Alzheimer's research & therapyOct 6, 2017

Shortened Aβ4-x peptides in typical Alzheimer's disease and mouse models

Longevity & Aging Weekly Brief ↗PubMed ↗DOI ↗

Updated Apr 4, 2026

Abstract

Amyloid-β staining was primarily found in amyloid plaque cores and in cerebral blood vessels in brains affected by Alzheimer's disease and Down syndrome.

N-terminally truncated amyloid-β peptides may play a significant role in the aggregation process leading to plaque formation.
Immunohistochemical analysis revealed that staining for these peptides was concentrated in specific areas associated with amyloid pathology.
Diffuse amyloid deposits showed little to no reactivity for the newly developed antibodies targeting truncated amyloid-β species.
No significant staining was detected within neurons, indicating that the amyloid-β peptides are primarily localized outside of neuronal cells.

Simplified

BACKGROUND: The deposition of neurotoxic amyloid-β (Aβ) peptides in plaques in the brain parenchyma and in cerebral blood vessels is considered to be a key event in Alzheimer's disease (AD) pathogenesis. Although the presence and impact of full-length Aβ peptides such as Aβand Aβhave been analyzed extensively, the deposition of N-terminally truncated Aβ peptide species has received much less attention, largely because of the lack of specific antibodies. 1-40 1-42

METHODS: This paper describes the generation and characterization of novel antibodies selective for Aβpeptides and provides immunohistochemical evidence of Aβin the human brain and its distribution in the APP/PS1KI and 5XFAD transgenic mouse models. 4-x4-x

RESULTS: The Aβstaining pattern was restricted mainly to amyloid plaque cores and cerebral amyloid angiopathy in AD and Down syndrome cases and in both AD mouse models. In contrast, diffuse amyloid deposits were largely negative for Aβimmunoreactivity. No overt intraneuronal staining was observed. 4-x4-x

CONCLUSIONS: The findings of this study are consistent with previous reports demonstrating a high aggregation propensity of Aβpeptides and suggest an important role of these N-truncated Aβ species in the process of amyloidogenesis and plaque core formation. 4-x

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Competing interests

ETHICS APPROVAL AND CONSENT TO PARTICIPATE: All procedures involving human tissue were approved by the ethics committee of the University Medical Center Göttingen (protocol number 12/1/15). All tissues were received from the Netherlands Brain Bank (NBB), and all materials and data collected by the NBB are obtained on the basis of written informed consent. All experimental procedures in the study that involved animals were approved by the institutional animal care and use committee at University Medicine Göttingen. CONSENT FOR PUBLICATION: All authors gave consent for publication. COMPETING INTERESTS: The authors declare that they have no competing interests. PUBLISHER’S NOTE: Springer Nature remains neutral with regard to jurisdictional claims in published maps and institutional affiliations.

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Shortened Aβ4-x peptides in typical Alzheimer's disease and mouse models

Abstract

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Competing interests

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