China
Africa
Explore chapters and articles related to this topic
Protein–Nanoparticle Interactions
Published in Lajos P. Balogh, Nano-Enabled Medical Applications, 2020
Iseult Lynch, Kenneth A. Dawson
Amyloidogenic proteins are a group of proteins that aggregate under certain conditions to form highly insoluble structures (fibrils), which precipitate to form plaques. These aggregates are involved in a range of serious and irreversibly progressive pathological conditions (protein-misfolding diseases), such as Alzheimer’s disease, Parkinson’s disease, and dialysis-related amyloidosis. At least 20 such diseases are known.
Hyperglycemia Impairs Blood Vessel Function
Published in Robert Fried, Richard M. Carlton, Type 2 Diabetes, 2018
Robert Fried, Richard M. Carlton
Alterations in protein-folding in the endoplasmic reticulum cause accumulation of improperly structured (misfolded) proteins that profoundly affect cellular signaling processes, including reduction–oxidation (redox) homeostasis, energy production, inflammation, differentiation, and apoptosis. The unfolded protein response is a set of signaling pathways that resolve protein misfolding and restore an efficient protein-folding environment.
Maturation, Barrier Function, Aging, and Breakdown of the Blood–Brain Barrier
Published in Shamim I. Ahmad, Aging: Exploring a Complex Phenomenon, 2017
Elizabeth de Lange, Ágnes Bajza, Péter Imre, Attila Csorba, László Dénes, Franciska Erdő
Protein misfolding is a naturally occurring process in living cells. Under healthy conditions, the so-called protein quality control systems dispose of misfolded proteins. When the capacity of these systems becomes limiting, misfolded proteins may accumulate and aggregate. It seems that proteins that have repetitive amino acid motifs are mostly prone to changing into a misfolded state. Such a state is often toxic and can be viewed as “infective” when the misfolded protein is able to induce the conversion of other, normally folded proteins into the toxic configuration, and may lead to an amplification loop. Accumulation and aggregation of misfolded proteins further lead to impairment of proper cellular functioning and ultimate cell killing (Figure 15.5).
Thermodynamic and kinetic approaches for drug discovery to target protein misfolding and aggregation
Published in Expert Opinion on Drug Discovery, 2023
To extend these advances to other protein misfolding diseases, it will be important to develop more accurate methods for the identification and the quantitative measurements of the most toxic species produced when proteins misfold and aggregate. This is a challenging task, since the aggregation process involves many interconverting species, which are difficult to separate and characterize individually within a complex kinetic network [93,95,96,129]. This task is intertwined with the development of pre-clinical toxicity assays that recapitulate the pathological mechanisms relevant in a disease. Neuronal cell models derived from induced pluripotent stem cells hold great promise in this direction [130–132], as also indicated by the recent revision of the FDA guidelines concerning the use of animal models.
Role of curcumin and its nanoformulations in the treatment of neurological diseases through the effects on stem cells
Published in Journal of Drug Targeting, 2023
Nasim Sabouni, Hadi Zare Marzouni, Sepideh Palizban, Sepideh Meidaninikjeh, Prashant Kesharwani, Tannaz Jamialahmadi, Amirhossein Sahebkar
Regarding the molecular mechanisms of the hormesis effect, a connection has been assumed between modulating redox status and vitagenes-related neuroprotection [80]. Nowadays, we know that some molecular chaperones must maintain homeostasis by disrupting the aggregate and preventing protein misfolding. Nonetheless, during multiple diseases such as cancer, metabolic diseases, and neurodegenerative disorders in which chronic oxidative stress is soaring to an uncontrolled level, the repair system, including vitagenes, begins to function [63]. Vitagenes are protective genes involved in restoring hemostasis during the oxidative stress-induced condition. Therefore, they are effective agents for controlling ageing. These genes encode for Hsp32, Hsp70, heat shock proteins (Hsp), sirtuin protein system, and thioredoxin, and their activity reduces mitochondrial ROS production [81]. Recently, herbal extracts such as natural polyphenols have been neuroprotective via activating vitagenes as the hormetic pathways [82, 83]. Recent findings have revealed that one of the intracellular systems affected by curcumin and its metabolites is members of the vitagenes family, such as HSP70. Indeed, stimulation of vitagenes by curcumin results in modulating the redox system that consequently causes an antioxidant effect in a dose-dependent manner. Hence, this property can be an excellent optional therapy for age-related neurological disorders [84, 85].
Neurological effects of static and extremely-low frequency electromagnetic fields
Published in Electromagnetic Biology and Medicine, 2022
Another possible explanation for these effects may involve protein misfolding in nerve cells. Protein misfolding can lead to Alzheimer’s disease, Parkinson’s disease, Huntington’s disease and amyotropic lateral sclerosis (Ciechanover and Kwon 2015). ELF EMF induced protein misfolding involving reactive oxygen species has been reported (Lian et al. 2018). It is interesting to note that radiofrequency radiation has also been reported to cause protein misfolding (Lian et al. 2018; Mancinelli et al. 2004; Solomentsev et al. 2012). On the other hand, El F EMF can also activate heat shock proteins (Zeni et al. 2017), which are involved in the removal and repair of misfolded proteins in cell and enable cells to resume normal functions (Ciechanover and Kwon 2015; Radons 2016). Thus, ELF EMF can trigger two counteracting cellular processes, i.e., the production and removal of harmful misfolded proteins. The outcome depends on which process predominates- which can either cause or reverse the progress of neurodegenerative diseases.