Neurofibrillary tangles of Guam parkinson-dementia are associated with reactive microglia and complement proteins.
Identifieur interne : 004358 ( Main/Merge ); précédent : 004357; suivant : 004359Neurofibrillary tangles of Guam parkinson-dementia are associated with reactive microglia and complement proteins.
Auteurs : C. Schwab [Canada] ; J C Steele ; P L McgeerSource :
- Brain research [ 0006-8993 ] ; 1996.
English descriptors
- KwdEn :
- Adult, Aged, Aged, 80 and over, Amyloid beta-Peptides (metabolism), Amyotrophic Lateral Sclerosis (pathology), Astrocytes (physiology), Brain (pathology), Complement Pathway, Classical, Complement System Proteins (metabolism), Dementia (pathology), Female, Guam, Humans, Immunohistochemistry, Male, Microglia (physiology), Middle Aged, Neurofibrillary Tangles (pathology), Parkinson Disease (pathology), Syndrome.
- MESH :
- chemical , metabolism : Amyloid beta-Peptides, Complement System Proteins.
- geographic : Guam.
- pathology : Amyotrophic Lateral Sclerosis, Brain, Dementia, Neurofibrillary Tangles, Parkinson Disease.
- physiology : Astrocytes, Microglia.
- Adult, Aged, Aged, 80 and over, Complement Pathway, Classical, Female, Humans, Immunohistochemistry, Male, Middle Aged, Syndrome.
Abstract
Guamanian parkinsonism-dementia, locally described as bodig, is characterized by the widespread appearance of neurofibrillary tangles in cortical and subcortical areas. These tangles have similar regional distribution and immunohistochemical profile to those found in Alzheimer disease (AD). We studied the immunohistochemical staining of these tangles, as well as those of AD, using antibodies to complement proteins and related molecules. In bodig, as in AD, extracellular tangles were intensely decorated with antibodies to C1q, C4d and C3d, but not fraction Bb of factor B, properidin or immunoglobulins. This is evidence that the classical, but not the alternative complement pathway is activated on extracellular tangles and that the activation is independent of antibodies. Immunohistochemical staining for amyloid P, an in vitro activator of complement, was remarkably similar to that for the C1q, C4d and C3d in both bodig and AD. This was not the case for beta-amyloid protein (BAP), another in vitro complement activator. Positive staining was observed in only a minority of extracellular tangles in bodig and was only rarely observed in those of AD. BAP would therefore not appear to be a candidate for activating complement on extracellular neurofibrillary tangles. Reactive microglia and reactive astrocytes were closely associated with complement positive extracellular neurofibrillary tangles, indicating an inflammatory response similar to that seen in AD.
PubMed: 8919296
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pubmed:8919296Le document en format XML
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<affiliation wicri:level="1"><nlm:affiliation>Kinsmen Laboratory of Neurological Research and the Neurodegenerative Disorders Centre, University of British Columbia, Vancouver, Canada.</nlm:affiliation>
<country xml:lang="fr">Canada</country>
<wicri:regionArea>Kinsmen Laboratory of Neurological Research and the Neurodegenerative Disorders Centre, University of British Columbia, Vancouver</wicri:regionArea>
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<author><name sortKey="Steele, J C" sort="Steele, J C" uniqKey="Steele J" first="J C" last="Steele">J C Steele</name>
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<author><name sortKey="Mcgeer, P L" sort="Mcgeer, P L" uniqKey="Mcgeer P" first="P L" last="Mcgeer">P L Mcgeer</name>
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<sourceDesc><biblStruct><analytic><title xml:lang="en">Neurofibrillary tangles of Guam parkinson-dementia are associated with reactive microglia and complement proteins.</title>
<author><name sortKey="Schwab, C" sort="Schwab, C" uniqKey="Schwab C" first="C" last="Schwab">C. Schwab</name>
<affiliation wicri:level="1"><nlm:affiliation>Kinsmen Laboratory of Neurological Research and the Neurodegenerative Disorders Centre, University of British Columbia, Vancouver, Canada.</nlm:affiliation>
<country xml:lang="fr">Canada</country>
<wicri:regionArea>Kinsmen Laboratory of Neurological Research and the Neurodegenerative Disorders Centre, University of British Columbia, Vancouver</wicri:regionArea>
<wicri:noRegion>Vancouver</wicri:noRegion>
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<author><name sortKey="Steele, J C" sort="Steele, J C" uniqKey="Steele J" first="J C" last="Steele">J C Steele</name>
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<author><name sortKey="Mcgeer, P L" sort="Mcgeer, P L" uniqKey="Mcgeer P" first="P L" last="Mcgeer">P L Mcgeer</name>
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<series><title level="j">Brain research</title>
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<imprint><date when="1996" type="published">1996</date>
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<term>Aged</term>
<term>Aged, 80 and over</term>
<term>Amyloid beta-Peptides (metabolism)</term>
<term>Amyotrophic Lateral Sclerosis (pathology)</term>
<term>Astrocytes (physiology)</term>
<term>Brain (pathology)</term>
<term>Complement Pathway, Classical</term>
<term>Complement System Proteins (metabolism)</term>
<term>Dementia (pathology)</term>
<term>Female</term>
<term>Guam</term>
<term>Humans</term>
<term>Immunohistochemistry</term>
<term>Male</term>
<term>Microglia (physiology)</term>
<term>Middle Aged</term>
<term>Neurofibrillary Tangles (pathology)</term>
<term>Parkinson Disease (pathology)</term>
<term>Syndrome</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Amyloid beta-Peptides</term>
<term>Complement System Proteins</term>
</keywords>
<keywords scheme="MESH" type="geographic" xml:lang="en"><term>Guam</term>
</keywords>
<keywords scheme="MESH" qualifier="pathology" xml:lang="en"><term>Amyotrophic Lateral Sclerosis</term>
<term>Brain</term>
<term>Dementia</term>
<term>Neurofibrillary Tangles</term>
<term>Parkinson Disease</term>
</keywords>
<keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>Astrocytes</term>
<term>Microglia</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Adult</term>
<term>Aged</term>
<term>Aged, 80 and over</term>
<term>Complement Pathway, Classical</term>
<term>Female</term>
<term>Humans</term>
<term>Immunohistochemistry</term>
<term>Male</term>
<term>Middle Aged</term>
<term>Syndrome</term>
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<front><div type="abstract" xml:lang="en">Guamanian parkinsonism-dementia, locally described as bodig, is characterized by the widespread appearance of neurofibrillary tangles in cortical and subcortical areas. These tangles have similar regional distribution and immunohistochemical profile to those found in Alzheimer disease (AD). We studied the immunohistochemical staining of these tangles, as well as those of AD, using antibodies to complement proteins and related molecules. In bodig, as in AD, extracellular tangles were intensely decorated with antibodies to C1q, C4d and C3d, but not fraction Bb of factor B, properidin or immunoglobulins. This is evidence that the classical, but not the alternative complement pathway is activated on extracellular tangles and that the activation is independent of antibodies. Immunohistochemical staining for amyloid P, an in vitro activator of complement, was remarkably similar to that for the C1q, C4d and C3d in both bodig and AD. This was not the case for beta-amyloid protein (BAP), another in vitro complement activator. Positive staining was observed in only a minority of extracellular tangles in bodig and was only rarely observed in those of AD. BAP would therefore not appear to be a candidate for activating complement on extracellular neurofibrillary tangles. Reactive microglia and reactive astrocytes were closely associated with complement positive extracellular neurofibrillary tangles, indicating an inflammatory response similar to that seen in AD.</div>
</front>
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