Cited by 174Alzheimer's disease research and treatmentsNeuroinflammation and Neurodegeneration MechanismsDementia and Cognitive Impairment Research

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Intraneuronal pyroglutamate-Abeta 3–42 triggers neurodegeneration and lethal neurological deficits in a transgenic mouse model

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Wirths, Oliver, Breyhan, Henning, Cynis, Holger, Schilling, Stephan, Demuth, Hans-Ulrich, Bayer, Thomas A.·2009·Acta Neuropathologica

DOI 10.1007/s00401-009-0557-5PMC PMC2737116

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Abstract

It is well established that only a fraction of Abeta peptides in the brain of Alzheimer's disease (AD) patients start with N-terminal aspartate (Abeta(1D)) which is generated by proteolytic processing of amyloid precursor protein (APP) by BACE. N-terminally truncated and pyroglutamate modified Abeta starting at position 3 and ending with amino acid 42 [Abeta(3(pE)-42)] have been previously shown to represent a major species in the brain of AD patients. When compared with Abeta(1-42), this peptide has stronger aggregation propensity and increased toxicity in vitro. Although it is unknown which peptidases remove the first two N-terminal amino acids, the cyclization of Abeta at N-terminal glutamate can be catalyzed in vitro. Here, we show that Abeta(3(pE)-42) induces neurodegeneration and concomitant neurological deficits in a novel mouse model (TBA2 transgenic mice). Although TBA2 transgenic mice exhibit a strong neuronal expression of Abeta(3-42) predominantly in hippocampus and cerebellum, few plaques were found in the cortex, cerebellum, brain stem and thalamus. The levels of converted Abeta(3(pE)-42) in TBA2 mice were comparable to the APP/PS1KI mouse model with robust neuron loss and associated behavioral deficits. Eight weeks after birth TBA2 mice developed massive neurological impairments together with abundant loss of Purkinje cells. Although the TBA2 model lacks important AD-typical neuropathological features like tangles and hippocampal degeneration, it clearly demonstrates that intraneuronal Abeta(3(pE)-42) is neurotoxic in vivo.

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Alzheimer's Disease: Genes, Proteins, and Therapy
Selkoe, D. J. (2001) · Physiological Reviews · doi:10.1152/physrev.2001.81.2.741 · Cited by 6,063
Amyloid plaque core protein in Alzheimer disease and Down syndrome.
Masters, C. L., Simms, G., Weinman, N. A., Multhaup, G., McDonald, B. L., & Beyreuther, K. (1985) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.82.12.4245 · Cited by 4,431
Intraneuronal β-Amyloid Aggregates, Neurodegeneration, and Neuron Loss in Transgenic Mice with Five Familial Alzheimer's Disease Mutations: Potential Factors in Amyloid Plaque Formation
Oakley, H., Cole, S. L., Logan, S., Maus, E., Shao, P., Craft, J., Guillozet-Bongaarts, A., Ohno, M., Disterhoft, J., Van Eldik, L., et al. (2006) · The Journal of Neuroscience · doi:10.1523/jneurosci.1202-06.2006 · Cited by 3,530 · cited 2×
“deficits [2, 15, 21, 43, 48] and reduced brain volume [4] were evident in transgenic APP models.”
Background
Accelerated Alzheimer-type phenotype in transgenic mice carrying both mutant amyloid precursor protein and presenilin 1 transgenes
Holcomb, L., Gordon, M. N., McGowan, E., Yu, X., Benkovic, S., Jantzen, P., Wright, K., Saad, I., Mueller, R., Morgan, D., et al. (1998) · Nature Medicine · doi:10.1038/nm0198-097 · Cited by 1,386
Intraneuronal Aβ Causes the Onset of Early Alzheimer’s Disease-Related Cognitive Deficits in Transgenic Mice
Billings, L. M., Oddo, S., Green, K. N., McGaugh, J. L., & LaFerla, F. M. (2005) · Neuron · doi:10.1016/j.neuron.2005.01.040 · Cited by 1,294
Correlation Between Elevated Levels of Amyloid β-Peptide in the Brain and Cognitive Decline
Näslund, J. (2000) · JAMA · doi:10.1001/jama.283.12.1571 · Cited by 1,268
Plaque-independent disruption of neural circuits in Alzheimer’s disease mouse models
Hsia, A. Y., Masliah, E., McConlogue, L., Yu, G.-Q., Tatsuno, G., Hu, K., Kholodenko, D., Malenka, R. C., Nicoll, R. A., & Mucke, L. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.6.3228 · Cited by 1,123
BACE1 is the major β-secretase for generation of Aβ peptides by neurons
Cai, H., Wang, Y., McCarthy, D. B., Wen, H., Borchelt, D., Price, D. L., & Wong, P. C. (2001) · Nature Neuroscience · doi:10.1038/85064 · Cited by 1,087
Intraneuronal Aβ42 Accumulation in Human Brain
Gouras, G. K., Tsai, J., Naslund, J., Vincent, B., Edgar, M., Checler, F., Greenfield, J. P., Haroutunian, V., Buxbaum, J. D., Xu, H., et al. (2000) · The American Journal of Pathology · doi:10.1016/s0002-9440(10)64700-1 · Cited by 991
Amyloid deposition precedes tangle formation in a triple transgenic model of Alzheimer's disease
Oddo, S. (2003) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2003.08.012 · Cited by 980

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Laumet, G. O. (2010) · theses.fr (ABES) · doi:10.70675/94126786zf990z488ezb471z5f1d5686766c
Influences biochimiques, anatomiques et cognitives de la troncation exopeptidasique N-terminale du peptide Aβ
Valverde, A. (2020) · theses.fr (ABES) · doi:10.70675/f1b70734zf4e3z4870z8fbdz950d831642a7
Contribution à l'étude des facteurs de risque pour la maladie d'Alzheimer : analyse de candidats identifiés par étude d'association pangénomique ou GWAS
Bauer, C. (2023) · theses.fr (ABES) · doi:10.70675/0d82043ezd7c7z4fb4z9fc8ze2d05d18b02b
Pathophysiological Characterization of intra‐ and extracellularly aggregated Amyloid Peptides in Dementias
Saul, A. (2013) · eDiss (Georg-August-Universität Göttingen) · doi:10.53846/goediss-3915

Authors: Wirths, O., Breyhan, H., Cynis, H., Schilling, S., Demuth, H.-U., & Bayer, T. A.
Affiliations: University of Göttingen (DE)
Probiodrug (Germany) (DE)
Corresponding author: Bayer, Thomas A.
ORCID: Wirths, Oliver
Cynis, Holger
Schilling, Stephan
Demuth, Hans-Ulrich
Bayer, Thomas A.
Venue: Acta Neuropathologica
Publisher: Springer Science and Business Media LLC
Published: 2009-06-23
Volume: 118
Issue: 4
Pages: 487-496
ISSN: 0001-6322 (ISSN-L)
1432-0533
DOI: 10.1007/s00401-009-0557-5
PMC: PMC2737116
OpenAlex: W2127458156
Cited by: 174
References: 71
Citations by year: 2026: 1 · 2025: 5 · 2024: 7 · 2023: 10 · 2022: 6 · 2021: 8 · 2020: 6 · 2019: 7 · 2018: 9 · 2017: 9 · 2016: 11 · 2015: 13 · 2014: 18 · 2013: 12 · 2012: 19
FWCI: 11.49
Type: journal article
Language: en
Open access: hybrid
doi.org
Licence: cc-by-nc
Locations: Acta Neuropathologica (publishedVersion, cc-by-nc)
Europe PMC (PubMed Central) (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
GoeScholar The Publication Server of the Georg-August-Universität Göttingen (Georg-August-Universität Göttingen) (submittedVersion, cc-by)
Funders: Alzheimer Forschung Initiative
European Commission (MEST-CT-2005-020013)
Topics: Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
Keywords: pyroglutamate amyloid-beta, Alzheimer's disease, neurodegeneration, Purkinje cell degeneration, neurotoxicity, neurological deficit, amyloid precursor protein, BACE, amyloid fibril formation, cerebellum
MeSH terms: Analysis of Variance, Animals, Body Weight, Brain, Brain Diseases, Enzyme-Linked Immunosorbent Assay, Immunohistochemistry, Mice, Transgenic, Nerve Degeneration, Neurons, Peptide Fragments, Phenotype, Purkinje Cells, Amyloid beta-Peptides, Cell Death, Mice

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Intraneuronal pyroglutamate-Abeta 3–42 triggers neurodegeneration and lethal neurological deficits in a transgenic mouse model

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