Cited by 720Mitochondrial Function and PathologyAlzheimer's disease research and treatmentsParkinson's Disease Mechanisms and Treatments

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Mitochondrial defects and oxidative stress in Alzheimer disease and Parkinson disease

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Yan, Michael H., Wang, Xinglong, Zhu, Xiongwei·2013·Free Radical Biology and Medicine

DOI 10.1016/j.freeradbiomed.2012.11.014PMC PMC3744189

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Abstract

Alzheimer disease (AD) and Parkinson disease (PD) are the two most common age-related neurodegenerative diseases characterized by prominent neurodegeneration in selective neural systems. Although a small fraction of AD and PD cases exhibit evidence of heritability, among which many genes have been identified, the majority are sporadic without known causes. Molecular mechanisms underlying neurodegeneration and pathogenesis of these diseases remain elusive. Convincing evidence demonstrates oxidative stress as a prominent feature in AD and PD and links oxidative stress to the development of neuronal death and neural dysfunction, which suggests a key pathogenic role for oxidative stress in both AD and PD. Notably, mitochondrial dysfunction is also a prominent feature in these diseases, which is likely to be of critical importance in the genesis and amplification of reactive oxygen species and the pathophysiology of these diseases. In this review, we focus on changes in mitochondrial DNA and mitochondrial dynamics, two aspects critical to the maintenance of mitochondrial homeostasis and function, in relationship with oxidative stress in the pathogenesis of AD and PD.

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Drp-1-Dependent Division of the Mitochondrial Network Blocks Intraorganellar Ca2+ Waves and Protects against Ca2+-Mediated Apoptosis
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DJ-1 acts in parallel to the PINK1/parkin pathway to control mitochondrial function and autophagy
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Abnormal interaction between the mitochondrial fission protein Drp1 and hyperphosphorylated tau in Alzheimer's disease neurons: implications for mitochondrial dysfunction and neuronal damage
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LRRK2 regulates mitochondrial dynamics and function through direct interaction with DLP1
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CaM kinase Iα–induced phosphorylation of Drp1 regulates mitochondrial morphology
Han, X.-J., Lü, Y.-F., Li, S.-A., Kaitsuka, T., Sato, Y., Tomizawa, K., Nairn, A. C., Takei, K., Matsui, H., & Matsushita, M. (2008) · The Journal of Cell Biology · doi:10.1083/jcb.200802164 · Cited by 435
The role of O2.− in the production of HO.: in vitro and in vivo
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MARCH‐V is a novel mitofusin 2‐ and Drp1‐binding protein able to change mitochondrial morphology
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PINK1 controls mitochondrial localization of Parkin through direct phosphorylation
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The mitochondrial intramembrane protease PARL cleaves human Pink1 to regulate Pink1 trafficking
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Loss of the Parkinson's disease-linked gene DJ-1 perturbs mitochondrial dynamics
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Parkin Ubiquitinates Drp1 for Proteasome-dependent Degradation
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Repair of oxidative DNA damage in nuclear and mitochondrial DNA, and some changes with aging in mammalian cells1,2 1Guest Editor: Miral Dizdaroglu 2This article is part of a series of reviews on “Oxidative DNA Damage and Repair.” The full list of papers may be found on the homepage of the journal.
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Reduced Basal Autophagy and Impaired Mitochondrial Dynamics Due to Loss of Parkinson's Disease-Associated Protein DJ-1
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Tau Promotes Neurodegeneration via DRP1 Mislocalization In Vivo
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Localization of a gene for an autosomal recessive form of juvenile Parkinsonism to chromosome 6q25.2-27.
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Human MIEF1 recruits Drp1 to mitochondrial outer membranes and promotes mitochondrial fusion rather than fission
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Sumo1 Conjugates Mitochondrial Substrates and Participates in Mitochondrial Fission
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Mitochondrial function and morphology are impaired in parkin‐mutant fibroblasts
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Mitochondrial Function and Actin Regulate Dynamin-Related Protein 1-Dependent Mitochondrial Fission
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Dynamin-Like Protein 1 Reduction Underlies Mitochondrial Morphology and Distribution Abnormalities in Fibroblasts from Sporadic Alzheimer's Disease Patients
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Fzo1, a Protein Involved in Mitochondrial Fusion, Inhibits Apoptosis
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ChChd3, an Inner Mitochondrial Membrane Protein, Is Essential for Maintaining Crista Integrity and Mitochondrial Function
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Mitochondrial localization of DJ‐1 leads to enhanced neuroprotection
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The kinase domain of mitochondrial PINK1 faces the cytoplasm
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Parkinson's disease and pesticides: a toxicological perspective
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Marked changes in mitochondrial DNA deletion levels in Alzheimer brains
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“Studies analyzing mtDNA found that the mtDNA of cortical neurons in AD patients younger than 75 years of age has 15 times more of the common 5-kb mtDNA deletion mutations than age-matched controls [68].”
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Redox imbalance in Parkinson's disease
Chinta, S. J., & Andersen, J. K. (2008) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2008.02.005 · Cited by 303
Enhanced substantia nigra mitochondrial pathology in human α-synuclein transgenic mice after treatment with MPTP111-Methyl-4-phenyl-1,2,3,6-tetrahydropyridine.
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Abnormal mitochondrial dynamics and neurodegenerative diseases
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A mitochondrial etiology of Alzheimer and Parkinson disease
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The 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine mouse model: a tool to explore the pathogenesis of Parkinson's disease.
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The genetic architecture of Alzheimer's disease: beyond APP, PSENs and APOE
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The 1‐Methyl‐4‐Phenyl‐1,2,3,6‐Tetrahydropyridine Mouse Model
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Analysis of European mitochondrial haplogroups with Alzheimer disease risk
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Age-dependent cardiomyopathy in mitochondrial mutator mice is attenuated by overexpression of catalase targeted to mitochondria
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Defects in Mitochondrial Dynamics and Metabolomic Signatures of Evolving Energetic Stress in Mouse Models of Familial Alzheimer's Disease
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Parkin enhances mitochondrial biogenesis in proliferating cells
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LRRK2 Modulates Vulnerability to Mitochondrial Dysfunction in Caenorhabditis elegans
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Ageing-associated 5 kb deletion in human liver mitochondrial DNA
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Mitochondrial complex I inhibition is not required for dopaminergic neuron death induced by rotenone, MPP + , or paraquat
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Early‐onset familial parkinsonism due to POLG mutations
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Antioxidants in Central Nervous System Diseases: Preclinical Promise and Translational Challenges
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Mild Cerebral Ischemia Induces Loss of Cyclin-Dependent Kinase Inhibitors and Activation of Cell Cycle Machinery before Delayed Neuronal Cell Death
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Short- and long-term alterations of mitochondrial morphology, dynamics and mtDNA after transient oxidative stress
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Pathogenic mutations in Parkinson disease
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Somatic progenitor cell vulnerability to mitochondrial DNA mutagenesis underlies progeroid phenotypes in Polg mutator mice
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The PINK1/Parkin pathway regulates mitochondrial dynamics and function in mammalian hippocampal and dopaminergic neurons
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Parkinson’s disease‐associated DJ‐1 mutations impair mitochondrial dynamics and cause mitochondrial dysfunction
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α-Synuclein is differentially expressed in mitochondria from different rat brain regions and dose-dependently down-regulates complex I activity
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Detection of "deleted" mitochondrial genomes in cytochrome-c oxidase-deficient muscle fibers of a patient with Kearns-Sayre syndrome.
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Regulation of Mitochondrial Transport and Inter-Microtubule Spacing by Tau Phosphorylation at the Sites Hyperphosphorylated in Alzheimer's Disease
Shahpasand, K., Uemura, I., Saito, T., Asano, T., Hata, K., Shibata, K., Toyoshima, Y., Hasegawa, M., & Hisanaga, S.-I. (2012) · The Journal of Neuroscience · doi:10.1523/jneurosci.5927-11.2012 · Cited by 206
Mitochondrial DNA haplogroup K is associated with a lower risk of Parkinson's disease in Italians
Ghezzi, D., Marelli, C., Achilli, A., Goldwurm, S., Pezzoli, G., Barone, P., Pellecchia, M. T., Stanzione, P., Brusa, L., Bentivoglio, A. R., et al. (2005) · European Journal of Human Genetics · doi:10.1038/sj.ejhg.5201425 · Cited by 205
Ca2+ Homeostasis during Mitochondrial Fragmentation and Perinuclear Clustering Induced by hFis1
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Silencing of PINK1 Expression Affects Mitochondrial DNA and Oxidative Phosphorylation in DOPAMINERGIC Cells
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Pink1 regulates the oxidative phosphorylation machinery via mitochondrial fission
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The PINK1–Parkin pathway is involved in the regulation of mitochondrial remodeling process
Park, J., Lee, G., & Chung, J. (2008) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2008.11.086 · Cited by 187
A mitochondrial DNA clone is associated with increased risk for Alzheimer disease.
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Mitochondrial Alterations in PINK1 Deficient Cells Are Influenced by Calcineurin-Dependent Dephosphorylation of Dynamin-Related Protein 1
Matton, A., Craig, K. J. T., Beilina, A. G., van der Brug, M., Harwig, M. C., Ahmad, R., Miller, D. W., Zambrano, I., Cowburn, R. F., Behbahani, H., et al. (2009) · PLoS ONE · doi:10.1371/journal.pone.0005701 · Cited by 181
Differentiation-specific effects of LHON mutations introduced into neuronal NT2 cells
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Apolipoprotein E promotes β-amyloid trafficking and degradation by modulating microglial cholesterol levels
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“In fact, ApoE has been discovered to affect amyloid-β (Aβ) degradation, perhaps through a complex system of increased Aβ trafficking to lysosomes by regulating cholesterol levels and Rab7 (a protein involved in the vesicular transport of the late endocytotic pathway) recycling [82], and extensive research has found im…”
Background
Mitochondrial DNA haplogroup cluster UKJT reduces the risk of PD
Pyle, A., Foltynie, T., Tiangyou, W., Lambert, C., Keers, S. M., Allcock, L. M., Davison, J., Lewis, S. J. G., Perry, R. H., Barker, R. A., et al. (2005) · Annals of Neurology · doi:10.1002/ana.20417 · Cited by 176
Alzheimer's disease cybrids replicate beta-amyloid abnormalities through cell death pathways.
Khan, S. M., Cassarino, D. S., Abramova, N. N., Keeney, P. M., Borland, M. K., Pa, T., Krebs, C. T., Bennett, J. C., Parks, J. K., Swerdlow, R. H., et al. (2000) · PubMed · Cited by 176
Caspase-cleaved Tau Expression Induces Mitochondrial Dysfunction in Immortalized Cortical Neurons
Quintanilla, R. A., Matthews-Roberson, T. A., Dolan, P. J., & Johnson, G. V. W. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m808908200 · Cited by 170
Mitochondrial DNA haplogroups and APOE4 allele are non-independent variables in sporadic Alzheimer's disease
Carrieri, G., Bonafè, M., Luca, M. D., Rose, G., Varcasia, O., Bruni, A. C., Maletta, R., Nacmias, B., Sorbi, S., Corsonello, F., et al. (2001) · Human Genetics · doi:10.1007/s004390100463 · Cited by 169
6-Hydroxydopamine (6-OHDA) induces Drp1-dependent mitochondrial fragmentation in SH-SY5Y cells
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Leucine‐rich repeat kinase 2 disturbs mitochondrial dynamics via Dynamin‐like protein
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S-Nitrosylation of DRP1 Does Not Affect Enzymatic Activity and is Not Specific to Alzheimer's Disease
Bossy, B., Petrilli, A. M., Klinglmayr, E., Chen, J., Lütz‐Meindl, U., Knott, A. B., Masliah, E., Schwarzenbacher, R., & Bossy‐Wetzel, E. (2010) · Journal of Alzheimer s Disease · doi:10.3233/jad-2010-100552 · Cited by 165
Systemic Mitochondrial Dysfunction and the Etiology of Alzheimer's Disease and Down Syndrome Dementia
Coskun, P. E., Wyrembak, J., Derbereva, O., Melkonian, G., Doran, E. W., Lott, I. T., Head, E., Cotman, C. W., & Wallace, D. C. (2010) · Journal of Alzheimer s Disease · doi:10.3233/jad-2010-100351 · Cited by 161
Mitochondrial DNA polymerase gamma variants in idiopathic sporadic Parkinson disease
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Mitoenergetic failure in Alzheimer disease
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Alpha‐synuclein impairs normal dynamics of mitochondria in cell and animal models of Parkinson’s disease
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Evolutionary and functional relationships within the DJ1 superfamily
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Altered Calcium Homeostasis in Cells Transformed by Mitochondria from Individuals with Parkinson's Disease
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The Neuropsychiatric Aspects of Boxing
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Truncated tau and Aβ cooperatively impair mitochondria in primary neurons
Quintanilla, R. A., Dolan, P. J., Jin, Y. N., & Johnson, G. V. W. (2011) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2011.02.007 · Cited by 139
Cells Bearing Mutations Causing Leber's Hereditary Optic Neuropathy Are Sensitized to Fas-induced Apoptosis
Danielson, S. R., Wong, A., Carelli, V., Martinuzzi, A., Schapira, A. H. V., & Cortopassi, G. A. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m110119200 · Cited by 139
High frequency of mitochondrial complex I mutations in Parkinson’s disease and aging
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DLP1‐dependent mitochondrial fragmentation mediates 1‐methyl‐4‐phenylpyridinium toxicity in neurons: implications for Parkinson’s disease
Wang, X., Su, B., Liu, W., He, X., Gao, Y., Castellani, R. J., Perry, G. L., Smith, M. A., & Zhu, X. (2011) · Aging Cell · doi:10.1111/j.1474-9726.2011.00721.x · Cited by 134
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Expression of β-Amyloid Induced Age-Dependent Presynaptic and Axonal Changes in Drosophila
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Authors: Yan, M. H., Wang, X., & Zhu, X.
Affiliations: Case Western Reserve University (US)
Corresponding author: Wang, Xinglong
Zhu, Xiongwei
ORCID: Wang, Xinglong
Zhu, Xiongwei
Venue: Free Radical Biology and Medicine
Publisher: Elsevier BV
Published: 2013-09
Volume: 62
Pages: 90-101
ISSN: 0891-5849 (ISSN-L)
DOI: 10.1016/j.freeradbiomed.2012.11.014
PMC: PMC3744189
OpenAlex: W2027783468
Cited by: 718
References: 209
Citations by year: 2026: 14 · 2025: 34 · 2024: 73 · 2023: 56 · 2022: 69 · 2021: 67 · 2020: 53 · 2019: 47 · 2018: 53 · 2017: 71 · 2016: 54 · 2015: 49 · 2014: 48 · 2013: 30
FWCI: 16.31
Type: journal article
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/legal/tdmrep-license (tdm)
Locations: Free Radical Biology and Medicine (publishedVersion)
PubMed (publishedVersion)
Europe PMC (PubMed Central) (acceptedVersion)
PubMed Central (acceptedVersion)
Funders: the National Institutes of Health (AG031852, NS071184)
Alzheimer's Association (IIRG-10–173358)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
Health Sciences › Medicine › Clinical Neurology › Parkinson's Disease Mechanisms and Treatments
Keywords: Alzheimer's disease, Parkinson's disease, mitochondrial dysfunction, oxidative stress, mitochondrial DNA, mitochondrial dynamics, reactive oxygen species, neurodegeneration, mitochondrial homeostasis
MeSH terms: Alzheimer Disease, Humans, Mitochondria, Nerve Degeneration, Neurons, Parkinson Disease, Amyloid beta-Peptides, Cell Death, Reactive Oxygen Species, Oxidative Stress

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Mitochondrial defects and oxidative stress in Alzheimer disease and Parkinson disease

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