Cited by 684Parkinson's Disease Mechanisms and TreatmentsNuclear Receptors and SignalingNeuroinflammation and Neurodegeneration Mechanisms

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Parkinson's Disease α-Synuclein Transgenic Mice Develop Neuronal Mitochondrial Degeneration and Cell Death

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Martin, Lee J., Pan, Yan, Price, Ann C., Sterling, Wanda, Copeland, Neal G., Jenkins, Nancy A., Price, Donald L., Lee, Michael K.·2006·The Journal of Neuroscience

DOI 10.1523/jneurosci.4308-05.2006PMC PMC6381830

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Abstract

α-Synuclein (α-Syn) is enriched in nerve terminals. Two mutations in the α-Syn gene (Ala53→ Thr and Ala30→ Pro) occur in autosomal dominant familial Parkinson's disease. Mice overexpressing the human A53T mutant α-Syn develop a severe movement disorder, paralysis, and synucleinopathy, but the mechanisms are not understood. We examined whether transgenic mice expressing human wild-type or familial Parkinson's disease-linked A53T or A30P mutant α-syn develop neuronal degeneration and cell death. Mutant mice were examined at early- to mid-stage disease and at near end-stage disease. Age-matched nontransgenic littermates were controls. In A53T mice, neurons in brainstem and spinal cord exhibited large axonal swellings, somal chromatolytic changes, and nuclear condensation. Spheroid eosinophilic Lewy body-like inclusions were present in the cytoplasm of cortical neurons and spinal motor neurons. These inclusions contained human α-syn and nitrated synuclein. Motor neurons were depleted (∼75%) in A53T mice but were affected less in A30P mice. Axonal degeneration was present in many regions. Electron microscopy confirmed the cell and axonal degeneration and revealed cytoplasmic inclusions in dendrites and axons. Some inclusions were degenerating mitochondria and were positive for humanα-syn. Mitochondrial complex IV and V proteins were at control levels, but complex IV activity was reduced significantly in spinal cord. Subsets of neurons in neocortex, brainstem, and spinal cord ventral horn were positive for terminal deoxynucleotidyl transferase-mediated biotinylated UTP nick end labeling, cleaved caspase-3, and p53. Mitochondria in neurons had terminal deoxynucleotidyl transferase-mediated biotinylated UTP nick end labeling-positive matrices and p53 at the outer membrane. Thus, A53T mutant mice develop intraneuronal inclusions, mitochondrial DNA damage and degeneration, and apoptotic-like death of neocortical, brainstem, and motor neurons.

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Authors: Martin, L. J., Pan, Y., Price, A. C., Sterling, W., Copeland, N. G., Jenkins, N. A., Price, D. L., & Lee, M. K.
Affiliations: Johns Hopkins University (US)
National Institutes of Health (US)
ORCID: Martin, Lee J.
Jenkins, Nancy A.
Lee, Michael K.
Venue: The Journal of Neuroscience
Publisher: Society for Neuroscience
Published: 2006-01-04
Volume: 26
Issue: 1
Pages: 41-50
ISSN: 0270-6474 (ISSN-L)
1529-2401
DOI: 10.1523/jneurosci.4308-05.2006
PMC: PMC6381830
OpenAlex: W2084910880
Cited by: 684
References: 59
Citations by year: 2026: 15 · 2025: 14 · 2024: 24 · 2023: 27 · 2022: 37 · 2021: 34 · 2020: 27 · 2019: 34 · 2018: 39 · 2017: 43 · 2016: 34 · 2015: 30 · 2014: 35 · 2013: 41 · 2012: 49
FWCI: 26.91
Type: journal article
Language: en
Open access: hybrid
doi.org
Licence: cc-by-nc-sa
creativecommons.org/licenses/by-nc-sa/4.0/ (vor, 181 d)
Locations: Journal of Neuroscience (publishedVersion, cc-by-nc-sa)
Europe PMC (PubMed Central) (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Funders: National Institutes of Health (NS38377)
U.S. Public Health Service
National Institute on Aging (AG 16282, R01AG016282)
National Institute of Neurological Disorders and Stroke (NS 38377, R01NS052098, NS34 100, P01NS038065, R56NS038065, P50NS038377, NS 38065, R01NS034100, R01NS038065, NS52098)
Topics: Health Sciences › Medicine › Clinical Neurology › Parkinson's Disease Mechanisms and Treatments
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Nuclear Receptors and Signaling
Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
Keywords: alpha-synuclein, Parkinson's disease, A53T mutation, A30P mutation, transgenic mice, mitochondrial degeneration, neuronal cell death, motor neuron degeneration, axonal degeneration, Lewy bodies, mitochondrial DNA damage, apoptosis, caspase-3, p53, mitochondrial complex IV, synucleinopathies
MeSH terms: Alanine, Animals, Brain Stem, DNA Damage, Humans, Mice, Transgenic, Mitochondria, Mutation, Nerve Degeneration, Parkinson Disease, Threonine, Cell Death, Neocortex, Mice, alpha-Synuclein

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Parkinson's Disease α-Synuclein Transgenic Mice Develop Neuronal Mitochondrial Degeneration and Cell Death

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