Mitochondrial associated metabolic proteins are selectively oxidized in A30P α-synuclein transgenic mice—a model of familial Parkinson's disease

Poon, H. Fai; Frasier, Mark; Shreve, Nathan; Calabrese, Vittorio; Wolozin, Benjamin; Butterfield, D. Allan

doi:10.1016/j.nbd.2004.12.009

Cited by 153 publications

(32 citation statements)

References 59 publications

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“…Alpha-enolase is a housekeeping enzyme, which catalyzes the hydrolysis dehydration of 2-phospho-D-glycerate (2-PGA) to phosphoenolpyruvate (PEP) in the penultimate step of glycolysis in cytoplasm. Many studies demonstrate that ENO1 is subjected to oxidative modification, which can be accompanied by decreasing its activity in different pathological conditions such as aging [182], Alzheimer's and Parkinson's diseases [183–186], Huntington's disease [187], and cancer [188, 189]. However, ENO1 does not directly affect ATP production in spite of its glycolytic function.…”

Section: Oxidation Protein-adductsmentioning

confidence: 99%

Mitochondrial dysfunction and oxidative stress in aging and cancer

et al. 2016

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Aging and cancer are the most important issues to research. The population in the world is growing older, and the incidence of cancer increases with age. There is no doubt about the linkage between aging and cancer. However, the molecular mechanisms underlying this association are still unknown. Several lines of evidence suggest that the oxidative stress as a cause and/or consequence of the mitochondrial dysfunction is one of the main drivers of these processes. Increasing ROS levels and products of the oxidative stress, which occur in aging and age-related disorders, were also found in cancer. This review focuses on the similarities between ageing-associated and cancer-associated oxidative stress and mitochondrial dysfunction as their common phenotype.

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Section: Oxidation Protein-adductsmentioning

confidence: 99%

Mitochondrial dysfunction and oxidative stress in aging and cancer

et al. 2016

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“…α-synuclein is a hydrophobic protein prone form the typical fibrillar aggregations observed in Lewy bodies, which links this protein with both sporadic and familial forms of PD [42]. α-synuclein aggregation inhibits mitochondrial complex I activity, elevates ROS production [192] and increases protein-carbonyl levels [193]. In vitro , the interaction of α-synuclein with mitochondria leads to cytochrome c release, enhances mitochondrial Ca 2+ , and triggers oxidative modifications of mitochondrial components [194].…”

Section: Metabolic Disturbances In Genetic Models Of Pdmentioning

confidence: 99%

Mitochondrial control of cell bioenergetics in Parkinson’s disease

Requejo-Aguilar

Bolaños

2016

Free Radical Biology and Medicine

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Parkinson disease (PD) is a neurodegenerative disorder characterized by a selective loss of dopaminergic neurons in the substantia nigra. The earliest biochemical signs of the disease involve failure in mitochondrial-endoplasmic reticulum cross talk and lysosomal function, mitochondrial electron chain impairment, mitochondrial dynamics alterations, and calcium and iron homeostasis abnormalities. These changes are associated with increased mitochondrial reactive oxygen species (mROS) and energy deficiency. Recently, it has been reported that, as an attempt to compensate for the mitochondrial dysfunction, neurons invoke glycolysis as a low-efficient mode of energy production in models of PD. Here, we review how mitochondria orchestrate the maintenance of cellular energetic status in PD, with special focus on the switch from oxidative phosphorylation to glycolysis, as well as the implication of endoplasmic reticulum and lysosomes in the control of bioenergetics.

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“…61–63 α-Syn aggregates also interact with other mitochondrial proteins such as carbonic anhydrase, enolase, and lactate dehydrogenase which were found to be oxidized in brains of transgenic mice overexpressing mutant A30P α-Syn. 64 α-Syn overexpression was shown to significantly increase the translocation of mitochondrial fission protein Drp1 via extracellular signal-regulated kinase (ERK) pathway 65 and induced mitochondrial cytochrome C release and caspase-9 and -3 activities promoting apoptosis. 55,66 In contrast, inhibition of α-Syn expression prevented MPP + -induced mitochondrial fragmentation in vitro.…”

Section: The Proteopathic Basis Of Neurodegenerative Processes In Pd mentioning

confidence: 99%

Mechanisms of Parkinson’s disease-related proteins in mediating secondary brain damage after cerebral ischemia

Kim

Vemuganti

2017

J Cereb Blood Flow Metab

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Both Parkinson’s disease (PD) and stroke are debilitating conditions that result in neuronal death and loss of neurological functions. These two conditions predominantly affect aging populations with the deterioration of the quality of life for the patients themselves and a tremendous burden to families. While the neurodegeneration and symptomology of PD develop chronically over the years, post-stroke neuronal death and dysfunction develop rapidly in days. Despite the discrepancy in the pathophysiological time frame and severity, both conditions share common molecular mechanisms that include oxidative stress, mitochondrial dysfunction, inflammation, endoplasmic reticulum stress, and activation of various cell death pathways (apoptosis/necrosis/autophagy) that synergistically modulate the neuronal death. Emerging evidence indicates that several proteins associated with early-onset familial PD play critical roles in mediating the neuronal death. Importantly, mutations in the genes encoding Parkin, PTEN-induced putative kinase 1 and DJ-1 mediate autosomal recessive forms of PD, whereas mutations in the genes encoding leucine-rich repeat kinase 2 and α-synuclein are responsible for autosomal dominant PD. This review discusses the significance of these proteins with the emphasis on the role of α-synuclein in mediating post-ischemic brain damage.

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Mitochondrial associated metabolic proteins are selectively oxidized in A30P α-synuclein transgenic mice—a model of familial Parkinson's disease

Cited by 153 publications

References 59 publications

Mitochondrial dysfunction and oxidative stress in aging and cancer

Mitochondrial dysfunction and oxidative stress in aging and cancer

Mitochondrial control of cell bioenergetics in Parkinson’s disease

Mechanisms of Parkinson’s disease-related proteins in mediating secondary brain damage after cerebral ischemia

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