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.
English descriptors
- KwdEn :
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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<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>
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<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>
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<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>
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<item><term>Aging</term>
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<item><term>Amyloidosis</term>
</item>
<item><term>Apolipoprotein E</term>
</item>
<item><term>Neuropathology</term>
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<head><ce:dochead><ce:textfn>Research report</ce:textfn>
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<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>
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<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>
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<ce:cross-ref refid="AFF1"><ce:sup loc="post">a</ce:sup>
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<ce:author><ce:given-name>Jean-Philippe</ce:given-name>
<ce:surname>David</ce:surname>
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<ce:author><ce:given-name>Catherine</ce:given-name>
<ce:surname>Fallet-Bianco</ce:surname>
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<ce:author><ce:given-name>Claude</ce:given-name>
<ce:surname>Di Menza</ce:surname>
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<ce:author><ce:given-name>André</ce:given-name>
<ce:surname>Delacourte</ce:surname>
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<ce:textfn>INSERM U422, Place de Verdun, 59045 Lille Cedex, France</ce:textfn>
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<ce:affiliation id="AFF2"><ce:label>b</ce:label>
<ce:textfn>Hôpital Emile Roux, Avenue de Verdun, 94450 Limeil-Brévannes, France</ce:textfn>
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<ce:correspondence id="COR1"><ce:label>∗</ce:label>
<ce:text>Corresponding author. Fax: (33) 2052-3794; or (33) 2062-2061.</ce:text>
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<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>
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<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>
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<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>
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<topic>Aging</topic>
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<topic>Neuropathology</topic>
<topic>Proteoglycans</topic>
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