Mitochondrial dysfunction in Parkinson's disease

Winklhofer, Konstanze F.; Haass, Christian

doi:10.1016/j.bbadis.2009.08.013

Cited by 690Parkinson's Disease Mechanisms and TreatmentsMitochondrial Function and PathologyAutophagy in Disease and Therapy

Mitochondrial dysfunction in Parkinson's disease

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Winklhofer, Konstanze F., Haass, Christian·2010·Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease

DOI 10.1016/j.bbadis.2009.08.013

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Abstract

Mitochondria are highly dynamic organelles which fulfill a plethora of functions. In addition to their prominent role in energy metabolism, mitochondria are intimately involved in various key cellular processes, such as the regulation of calcium homeostasis, stress response and cell death pathways. Thus, it is not surprising that an impairment of mitochondrial function results in cellular damage and is linked to aging and neurodegeneration. Many lines of evidence suggest that mitochondrial dysfunction plays a central role in the pathogenesis of Parkinson's disease (PD), starting in the early 1980s with the observation that an inhibitor of complex I of the electron transport chain can induce parkinsonism. Remarkably, recent research indicated that several PD-associated genes interface with pathways regulating mitochondrial function, morphology, and dynamics. In fact, sporadic and familial PD seem to converge at the level of mitochondrial integrity.

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Recessively inherited loss-of-function mutations in PINK1 and PRKN are the most common genetic causes of early-onset PD, which occurs in about 5%-10% of cases.
“Recessively inherited loss-of-function mutations in PTEN-induced kinase 1 (PINK1) and the E3 ubiquitin ligase PRKN are the most common genetic causes for early-onset PD, which occurs in about 5%–10% of cases [1, 2].”
From miRNA family miR-29 inhibits PINK1-PRKN signaling via ATG9A (2026) · cites this paper as [2]
The Introduction identifies loss-of-function mutations in parkin (PRKN) and PINK1 as causes of autosomal recessive PD. Sections 2.1.1.1 and 2.1.2.1 describe PINK1 as the second most common cause of recessive early-onset parkinsonism after parkin, which accounts for the majority of recessive cases. Section 2.1 says familial PD accounts for up to 10% of PD cases and usually, but not always, has early onset; it does not establish that early-onset PD itself occurs in 5%–10% of cases. (LLM, conf=0.88)
Experimental — accuracy not yet measured
Loss-of-function mutations in PINK1 and PRKN result in early-onset Parkinson disease.
“Loss-of-function mutations in the genes encoding PINK1 and PRKN result in early-onset Parkinson disease (EOPD).”
From miRNA family miR-29 inhibits PINK1-PRKN signaling via ATG9A (2026) · cites this paper as [2]
α-Synuclein causes dysfunction of mitochondrial complex I in PD, which increases ROS and oxidative stress.
“α-Synuclein has been reported to cause dysfunction of mitochondrial complex I in PD which in turn increases levels of ROS and consequently ROS-induced oxidative stress (Winklhofer and Haass 2010).”
From Reactive Oxygen Species, Toxicity, Oxidative Stress, and Antioxidants: Chronic Diseases and Aging (2023) · cites this paper as Winklhofer and Haass 2010

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THE BIOCHEMISTRY OF PARKINSON'S DISEASE
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The HtrA Family of Proteases
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Experimental models of Parkinson's disease
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Mitochondrial DNA mutations in disease and aging
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“A conditional knockout of TFAM in midbrain dopaminergic neurons caused reduced mtDNA expression, respiratory chain deficiency and neuronal cell death, leading to progressive, L-dopa-responsive impairment of motor functions [98].”
Background
Animal models of Parkinson's disease
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PINK1 Protects against Oxidative Stress by Phosphorylating Mitochondrial Chaperone TRAP1
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Mitochondrial disease
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Resistance of α-synuclein null mice to the parkinsonian neurotoxin MPTP
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Expression of A53T Mutant But Not Wild-Type α-Synuclein in PC12 Cells Induces Alterations of the Ubiquitin-Dependent Degradation System, Loss of Dopamine Release, and Autophagic Cell Death
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Loss of function mutations in the gene encoding Omi/HtrA2 in Parkinson's disease
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Neuropathology, biochemistry, and biophysics of α‐synuclein aggregation
Uversky, V. N. (2007) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2007.04764.x · Cited by 567 · see citing works
Parkin Protects against the Toxicity Associated with Mutant α-Synuclein
Petrucelli, L., O’Farrell, C., Lockhart, P. J., Baptista, M. J., Kehoe, K. J., Vink, L., Choi, P., Wolozin, B. L., Farrer, M. J., Hardy, J., et al. (2002) · Neuron · doi:10.1016/s0896-6273(02)01125-x · Cited by 552 · see citing works
Parkinsonism, premature menopause, and mitochondrial DNA polymerase γ mutations: clinical and molecular genetic study
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Parkin Mediates Nonclassical, Proteasomal-Independent Ubiquitination of Synphilin-1: Implications for Lewy Body Formation
Lim, K. L., Chew, K. C. M., Tan, J. M. M., Wang, C., Chung, K. K. K., Zhang, Y., Tanaka, Y., Smith, W. W., Engelender, S., Ross, C. A., et al. (2005) · Journal of Neuroscience · doi:10.1523/jneurosci.4474-04.2005 · Cited by 543 · see citing works
Impaired dopamine release and synaptic plasticity in the striatum of PINK1 -deficient mice
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Pink1 regulates mitochondrial dynamics through interaction with the fission/fusion machinery
Yang, Y., Ouyang, Y., Yang, L., Beal, M. F., McQuibban, G. A., Vogel, H. S., & Lu, B. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0711845105 · Cited by 536 · see citing works
Mitochondria, Oxidative Damage, and Inflammation in Parkinson's Disease
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Nitrosative stress linked to sporadic Parkinson's disease: S-nitrosylation of parkin regulates its E3 ubiquitin ligase activity
Yao, D., Gu, Z., Nakamura, T., Shi, Z., Ma, Y., Gaston, B. M., Palmer, L. A., Rockenstein, E. M., Zhang, Z., Masliah, E., et al. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0404161101 · Cited by 516 · see citing works
Localization of LRRK2 to membranous and vesicular structures in mammalian brain
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Loss-of-Function of Human PINK1 Results in Mitochondrial Pathology and Can Be Rescued by Parkin
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Self-citation
Parkin gene inactivation alters behaviour and dopamine neurotransmission in the mouse
Itier, J. (2003) · Human Molecular Genetics · doi:10.1093/hmg/ddg239 · Cited by 507 · see citing works
Oxidative stress and inflammation in Parkinson's disease: is there a causal link?
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Inducible expression of mutant alpha-synuclein decreases proteasome activity and increases sensitivity to mitochondria-dependent apoptosis
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LRRK2 in Parkinson's disease: protein domains and functional insights
Mata, I. F., Wedemeyer, W. J., Farrer, M. J., Taylor, J. P., & Gallo, K. A. (2006) · Trends in Neurosciences · doi:10.1016/j.tins.2006.03.006 · Cited by 490 · see citing works
Inhibitors of the quinone-binding site allow rapid superoxide production from mitochondrial nadh:Ubiquinone oxidoreductase (complex i)
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DJ-1 gene deletion reveals that DJ-1 is an atypical peroxiredoxin-like peroxidase
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The Parkinson disease causing LRRK2 mutation I2020T is associated with increased kinase activity
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The mitochondrial protease HtrA2 is regulated by Parkinson's disease-associated kinase PINK1
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The Mitochondrial Inner Membrane Protein Mitofilin Controls Cristae Morphology
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Oxidative Stress in Parkinson's Disease
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Mitochondrial import and enzymatic activity of PINK1 mutants associated to recessive parkinsonism
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Parkinson's disease mutations in PINK1 result in decreased Complex I activity and deficient synaptic function
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Drosophila parkin mutants have decreased mass and cell size and increased sensitivity to oxygen radical stress
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1-Methyl-4-phenylpyridinium ion (MPP+): Identification of a metabolite of MPTP, a toxin selective to the substantia nigra
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Low platelet mitochondrial complex I and complex II/III activity in early untreated parkinson's disease
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Zeroing in on the Pathogenic Form of α-Synuclein and Its Mechanism of Neurotoxicity in Parkinson's Disease
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Inhibition of neuronal nitric oxide synthase prevents MPTP–induced parkinsonism in baboons
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Loss of Parkin or PINK1 Function Increases Drp1-dependent Mitochondrial Fragmentation*
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Mice with Mitochondrial Complex I Deficiency Develop a Fatal Encephalomyopathy
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Aggregated and Monomeric α-Synuclein Bind to the S6′ Proteasomal Protein and Inhibit Proteasomal Function
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Mitochondrial localization of the Parkinson's disease related protein DJ-1: implications for pathogenesis
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Parkin prevents mitochondrial swelling and cytochrome c release in mitochondria-dependent cell death
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Proteasomal Inhibition by α-Synuclein Filaments and Oligomers
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Neuroprotective Role of the Reaper-Related Serine Protease HtrA2/Omi Revealed by Targeted Deletion in Mice
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The two faces of protein misfolding: gain‐ and loss‐of‐function in neurodegenerative diseases
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PINK1 controls mitochondrial localization of Parkin through direct phosphorylation
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Complex I deficiency in Parkinson's disease frontal cortex
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Mutations in PTEN-induced putative kinase 1 associated with recessive parkinsonism have differential effects on protein stability
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Parkinson Phenotype in Aged PINK1-Deficient Mice Is Accompanied by Progressive Mitochondrial Dysfunction in Absence of Neurodegeneration
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Loss of Omi mitochondrial protease activity causes the neuromuscular disorder of mnd2 mutant mice
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Mitochondrial dysfunction as a cause of ageing
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Reactive Oxygen Species Production by Mitochondria
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Cysteine-106 of DJ-1 is the most sensitive cysteine residue to hydrogen peroxide-mediated oxidation in vivo in human umbilical vein endothelial cells
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Endoplasmic reticulum stress and mitochondrial cell death pathways mediate A53T mutant alpha-synuclein-induced toxicity
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Sensitivity to Oxidative Stress in DJ-1-Deficient Dopamine Neurons: An ES- Derived Cell Model of Primary Parkinsonism
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Mitochondrial DNA and disease
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Platelet mitochondria function in Parkinson's disease
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A regulated interaction with the UIM protein Eps15 implicates parkin in EGF receptor trafficking and PI(3)K–Akt signalling
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Down regulation of DJ-1 enhances cell death by oxidative stress, ER stress, and proteasome inhibition
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Drosophila DJ-1 Mutants Are Selectively Sensitive to Environmental Toxins Associated with Parkinson’s Disease
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BRAIN, SKELETAL MUSCLE AND PLATELET HOMOGENATE MITOCHONDRIAL FUNCTION IN PARKINSON'S DISEASE
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PINK1 protein in normal human brain and Parkinson's disease
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Mechanism of toxicity of pesticides acting at complex I: relevance to environmental etiologies of Parkinson’s disease
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Mitochondrial function and morphology are impaired in parkin‐mutant fibroblasts
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Inactivation of Drosophila DJ-1 leads to impairments of oxidative stress response and phosphatidylinositol 3-kinase/Akt signaling
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ATP13A2 missense mutations in juvenile parkinsonism and young onset Parkinson disease
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Mitochondrial oxidative phosphorylation defects in parkinson's disease
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“, Huntington’s disease [39], amyotrophic lateral sclerosis [40], Parkinson’s disease [41], Friedreich ataxia [42], Alzheimer’s disease [43]), and chronic liver diseases (e.”
Background
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Authors: Winklhofer, K. F., & Haass, C.
Affiliations: German Center for Neurodegenerative Diseases (DE)
Corresponding author: Winklhofer, Konstanze F.
ORCID: Winklhofer, Konstanze F.
Haass, Christian
Venue: Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease
Publisher: Elsevier BV
Published: 2010-01
Volume: 1802
Issue: 1
Pages: 29-44
ISSN: 0925-4439 (ISSN-L)
DOI: 10.1016/j.bbadis.2009.08.013
OpenAlex: W2130497877
Cited by: 688
References: 326
Citations by year: 2026: 10 · 2025: 16 · 2024: 13 · 2023: 27 · 2022: 30 · 2021: 37 · 2020: 55 · 2019: 38 · 2018: 72 · 2017: 51 · 2016: 61 · 2015: 39 · 2014: 29 · 2013: 37 · 2012: 49
FWCI: 5.83
Type: journal article
Language: en
Open access: bronze
doi.org
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/open-access/userlicense/1.0/ (vor, 1784 d)
Locations: Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease (publishedVersion)
PubMed (publishedVersion)
HAL (submittedVersion, other-oa)
Trinity's Access to Research Output (TARA) (Trinity College Dublin) (submittedVersion)
Funders: Deutsche Forschungsgemeinschaft (SFB 596)
German Ministry for Education and Research
the Helmholtz Alliance “Mental Health in an Ageing Society,”
the Center for Integrated Protein Science Munich
the Hans and Ilse Breuer Foundation
Topics: Health Sciences › Medicine › Neurology › Parkinson's Disease Mechanisms and Treatments
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
Health Sciences › Medicine › Epidemiology › Autophagy in Disease and Therapy
Keywords: mitochondrial dysfunction, Parkinson's disease, mitochondrial dynamics, mitochondrial morphology, mitochondrial complex I inhibition, parkinsonism, electron transport chain, calcium homeostasis, stress response, cell death pathways, neurodegeneration, aging, familial Parkinson's disease, sporadic Parkinson's disease
MeSH terms: Animals, DNA, Mitochondrial, Humans, Mitochondria, Models, Biological, Parkinson Disease, Oxidative Stress, Mitochondrial Proteins

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