Synuclein deficiency decreases the efficiency of dopamine uptake by synaptic vesicles

Ninkina, N. N.; Tarasova, T. V.; Chaprov, K. D.; Goloborshcheva, Valeria V; Bachurin, S. O.; Buchman, V. L.

doi:10.31857/s0869-56524861114-117

Cited by 2 publications

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“…Most of these proteins play a physiological role in monomeric form. Thus, α-synuclein is shown to be important in synaptic transmission and mitochondrial bioenergetics [ 13 , 14 , 15 ]. Tau is a microtubule-associated protein which also plays a role in stabilizing neuronal microtubules and thus promotes axonal outgrowth [ 16 ].…”

Section: Introductionmentioning

confidence: 99%

Interaction of Oxidative Stress and Misfolded Proteins in the Mechanism of Neurodegeneration

Abramov

Potapova

Dremin

et al. 2020

Life

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Aggregation of the misfolded proteins β-amyloid, tau, huntingtin, and α-synuclein is one of the most important steps in the pathology underlying a wide spectrum of neurodegenerative disorders, including the two most common ones—Alzheimer’s and Parkinson’s disease. Activity and toxicity of these proteins depends on the stage and form of aggregates. Excessive production of free radicals, including reactive oxygen species which lead to oxidative stress, is proven to be involved in the mechanism of pathology in most of neurodegenerative disorders. Both reactive oxygen species and misfolded proteins play a physiological role in the brain, and only deregulation in redox state and aggregation of the proteins leads to pathology. Here, we review the role of misfolded proteins in the activation of ROS production from various sources in neurons and glia. We discuss if free radicals can influence structural changes of the key toxic intermediates and describe the putative mechanisms by which oxidative stress and oligomers may cause neuronal death.

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Section: Introductionmentioning

confidence: 99%

Interaction of Oxidative Stress and Misfolded Proteins in the Mechanism of Neurodegeneration

Abramov

Potapova

Dremin

et al. 2020

Life

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“…Белки синуклеины являются многофункциональными: в норме они вовлечены в регуляцию нейротрансмиссии [2]. Для α-и β-синуклеинов была показана спо-собность связываться с везикуло-ассоциированным мембранным белком VAMP2 и участие в формировании SNARE-комплексов в пресинаптических терминалиях дофаминергических нейронов [3,4]. Третий члена семейства -γ-синуклеин, вовлечен в процессы формирования липидных рафтов и регуляцию липидного обмена, a нарушение функции γ-синуклеина ведет к усилению липолиза и изменению липидного гомеостаза [5,6].…”

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Knock-out of α-, β-, and γ-synuclein genes in mice leads to changes in the distribution of several lipids in the liver and blood plasma

Lysikova¹,

Chaprov²

2022

RR. in B.

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In addition to the role of synuclein proteins in synaptic transmission through binding with lipid membranes, the function of synucleins in reactions of the synthesis of lipids and fatty acids is also widely studied. Studying the disruption of lipid metabolism in Parkinson’s disease caused by synuclein dysfunction is particularly interesting. The aim of the study: To determine the effect of the absence of synuclein family proteins on the total lipid content and the ratio of different lipid classes in the liver and blood plasma in transgenic mice. Materials and methods: Measurement of lipid classes of αβγ-synuclein triple knockout mice (N=6) and wild type controls (N=6) was performed by the HPLC on the silica gel plates. Results: A 1.4-fold (P<0.05) increase in the percentage of total polar lipids was detected in the liver of knockout mice compared with the wild type, while the relative content of triglycerides decreased 1.2-fold (P<0.05), respectively. At the same time plasma levels of the polar lipids and triacylglycerols were unaltered. The lack of synucleins causes changes in the levels of fatty acids in comparison to wild type animals: C16:0 levels increased 1.2-fold in the liver (P<0.05) and 1.8-fold in plasma (P<0.05), and C18:1n9 levels increased both 1.4-fold (P<0.05) in plasma and 1.2-fold in the liver (P<0.05). C20:4n6 levels decreased 1.5-fold (P<0.05) in the liver of nonsynuclein mice. C18:2n6 levels decreased 7-fold in plasma (P<0.05), but did not change in liver. Conclusion: Our data demonstrate that the absence of all three members of the synuclein family causes disruption of lipid metabolism and leads to altered synthesis of fatty acids and hepatic lipid accumulation.

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Synuclein deficiency decreases the efficiency of dopamine uptake by synaptic vesicles

Cited by 2 publications

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Interaction of Oxidative Stress and Misfolded Proteins in the Mechanism of Neurodegeneration

Interaction of Oxidative Stress and Misfolded Proteins in the Mechanism of Neurodegeneration

Knock-out of α-, β-, and γ-synuclein genes in mice leads to changes in the distribution of several lipids in the liver and blood plasma

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