C-terminally truncated Amyloid-β peptides in Alzheimer’s dementia: Deposition of Aβ37, Aβ38, and Aβ39 in the brains of patients with sporadic and familiar Alzheimer’s dementia and in transgenic mouse models.

by Jochim Reinert
Doctoral thesis
Date of Examination:2018-01-25
Date of issue:2018-01-24
Advisor:Prof. Dr. Oliver Wirths
Referee:Prof. Dr. Oliver Wirths
Referee:Prof. Dr. Christine Stadelmann-Nessler
Persistent Address: http://dx.doi.org/10.53846/goediss-6699

 

 

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Abstract

English

Alzheimer's dementia is a devastating neurodegenerative disease characterized by profound neuropathological changes of the brain. Imbalances in the production of aggregation-prone Amyloid-Beta Peptides are believed to play a pivotal role in disease pathogenesis. These peptides are generated by subsequent proteolysis of the Amyloid Precursor Protein by a Beta and a Gamma-Sekretase. This Proteolysis yields peptides of differing length with varying C-termini. While the presumably most toxic species Abeta42 and the most produced species Abeta40 have been subject to intensive research, C-terminally truncated Peptides have not received much attention. This study investigates the contribution of Abeta37, Abeta38, and Abeta39 to the neuropathological changes in sporadic and familial Alzheimer's dementia. C-terminally truncated Abeta peptides were found to be deposited primarily to the vasculature in sporadic cases, while familial cases presented more intense depositions that included neuritic plaques. Moreover, this study analyzed commonly employed transgenic mouse models for depositions of the C-terminally truncated Abeta peptides.
Keywords: Alzheimer's dementia; Cerebral amyloid angiopathy; Abeta38; Abeta37; Abeta39
 
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