Regulation by Different Types of Chaperones of Amyloid Transformation of Proteins Involved in the Development of Neurodegenerative Diseases

Muronetz, Vladimir I.; Kudryavtseva, Sofia S.; Leisi, Evgeniia V.; Kurochkina, Lidia P.; Barinova, Kseniya; Schmalhausen, E.V.

doi:10.3390/ijms23052747

Cited by 5 publications

(6 citation statements)

References 156 publications

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“…The molecular chaperones accelerate the process of protein folding and without them the cell could not perform any of its functions, hence no cell could live. 20 …”

Section: Resultsmentioning

confidence: 99%

A Theoretical Framework on the Biology of Prion Diseases

Bajrami,

Vyshka

2023

Acta Inform Med

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Background: Prion diseases or TSE diseases are a group of neurodegenerative disorders that manifest in several forms in humans, such as Kuru disease, Creutzfeldt‒Jakob disease (CJD), Gerstmann-Sträussler-Scheinker syndrome (GSS) and fatal familial insomnia. Objective: In this study, we propose a multimodular hypothesis of prion diseases. According to this hypothesis, a prion disease manifests because of the interaction of two genetic modules, such as the PRNP gene module and that of the gene or genes responsible for one or more chaperones, with one or some chemical module on whose structure the products of the genes or genetic modules interact. Methods: This study presents the perspective that modular thinking can allow us to overcome conceptual obstacles in the understanding and interpretation of prion diseases. Results and Discussion: The structure of the chemical module or modules is directly responsible for the folding or misfolding of the PrPC protein. The etiology of acquired prion diseases is explained based on this hypothesis. Hence, it has been proposed that (g) CJD involves the PRNP gene mutant and one or more mutant genes for one or more chaperone genes. In contrast, sCJD has one or more mutant chaperone genes. When does iCJD occur? Healthy individuals manifest acquired prion disease through contamination when infected with one or more mutant chaperones. The mutant chaperones interact with the prion protein, and PrPC is converted to its isoform PrPSc. In a recent study, there was a case of an individual with CJD after COVID-19 infection. Conclusion: This case emphasizes the link between neuroinflammation and protein misfolding and provides proof that chemical module formation is a necessary condition for the manifestation of prion diseases.

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“…The molecular chaperones accelerate the process of protein folding and without them the cell could not perform any of its functions, hence no cell could live. 20 …”

Section: Resultsmentioning

confidence: 99%

A Theoretical Framework on the Biology of Prion Diseases

Bajrami,

Vyshka

2023

Acta Inform Med

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“…Due to their barrel-like shape, chaperonins create perfect conditions inside the “barrel” for polypeptides to rearrange conformation, leading to the native form. Moreover, the process and its requirements protect from aggregation [ 12 , 13 ].…”

Section: Chaperonesmentioning

confidence: 99%

“…The molecular masses of the subunits vary from 12 to 43 kDa. For example, Hsp20, Hsp22, and Hsp25/27 can be mentioned [ 13 ]. The small Hsps and Hsp70 act as molecular “clamps” as a form of protection for native protein formation [ 15 ] ( Table 1 ).…”

Section: Chaperonesmentioning

confidence: 99%

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Chaperones—A New Class of Potential Therapeutic Targets in Alzheimer’s Disease

Batko,

Antosz,

Miśków

et al. 2024

IJMS

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The review describes correlations between impaired functioning of chaperones and co-chaperones in Alzheimer’s disease (AD) pathogenesis. The study aims to highlight significant lines of research in this field. Chaperones like Hsp90 or Hsp70 are critical agents in regulating cell homeostasis. Due to some conditions, like aging, their activity is damaged, resulting in β-amyloid and tau aggregation. This leads to the development of neurocognitive impairment. Dysregulation of co-chaperones is one of the causes of this condition. Disorders in the functioning of molecules like PP5, Cdc37, CacyBP/SIPTRAP1, CHIP protein, FKBP52, or STIP1 play a key role in AD pathogenesis. PP5, Cdc37, CacyBP/SIPTRAP1, and FKBP52 are Hsp90 co-chaperones. CHIP protein is a co-chaperone that switches Hsp70/Hsp90 complexes, and STIP1 binds to Hsp70. Recognition of precise processes allows for the invention of effective treatment methods. Potential drugs may either reduce tau levels or inhibit tau accumulation and aggregation. Some substances neuroprotect from Aβ toxicity. Further studies on chaperones and co-chaperones are required to understand the fundamental tenets of this topic more entirely and improve the prevention and treatment of AD.

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“…Muronetz et al [ 10 ] review various aspects of the influence of chaperones on amyloidogenic proteins. They consider both natural and artificial polymer-based chaperones.…”

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confidence: 99%