Cited by 777Alzheimer's disease research and treatmentsAntioxidant Activity and Oxidative StressDementia and Cognitive Impairment Research

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Increased Lipid Peroxidation Precedes Amyloid Plaque Formation in an Animal Model of Alzheimer Amyloidosis

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Praticò, Domenico, Uryu, Kunihiro, Leight, Susan, Trojanoswki, John Q., Lee, Virginia M.-Y.·2001·The Journal of Neuroscience

DOI 10.1523/jneurosci.21-12-04183.2001PMC PMC6762743

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Abstract

Oxidative stress is a key feature in the Alzheimer's disease (AD) brain and manifests as lipid peroxidation (LPO). Isoprostanes (iPs) are specific and sensitive markers of in vivo LPO. To determine whether amyloid beta (Abeta) deposition in vivo is associated with increased LPO, we examined iP levels in a transgenic mouse model (Tg2576) of AD amyloidosis. Urine, plasma, and brain tissues were collected from Tg2576 and littermate wild-type (WT) animals at different time points starting at 4 months of age and continuing until 18 months of age. Levels of urinary 8,12-iso-iPF(2alpha)-VI were higher in Tg2576 than in WT animals as early as 8 months of age and remained this high for the rest of the study. A similar pattern was observed for plasma levels of 8,12-iso-iPF(2alpha)-VI. Homogenates from the cerebral cortex and hippocampus of Tg2576 mice had higher levels of 8,12-iso-iPF(2alpha)-VI than those from WT mice starting at 8 months of age. In contrast, a surge of Abeta 1-40 and 1-42 levels as well as Abeta deposits in Tg2576 mouse brains occurred later, at 12 months of age. A direct correlation was observed between brain 8,12-iso-iPF(2alpha)-VI and Abeta 1-40 and 1-42. Because LPO precedes amyloid plaque formation in Tg2576 mice, this suggests that brain oxidative damage contributes to AD pathogenesis before Abeta accumulation in the AD brain.

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Correlative Memory Deficits, Aβ Elevation, and Amyloid Plaques in Transgenic Mice
Hsiao, K., Chapman, P., Nilsen, S., Eckman, C., Harigaya, Y., Younkin, S., Yang, F., & Cole, G. (1996) · Science · doi:10.1126/science.274.5284.99 · Cited by 4,210
The measurement and mechanism of lipid peroxidation in biological systems
Gutteridge, J. M. C., & Halliwell, B. B. (1990) · Trends in Biochemical Sciences · doi:10.1016/0968-0004(90)90206-q · Cited by 1,297
Age-Dependent Changes in Brain, CSF, and Plasma Amyloid β Protein in the Tg2576 Transgenic Mouse Model of Alzheimer's Disease
Kawarabayashi, T., Younkin, L. H., Saido, T. C., Shoji, M., Ashe, K. H., & Younkin, S. G. (2001) · The Journal of Neuroscience · doi:10.1523/jneurosci.21-02-00372.2001 · Cited by 1,053 · cited 4×
“Indeed, the recent demonstration of rare Ab plaques as well as scant amounts of formic acid-extractable Ab in 8-month-old Tg2576 mouse brains prompts cautious interpretation of our data with respect to whether LPO precedes or is linked to the initial stages of AD-like amyloidosis in Tg2576 mice ( Kawarabayashi et al.,…”
BackgroundInfluential
Antioxidants, Oxidative Stress, and Degenerative Neurological Disorders
Floyd, R. A. (1999) · Proceedings of The Society for Experimental Biology and Medicine · doi:10.1046/j.1525-1373.1999.d01-140.x · Cited by 828
Oxidative Alterations in Alzheimer's Disease
Markesbery, W. R., & Carney, J. M. (1999) · Brain Pathology · doi:10.1111/j.1750-3639.1999.tb00215.x · Cited by 789
Amyloid β Protein (Aβ) in Alzheimeri's Disease Brain
Gravina, S. A., Ho, L., Eckman, C. B., Long, K. E., Otvos, L., Younkin, L. H., Suzuki, N., & Younkin, S. G. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.13.7013 · Cited by 676
APPSW Transgenic Mice Develop Age-related Aβ Deposits and Neuropil Abnormalities, but no Neuronal Loss in CA1
IRIZARRY, M. C., MCNAMARA, M., FEDORCHAK, K., HSIAO, K., & HYMAN, B. T. (1997) · Journal of Neuropathology and Experimental Neurology · doi:10.1097/00005072-199709000-00002 · Cited by 649
Amyloid‐β Deposition in Alzheimer Transgenic Mice Is Associated with Oxidative Stress
Smith, M. A., Hirai, K., Hsiao, K., Pappolla, M. A., Harris, P. L. R., Siedlak, S. L., Tabaton, M., & Perry, G. L. (1998) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1998.70052212.x · Cited by 547
Age-related CNS disorder and early death in transgenic FVB/N mice overexpressing Alzheimer amyloid precursor proteins
Hsiao, K., Borchelt, D., Olson, K., Johannsdottir, R., Kitt, C. A., Yunis, W. S., Xu, S., Eckman, C., Younkin, S. G., Price, D., et al. (1995) · Neuron · doi:10.1016/0896-6273(95)90107-8 · Cited by 527
Non-enzymatically glycated tau in Alzheimer's disease induces neuronal oxidant stress resulting in cytokine gene expression and release of amyloid β-peptide
Yan, S. D., Yan, S. F., Chen, X., Fu, J., Chen, M., Kuppusamy, P., Smith, M. A., Perry, G., Godman, G. C., Nawroth, P., et al. (1995) · Nature Medicine · doi:10.1038/nm0795-693 · Cited by 406

Show all 24 references

Research works printed but not linked: 1

Pappolla, 1998, Evidence of oxidative stress and in vivo neurotoxicity of β-amyloid in a transgenic mouse model of Alzheimer's disease., Am J Pathol, 152, 871

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Authors: Praticò, D., Uryu, K., Leight, S., Trojanoswki, J. Q., & Lee, V. M.-Y.
Affiliations: University of Pennsylvania (US)
ORCID: Praticò, Domenico
Uryu, Kunihiro
Lee, Virginia M.-Y.
Venue: The Journal of Neuroscience
Publisher: Society for Neuroscience
Published: 2001-06-15
Volume: 21
Issue: 12
Pages: 4183-4187
ISSN: 0270-6474 (ISSN-L)
1529-2401
DOI: 10.1523/jneurosci.21-12-04183.2001
PMC: PMC6762743
OpenAlex: W1954454186
Cited by: 777
References: 24
Citations by year: 2026: 4 · 2025: 15 · 2024: 17 · 2023: 29 · 2022: 19 · 2021: 32 · 2020: 23 · 2019: 27 · 2018: 16 · 2017: 24 · 2016: 24 · 2015: 28 · 2014: 32 · 2013: 37 · 2012: 48
FWCI: 22.76
Type: journal article
Language: en
Open access: hybrid
doi.org
Licence: cc-by-nc-sa
creativecommons.org/licenses/by-nc-sa/4.0/ (vor, 183 d)
Locations: Journal of Neuroscience (publishedVersion, cc-by-nc-sa)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Funders: American Heart Association
National Institutes of Health (AG-11542)
National Institute on Aging (P01AG011542, AG 11542)
Topics: Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
Health Sciences › Medicine › Biochemistry (medical) › Antioxidant Activity and Oxidative Stress
Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
Keywords: lipid peroxidation, isoprostanes, amyloid-beta, amyloid plaques, Alzheimer's disease, Tg2576 mice, oxidative stress, Aβ40, amyloid-beta 42, brain oxidative damage, pathogenesis
MeSH terms: Aging, Alzheimer Disease, Amyloidosis, Animals, Brain, Cerebellum, Cerebral Cortex, Disease Models, Animal, Enzyme-Linked Immunosorbent Assay, Female, Hippocampus, Male, Mice, Transgenic, Peptide Fragments, Lipid Peroxidation, Dinoprost, Amyloid beta-Peptides, Mice, Plaque, Amyloid

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Increased Lipid Peroxidation Precedes Amyloid Plaque Formation in an Animal Model of Alzheimer Amyloidosis

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