Could Amyloid-β 1–42 or α-Synuclein Interact Directly with Mitochondrial DNA? A Hypothesis

Gezen-Ak, Duygu; Yurttaş, Zuhal; Çamoğlu, Tugay; Dursun, Erdinç

doi:10.1021/acschemneuro.2c00512

Cited by 8 publications

(2 citation statements)

References 122 publications

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“…The interaction of αSyn with mitochondria may occur not only through mitochondrial deoxyribonucleic acid, as previously predicted, but also through mitochondrial chaperones GRP75 is a mitochondria-associated membrane chaperone essential for regulating mitochondrial turnover and involved in energy production processes, , we did not find any significant change at the intracellular level of this chaperone. Conversely, another mitochondrial chaperone, Hsp10, displayed an increase in levels within the first 12 h in the control group, a response not observed in the presence of fibrils.…”

Section: Discussionsupporting

confidence: 82%

Fibrillar Alpha-Synuclein Alters the Intracellular Chaperone Levels within Hours of Its Internalization

Çamoğlu,

Yurttaş,

Kına

et al. 2024

ACS Omega

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Parkinson's disease (PD) is the second most prevalent neurodegenerative disorder worldwide. According to the Braak hypothesis, the disease spreads along specific neuroanatomical pathways. Studies indicate that fibrillar alpha-synuclein (F-αSyn) can propagate from cell-to-cell by following intercellular connections, leading to the selective death of certain cell groups like substantia nigra dopaminergic neurons and advancing the pathology. Internalized F-αSyn can be eliminated by lysosomes, proteasomes, or chaperones before it replicates inside the cell. Research has shown that F-αSyn can somehow escape from endosomes, lysosomes, and proteasomes and replicate itself. However, the impact of chaperones on intracellular levels during the initial hours of their internalization remains unknown. The present study investigates the effect of F-αSyn on chaperone levels within the first 6 and 12 h after internalization. Our findings showed that within the first 6 h, Hsc70 and Hsp90 levels were increased, while within 12 h, F-αSyn leads to a decrease or suppression of numerous intracellular chaperone levels. Exploring the pathological effects of PD on cells will contribute to identifying more targets for therapeutic interventions.

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Section: Discussionsupporting

confidence: 82%

Fibrillar Alpha-Synuclein Alters the Intracellular Chaperone Levels within Hours of Its Internalization

Çamoğlu,

Yurttaş,

Kına

et al. 2024

ACS Omega

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“…For example, does α-synuclein interact with mitochondrial DNA directly and influence transcription profile? What role synucleins play in endoplasmic reticulum-Golgi traffic [ 89 ]? Recent studies investigating microtubule dynamics showed that α-synuclein facilitated the formation of short microtubules and favorably binds to 4 protofilaments.…”

Section: Discussionmentioning

confidence: 99%

Synucleins: New Data on Misfolding, Aggregation and Role in Diseases

Surguchov

Surguchev

2022

Biomedicines

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The synucleins are a family of natively unfolded (or intrinsically unstructured) proteins consisting of α-, β-, and γ-synuclein involved in neurodegenerative diseases and cancer. The current number of publications on synucleins has exceeded 16.000. They remain the subject of constant interest for over 35 years. Two reasons explain this unchanging attention: synuclein’s association with several severe human diseases and the lack of understanding of the functional roles under normal physiological conditions. We analyzed recent publications to look at the main trends and developments in synuclein research and discuss possible future directions. Traditional areas of peak research interest which still remain high among last year’s publications are comparative studies of structural features as well as functional research on of three members of the synuclein family. Another popular research topic in the area is a mechanism of α-synuclein accumulation, aggregation, and fibrillation. Exciting fast-growing area of recent research is α-synuclein and epigenetics. We do not present here a broad and comprehensive review of all directions of studies but summarize only the most significant recent findings relevant to these topics and outline potential future directions.

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Application of metallic nanoparticles-amyloid protein supramolecular materials in tissue engineering and drug delivery: Recent progress and perspectives

Hekmat,

Kostova,

Saboury

2024

Colloids and Surfaces B: Biointerfaces

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Could Amyloid-β 1–42 or α-Synuclein Interact Directly with Mitochondrial DNA? A Hypothesis

Cited by 8 publications

References 122 publications

Fibrillar Alpha-Synuclein Alters the Intracellular Chaperone Levels within Hours of Its Internalization

Fibrillar Alpha-Synuclein Alters the Intracellular Chaperone Levels within Hours of Its Internalization

Synucleins: New Data on Misfolding, Aggregation and Role in Diseases

Application of metallic nanoparticles-amyloid protein supramolecular materials in tissue engineering and drug delivery: Recent progress and perspectives

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