preparation. The present biochemical procedure is a new and reliable method to quantify amyloid deposition in brain. Furthermore, it allows to detect amyloid-associated components such as apolipoprotein E, that may be involved in the pathological process of amyloidogenesis.</ce:simple-para></ce:abstract-sec></ce:abstract><ce:keywords class="keyword"><ce:section-title>Keywords</ce:section-title><ce:keyword><ce:text>Aging</ce:text></ce:keyword><ce:keyword><ce:text>Amyloidosis</ce:text></ce:keyword><ce:keyword><ce:text>Apolipoprotein E</ce:text></ce:keyword><ce:keyword><ce:text>Neuropathology</ce:text></ce:keyword><ce:keyword><ce:text>Proteoglycans</ce:text></ce:keyword></ce:keywords></head></converted-article></istex:document></istex:metadataXml><mods version="3.6"><titleInfo lang="en"><title>Quantitation of Alzheimer's amyloid peptide and identification of related amyloid proteins by dot-blot immunoassay</title></titleInfo><titleInfo type="alternative" lang="en" contentType="CDATA"><title>Quantitation of Alzheimer's amyloid peptide and identification of related amyloid proteins by dot-blot immunoassay</title></titleInfo><name type="personal"><namePart type="given">Bruno</namePart><namePart type="family">Permanne</namePart><affiliation>INSERM U422, Place de Verdun, 59045 Lille Cedex, France</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Luc</namePart><namePart type="family">Buée</namePart><affiliation>Corresponding author. Fax: (33) 2052-3794; or (33) 2062-2061.</affiliation><affiliation>INSERM U422, Place de Verdun, 59045 Lille Cedex, France</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Jean-Philippe</namePart><namePart type="family">David</namePart><affiliation>INSERM U422, Place de Verdun, 59045 Lille Cedex, France</affiliation><affiliation>Hôpital Emile Roux, Avenue de Verdun, 94450 Limeil-Brévannes, France</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Catherine</namePart><namePart type="family">Fallet-Bianco</namePart><affiliation>Hôpital Emile Roux, Avenue de Verdun, 94450 Limeil-Brévannes, France</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Claude</namePart><namePart type="family">Di Menza</namePart><affiliation>Hôpital Emile Roux, Avenue de Verdun, 94450 Limeil-Brévannes, France</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">André</namePart><namePart type="family">Delacourte</namePart><affiliation>INSERM U422, Place de Verdun, 59045 Lille Cedex, France</affiliation><role><roleTerm type="text">author</roleTerm></role></name><typeOfResource>text</typeOfResource><genre type="research-article" displayLabel="Full-length article"></genre><originInfo><publisher>ELSEVIER</publisher><dateIssued encoding="w3cdtf">1995</dateIssued><copyrightDate encoding="w3cdtf">1995</copyrightDate></originInfo><language><languageTerm type="code" authority="iso639-2b">eng</languageTerm><languageTerm type="code" authority="rfc3066">en</languageTerm></language><physicalDescription><internetMediaType>text/html</internetMediaType></physicalDescription><abstract lang="en">In Alzheimer's disease, the main component of amyloid deposits is a 39–43 amino acid peptide referred to as amyloid peptide or A β. A crucial issue in the study of this disorder is to define the sequence of events that lead to amyloid deposition. In the present study, a new approach was developed that allows to specifically solubilize A β peptide trapped within amyloid deposits and to quantify its amount by dot-blot immunoassay. The present method also permits to isolate components tightly bound to A β and that are likely to catalyze its aggregation. Biochemical A β quantitation was performed in 4 Brodmann areas from 17 elderly individuals exhibiting different degrees of amyloidosis. In parallel, classical neuropathology was done by histochemical and immunohistochemical methods. A β amounts (pmol) were correlated to the number of amyloid deposits determined by neuropathology showing high statistical significance. Moreover, amyloid-binding proteins including apolipoprotein E and heparan sulfate proteoglycans were also found associated to A β in the amyloid preparation. The present biochemical procedure is a new and reliable method to quantify amyloid deposition in brain. Furthermore, it allows to detect amyloid-associated components such as apolipoprotein E, that may be involved in the pathological process of amyloidogenesis.</abstract><note type="content">Section title: Research report</note><subject lang="en"><genre>Keywords</genre><topic>Aging</topic><topic>Amyloidosis</topic><topic>Apolipoprotein E</topic><topic>Neuropathology</topic><topic>Proteoglycans</topic></subject><relatedItem type="host"><titleInfo><title>Brain Research</title></titleInfo><titleInfo type="abbreviated"><title>BRES</title></titleInfo><genre type="journal">journal</genre><originInfo><dateIssued encoding="w3cdtf">19950710</dateIssued></originInfo><identifier type="ISSN">0006-8993</identifier><identifier type="PII">S0006-8993(00)X0050-9</identifier><part><date>19950710</date><detail type="volume"><number>685</number><caption>vol.</caption></detail><detail type="issue"><number>1–2</number><caption>no.</caption></detail><extent unit="issue pages"><start>1</start><end>238</end></extent><extent unit="pages"><start>154</start><end>162</end></extent></part></relatedItem><identifier type="istex">B8401D072C64B3BB7B811CBB9F6126FB98E98D9F</identifier><identifier type="DOI">10.1016/0006-8993(95)00431-O</identifier><identifier type="PII">0006-8993(95)00431-O</identifier><identifier type="ArticleID">9500431O</identifier><recordInfo><recordContentSource>ELSEVIER</recordContentSource></recordInfo></mods></metadata></istex></record>Pour manipuler ce document sous Unix (Dilib)
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