Article (Scientific journals)
Truncated and modified amyloid-beta species.
Kummer, Markus P; HENEKA, Michael
2014In Alzheimer's Research and Therapy, 6 (3), p. 28
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Keywords :
Neurology; Neurology (clinical); Cognitive Neuroscience
Abstract :
[en] Alzheimer's disease pathology is closely connected to the processing of the amyloid precursor protein (APP) resulting in the formation of a variety of amyloid-beta (Aβ) peptides. They are found as insoluble aggregates in senile plaques, the histopathological hallmark of the disease. These peptides are also found in soluble, mostly monomeric and dimeric, forms in the interstitial and cerebrospinal fluid. Due to the combination of several enzymatic activities during APP processing, Aβ peptides exist in multiple isoforms possessing different N-termini and C-termini. These peptides include, to a certain extent, part of the juxtamembrane and transmembrane domain of APP. Besides differences in size, post-translational modifications of Aβ - including oxidation, phosphorylation, nitration, racemization, isomerization, pyroglutamylation, and glycosylation - generate a plethora of peptides with different physiological and pathological properties that may modulate disease progression.
Disciplines :
Neurology
Author, co-author :
Kummer, Markus P;  Department of Neurology, University Hospital Bonn, Sigmund-Freud-Strasse 25, 53127 Bonn, Germany
HENEKA, Michael  ;  Department of Neurology, University Hospital Bonn, Sigmund-Freud-Strasse 25, 53127 Bonn, Germany , German Center for Neurodegenerative Diseases (DZNE), Holbeinstrasse 15, 53117 Bonn, Germany
External co-authors :
yes
Language :
English
Title :
Truncated and modified amyloid-beta species.
Publication date :
2014
Journal title :
Alzheimer's Research and Therapy
eISSN :
1758-9193
Publisher :
BioMed Central Ltd., England
Volume :
6
Issue :
3
Pages :
28
Peer reviewed :
Peer Reviewed verified by ORBi
Funding text :
The authors would like to thank Catherine Widmann, Dr Sascha Weggen and Dr Claus Pietrzik for discussion. This study was supported by the Deutsche Forschungsgemeinschaft (KFO177, TP4) to MTH and by grants of the INMiND project of the European Union to MTH. MTH is member of the DFG Cluster of Excellence ImmunoSensation.
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