Apolipoprotein E (apoE) colocalizes with amyloid β-protein (Aβ) deposits lacking immunoreactivity against N-terminal epitopes in new-formed plaques

Thal, D. R., Capetillo-Zarate, E., Schultz, C., Rüb, U., Saido, T. C., Yamaguchi, H., Haass, C., Griffin, S. T., Braak, H. and Ghebremedhin, E. (2005). Apolipoprotein E (apoE) colocalizes with amyloid β-protein (Aβ) deposits lacking immunoreactivity against N-terminal epitopes in new-formed plaques. In: The 35th Annual Meeting of Neuroscience, Washington, DC, USA, (). 12-16 November 2005.


Author Thal, D. R.
Capetillo-Zarate, E.
Schultz, C.
Rüb, U.
Saido, T. C.
Yamaguchi, H.
Haass, C.
Griffin, S. T.
Braak, H.
Ghebremedhin, E.
Title of paper Apolipoprotein E (apoE) colocalizes with amyloid β-protein (Aβ) deposits lacking immunoreactivity against N-terminal epitopes in new-formed plaques
Conference name The 35th Annual Meeting of Neuroscience
Conference location Washington, DC, USA
Conference dates 12-16 November 2005
Publisher Society for Neuroscience
Publication Year 2005
Sub-type Poster
Language eng
Abstract/Summary Different types of senile plaques occur in brains of Alzheimer’s disease (AD) patients. Senile plaques seen in early preclinical stages of AD differ from those in clinical stages both in their composition of Aβ-peptides of different lengths and other proteins, e.g., apoE. ApoE is involved in Aβ-transport and -uptake. Therefore, it is tempting to speculate that apoE plays a role in senile plaque generation. To characterize the association between apoE and Aβ-peptides of different lengths and its impact on initial Aβ-deposition, we studied the medial temporal lobe of 60 autopsy cases encompassing the full spectrum of AD-related pathology as well as controls. Aβ-deposits in regions becoming newly involved in a given stage of β-amyloidosis exclusively consisted of new-formed plaques. In 36 cases, apoE was present in these new-formed plaques. Here, apoE was frequently co-localized with Aβ-deposits detectable with anti-Aβ42 but not with antibodies raised against N-terminal epitopes of Aβ. In contrast, immunoreactivity against apoE was completely absent in new-formed plaques of other cases where at the same time immunoreactivity against N-terminal epitopes of Aβ was present. The lacking co-localization of N-terminal epitopes of Aβ with apoE in new-formed plaques suggests that these deposits represent apoE-Aβ complexes in which the N-terminal epitopes of Aβ are often concealed after complexing with apoE, thus, preventing subsequent binding of antibodies.
Subjects 1103 Clinical Sciences
Keyword Alzheimer
Amyloid
Apolipoprotein E
Neuropathology
Q-Index Code EX
Q-Index Status Provisional Code
Institutional Status Unknown
Additional Notes Presentation Number: 704.5

 
Versions
Version Filter Type
Citation counts: Google Scholar Search Google Scholar
Access Statistics: 46 Abstract Views  -  Detailed Statistics
Created: Wed, 03 Mar 2010, 11:35:57 EST by Laura McTaggart on behalf of Faculty of Science