Apolipoprotein E co-localizes with newly formed amyloid β-protein (Aβ) deposits lacking immunoreactivity against N-terminal epitopes of Aβ in a genotype-dependent ... View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2005-09-30

AUTHORS

Dietmar Rudolf Thal, Estibaliz Capetillo-Zarate, Christian Schultz, Udo Rüb, Takaomi C. Saido, Haruyasu Yamaguchi, Christian Haass, W. Sue T. Griffin, Kelly Del Tredici, Heiko Braak, Estifanos Ghebremedhin

ABSTRACT

Different types of amyloid β-protein (Aβ)-containing plaques occur in brains of Alzheimer’s disease (AD) patients. Diffuse plaques seen during early stages of AD differ from neuritic plaques in later stages both with respect to the length of the Aβ peptides and the presence of other proteins, e.g., apolipoprotein-E (apoE). Since apoE is involved in Aβ transport and clearance, and the ε4-allele of the apolipoprotein-E gene (APOE) is a major risk factor for sporadic AD, it is plausible to speculate that apoE plays a pathophysiological role in the initiation of Aβ deposition. To address the issue of whether binding of apoE to Aβ is involved in initial Aβ deposition, we studied the human medial temporal lobe of 60 autopsy cases encompassing the full spectrum of AD-related pathology. In temporal lobe regions, which become involved for the first time at a given stage of β-amyloidosis, all plaques represent newly formed plaques, and these were studied with immunohistochemical methods. ApoE was present in 36 cases, and was frequently co-localized with newly formed Aβ deposits detectable with anti-Aβ42 but not with antibodies raised against N-terminal epitopes of Aβ. In 10 additional cases, immunoreactivity against apoE was completely lacking in newly formed plaques, which, at the same time, displayed immunoreactivity against N-terminal epitopes of Aβ. The failure of N-terminal epitopes of Aβ to co-localize with apoE in newly formed plaques indicates that these deposits presumably contain apoE-Aβ complexes, in which the N-terminal epitopes of Aβ are often concealed after complexing with apoE, thus preventing subsequent binding of antibodies. Moreover, apoE-positive newly formed plaques were seen more frequently in APOE ε4/4 cases than in non-APOE ε4/4 individuals, thereby underlining the potentially crucial role of apoE for the development of Aβ deposits. More... »

PAGES

459-471

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/s00401-005-1053-1

DOI

http://dx.doi.org/10.1007/s00401-005-1053-1

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1046041301

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/16195918


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33 schema:description Different types of amyloid β-protein (Aβ)-containing plaques occur in brains of Alzheimer’s disease (AD) patients. Diffuse plaques seen during early stages of AD differ from neuritic plaques in later stages both with respect to the length of the Aβ peptides and the presence of other proteins, e.g., apolipoprotein-E (apoE). Since apoE is involved in Aβ transport and clearance, and the ε4-allele of the apolipoprotein-E gene (APOE) is a major risk factor for sporadic AD, it is plausible to speculate that apoE plays a pathophysiological role in the initiation of Aβ deposition. To address the issue of whether binding of apoE to Aβ is involved in initial Aβ deposition, we studied the human medial temporal lobe of 60 autopsy cases encompassing the full spectrum of AD-related pathology. In temporal lobe regions, which become involved for the first time at a given stage of β-amyloidosis, all plaques represent newly formed plaques, and these were studied with immunohistochemical methods. ApoE was present in 36 cases, and was frequently co-localized with newly formed Aβ deposits detectable with anti-Aβ42 but not with antibodies raised against N-terminal epitopes of Aβ. In 10 additional cases, immunoreactivity against apoE was completely lacking in newly formed plaques, which, at the same time, displayed immunoreactivity against N-terminal epitopes of Aβ. The failure of N-terminal epitopes of Aβ to co-localize with apoE in newly formed plaques indicates that these deposits presumably contain apoE-Aβ complexes, in which the N-terminal epitopes of Aβ are often concealed after complexing with apoE, thus preventing subsequent binding of antibodies. Moreover, apoE-positive newly formed plaques were seen more frequently in APOE ε4/4 cases than in non-APOE ε4/4 individuals, thereby underlining the potentially crucial role of apoE for the development of Aβ deposits.
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41 AD-related pathology
42 Alzheimer's disease patients
43
44 Aβ deposition
45 Aβ deposits
46 Aβ peptides
47 Aβ transport
48 additional cases
49 amyloid β
50 amyloidosis
51 antibodies
52 apoE
53 apolipoprotein E
54 apolipoproteins
55 autopsy cases
56 binding
57 binding of apoE
58 brain
59 cases
60 clearance
61 complexes
62 crucial role
63 deposition
64 deposits
65 development
66 different types
67 diffuse plaques
68 disease patients
69 early stages
70 epitopes
71 factors
72 failure
73 first time
74 full spectrum
75 genes
76 genotype-dependent manner
77 human medial temporal lobe
78 immunohistochemical methods
79 immunoreactivity
80 individuals
81 initiation
82 issues
83 later stages
84 length
85 lobe
86 lobe regions
87 major risk factor
88 manner
89 medial temporal lobe
90 method
91 neuritic plaques
92 pathology
93 pathophysiological role
94 patients
95 peptides
96 plaques
97 presence
98 protein
99 protein deposits
100 region
101 respect
102 risk factors
103 role
104 same time
105 spectra
106 sporadic AD
107 stage
108 subsequent binding
109 temporal lobe
110 temporal lobe regions
111 terminal epitope
112 time
113 transport
114 types
115 ε4 allele
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