Biochemical staging of synucleinopathy and amyloid deposition in dementia with lewy bodies
Identifieur interne : 002B32 ( Main/Exploration ); précédent : 002B31; suivant : 002B33Biochemical staging of synucleinopathy and amyloid deposition in dementia with lewy bodies
Auteurs : V. Deramecourt [France] ; S. Bombois [France] ; C.-A. Maurage [France] ; A. Ghestem [France] ; H. Drobecq [France] ; E. Vanmechelen [Belgique] ; F. Lebert [France] ; F. Pasquier [France] ; A. Delacourte [France]Source :
- Journal of neuropathology and experimental neurology [ 0022-3069 ] ; 2006.
Descripteurs français
- Pascal (Inist)
English descriptors
- KwdEn :
- Aged, Aged, 80 and over, Alzheimer Disease (metabolism), Alzheimer Disease (pathology), Alzheimer disease, Amyloid, Amyloid beta-Protein Precursor (metabolism), Cerebral Cortex (anatomy & histology), Cerebral Cortex (metabolism), Cerebral Cortex (pathology), Deposition, Electrophoresis, Gel, Two-Dimensional, Female, Humans, Lewy Body Disease (metabolism), Lewy Body Disease (pathology), Lewy body dementia, Male, Mass Spectrometry, Middle Aged, Nervous system diseases, Parkinson Disease (metabolism), Parkinson Disease (pathology), alpha-Synuclein (metabolism), tau Proteins (metabolism).
- MESH :
- chemical , metabolism : Amyloid beta-Protein Precursor, alpha-Synuclein, tau Proteins.
- anatomy & histology : Cerebral Cortex.
- metabolism : Alzheimer Disease, Cerebral Cortex, Lewy Body Disease, Parkinson Disease.
- pathology : Alzheimer Disease, Cerebral Cortex, Lewy Body Disease, Parkinson Disease.
- Aged, Aged, 80 and over, Electrophoresis, Gel, Two-Dimensional, Female, Humans, Male, Mass Spectrometry, Middle Aged.
Abstract
The primary feature of dementia with Lewy bodies (DLB) is the aggregation of alpha-synuclein into characteristic lesions: Lewy bodies (LBs) and Lewy neurites. However, in most of DLB cases, LBs are associated with neurofibrillary tangles and amyloid plaques (both Alzheimer disease [AD]-related lesions). We wanted to determine if this overlap of lesions is statistical, as a result of the late onset of both diseases, or results from a specific physiopathological synergy between synucleinopathy and either tauopathy or amyloid pathology. All patients with DLB from our prospective and multidisciplinary study were analyzed. These cases were compared with cases with pure AD and patients with Parkinson disease and controls. All cases were analyzed thoroughly at the neuropathologic and biochemical levels with a biochemical staging of aggregated >-synuclein, tau, and AA species. All sporadic cases of DLB were associated with abundant deposits of AA x-42 that were similar in quality and quantity to those of AD. Amyloid precursor protein (APP) dysfunction is a risk factor for AD as demonstrated by pathogenic mutations and AA accumulation. The constant and abundant AA x-42 deposition in sporadic DLB suggests that synucleinopathy is also promoted by APP dysfunction. Therefore, we conclude that APP is a therapeutic target for both AD and DLB.
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Le document en format XML
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<term>Aged, 80 and over</term>
<term>Alzheimer Disease (metabolism)</term>
<term>Alzheimer Disease (pathology)</term>
<term>Alzheimer disease</term>
<term>Amyloid</term>
<term>Amyloid beta-Protein Precursor (metabolism)</term>
<term>Cerebral Cortex (anatomy & histology)</term>
<term>Cerebral Cortex (metabolism)</term>
<term>Cerebral Cortex (pathology)</term>
<term>Deposition</term>
<term>Electrophoresis, Gel, Two-Dimensional</term>
<term>Female</term>
<term>Humans</term>
<term>Lewy Body Disease (metabolism)</term>
<term>Lewy Body Disease (pathology)</term>
<term>Lewy body dementia</term>
<term>Male</term>
<term>Mass Spectrometry</term>
<term>Middle Aged</term>
<term>Nervous system diseases</term>
<term>Parkinson Disease (metabolism)</term>
<term>Parkinson Disease (pathology)</term>
<term>alpha-Synuclein (metabolism)</term>
<term>tau Proteins (metabolism)</term>
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<term>alpha-Synuclein</term>
<term>tau Proteins</term>
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<keywords scheme="MESH" qualifier="anatomy & histology" xml:lang="en"><term>Cerebral Cortex</term>
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<keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Alzheimer Disease</term>
<term>Cerebral Cortex</term>
<term>Lewy Body Disease</term>
<term>Parkinson Disease</term>
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<term>Aged, 80 and over</term>
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<front><div type="abstract" xml:lang="en">The primary feature of dementia with Lewy bodies (DLB) is the aggregation of alpha-synuclein into characteristic lesions: Lewy bodies (LBs) and Lewy neurites. However, in most of DLB cases, LBs are associated with neurofibrillary tangles and amyloid plaques (both Alzheimer disease [AD]-related lesions). We wanted to determine if this overlap of lesions is statistical, as a result of the late onset of both diseases, or results from a specific physiopathological synergy between synucleinopathy and either tauopathy or amyloid pathology. All patients with DLB from our prospective and multidisciplinary study were analyzed. These cases were compared with cases with pure AD and patients with Parkinson disease and controls. All cases were analyzed thoroughly at the neuropathologic and biochemical levels with a biochemical staging of aggregated >-synuclein, tau, and AA species. All sporadic cases of DLB were associated with abundant deposits of AA x-42 that were similar in quality and quantity to those of AD. Amyloid precursor protein (APP) dysfunction is a risk factor for AD as demonstrated by pathogenic mutations and AA accumulation. The constant and abundant AA x-42 deposition in sporadic DLB suggests that synucleinopathy is also promoted by APP dysfunction. Therefore, we conclude that APP is a therapeutic target for both AD and DLB.</div>
</front>
</TEI>
<affiliations><list><country><li>Belgique</li>
<li>France</li>
</country>
<region><li>Hauts-de-France</li>
<li>Nord-Pas-de-Calais</li>
</region>
<settlement><li>Lille</li>
</settlement>
</list>
<tree><country name="France"><region name="Hauts-de-France"><name sortKey="Deramecourt, V" sort="Deramecourt, V" uniqKey="Deramecourt V" first="V." last="Deramecourt">V. Deramecourt</name>
</region>
<name sortKey="Bombois, S" sort="Bombois, S" uniqKey="Bombois S" first="S." last="Bombois">S. Bombois</name>
<name sortKey="Delacourte, A" sort="Delacourte, A" uniqKey="Delacourte A" first="A." last="Delacourte">A. Delacourte</name>
<name sortKey="Drobecq, H" sort="Drobecq, H" uniqKey="Drobecq H" first="H." last="Drobecq">H. Drobecq</name>
<name sortKey="Ghestem, A" sort="Ghestem, A" uniqKey="Ghestem A" first="A." last="Ghestem">A. Ghestem</name>
<name sortKey="Lebert, F" sort="Lebert, F" uniqKey="Lebert F" first="F." last="Lebert">F. Lebert</name>
<name sortKey="Maurage, C A" sort="Maurage, C A" uniqKey="Maurage C" first="C.-A." last="Maurage">C.-A. Maurage</name>
<name sortKey="Maurage, C A" sort="Maurage, C A" uniqKey="Maurage C" first="C.-A." last="Maurage">C.-A. Maurage</name>
<name sortKey="Maurage, C A" sort="Maurage, C A" uniqKey="Maurage C" first="C.-A." last="Maurage">C.-A. Maurage</name>
<name sortKey="Pasquier, F" sort="Pasquier, F" uniqKey="Pasquier F" first="F." last="Pasquier">F. Pasquier</name>
</country>
<country name="Belgique"><noRegion><name sortKey="Vanmechelen, E" sort="Vanmechelen, E" uniqKey="Vanmechelen E" first="E." last="Vanmechelen">E. Vanmechelen</name>
</noRegion>
</country>
</tree>
</affiliations>
</record>
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