Recent advances on the molecular pathogenesis of prion diseases

Glatzel, Markus; Sigurdson, Christina J.

doi:10.1111/bpa.12693

Cited by 2 publications

(3 citation statements)

References 24 publications

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“…Conformation changes the properties of proteins, thus having a direct impact on the principles of tool reprocessing (Table 1) [23]. [18,24,25]. Major animal diseases include scrapie of sheep and goats, bovine spongiform encephalopathy, chronic debilitating disease of cervids and camel prion disease (identified in 2018) [25].…”

Section: Characteristics Of Prionsmentioning

confidence: 99%

“…[18,24,25]. Major animal diseases include scrapie of sheep and goats, bovine spongiform encephalopathy, chronic debilitating disease of cervids and camel prion disease (identified in 2018) [25]. The debilitating disease of cervids has spread in North America and has recently appeared in Norway and Finland [18,26].…”

Section: Characteristics Of Prionsmentioning

confidence: 99%

“…3) Kuru disease (laughing death) -until the middle of the twentieth century this killed women and children from the Fore tribe on the island of Papua New Guinea, who for ritual reasons were eating infectious fragments of relatives. People born after the ban on cannibalism (after 1959) no longer suffer from Kuru [7,13,14,23,25,28,29,30].…”

Section: Characteristics Of Prionsmentioning

confidence: 99%

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Handling of endoscopic equipment after use in the case of a patient with suspected prion disease

Gruszecka

Filip

2020

Ann Agric Environ Med.

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Introduction. Prion diseases are slow-acting, neurodegenerative diseases found in humans and many species of animals. Although they occur very rarely in humans, currently, an increase in this type of disease is being observed, probably as a result of exposure to infectious prions causing BSE disease in cows. Objective. The aim of the procedures described in the article is to minimize the risk of human-to-human transfer of all forms of transmissible spongiform encephalopathy, including variant CJD (vCJD) by contaminated medical equipment. Brief description of the state of knowledge. All diseases caused by prions, referred to as transmissible spongiform encephalopathies, are fatal. They are characterized by a long development period (up to several decades). Enormous problems are connected with the risk of transferring prions from patient to patient on the surface of instruments used in medical procedures. Laboratory tests indicate that standard disinfection and sterilization procedures may be insufficient to completely remove infectious proteins from contaminated instruments. One of the methods of infection prevention involves taking equipment used for surgery within the brain, tonsils or appendix, into quarantine until biopsy results of these organs have been received that exclude, as far as possible, asymptomatic carriage of prions. Conclusions. Whenever possible and justified, disposable-use instruments should be used for invasive surgery in patients with definite, clinically probable cases of CJD (vCJD). After use, these instruments should be incinerated.

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Section: Characteristics Of Prionsmentioning

confidence: 99%

Section: Characteristics Of Prionsmentioning

confidence: 99%

Section: Characteristics Of Prionsmentioning

confidence: 99%

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Handling of endoscopic equipment after use in the case of a patient with suspected prion disease

Gruszecka

Filip

2020

Ann Agric Environ Med.

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Assessment of the therapeutic potential of Hsp70 activator against prion diseases using in vitro and in vivo models

Zayed,

Kim,

Jeong

2024

Front. Cell Dev. Biol.

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IntroductionPrion diseases are deadly neurodegenerative disorders in both animals and humans, causing the destruction of neural tissue and inducing behavioral manifestations. Heat shock proteins (Hsps), act as molecular chaperones by supporting the appropriate folding of proteins and eliminating the misfolded proteins as well as playing a vital role in cell signaling transduction, cell cycle, and apoptosis control. SW02 is a potent activator of Hsp 70 kDa (Hsp70).MethodsIn the current study, the protective effects of SW02 against prion protein 106-126 (PrP106-126)-induced neurotoxicity in human neuroblastoma cells (SH-SY5Y) were investigated. In addition, the therapeutic effects of SW02 in ME7 scrapie-infected mice were evaluated.ResultsThe results showed that SW02 treatment significantly increased Hsp70 mRNA expression levels and Hsp70 ATPase activity (p < 0.01). SW02 also significantly inhibited cytotoxicity and apoptosis induced by PrP106-126 (p < 0.01) and promoted neurite extension. In vivo, intraperitoneal administration of SW02 did not show a statistically significant difference in survival time (p = 0.16); however, the SW02-treated group exhibited a longer survival time of 223.6 ± 6.0 days compared with the untreated control group survival time of 217.6 ± 5.4 days. In addition, SW02 reduced the PrPSc accumulation in ME7 scrapie-infected mice at 5 months post-injection (p < 0.05). A significant difference was not observed in GFAP expression, an astrocyte marker, between the treated and untreated groups.ConclusionIn conclusion, the potential therapeutic role of the Hsp70 activator SW02 was determined in the present study and may be a novel and effective drug to mitigate the pathologies of prion diseases and other neurodegenerative diseases. Further studies using a combination of two pharmacological activators of Hsp70 are required to maximize the effectiveness of each intervention.

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Recent advances on the molecular pathogenesis of prion diseases

Cited by 2 publications

References 24 publications

Handling of endoscopic equipment after use in the case of a patient with suspected prion disease

Handling of endoscopic equipment after use in the case of a patient with suspected prion disease

Assessment of the therapeutic potential of Hsp70 activator against prion diseases using in vitro and in vivo models

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