scholarly journals TCF11 at the crossroads of oxidative stress and the ubiquitin proteasome system

Cell Cycle ◽  
2011 ◽  
Vol 10 (8) ◽  
pp. 1200-1207 ◽  
Author(s):  
Annett Koch ◽  
Janos Steffen ◽  
Elke Krüger
Keyword(s):  
Oxidative Stress ◽  
Ubiquitin Proteasome System ◽  
Ubiquitin Proteasome

Inhibition of the Ubiquitin-Proteasome System Protects Endothelial Cells from Oxidative Stress

2006 ◽  
Vol 2006 (Spring) ◽  
Author(s):  
Silke Meiners ◽  
Andrea Weller ◽  
Antje Ludwig ◽  
Karl Stangl ◽  
Verena Stangl
Keyword(s):  
Oxidative Stress ◽  
Endothelial Cells ◽  
Ubiquitin Proteasome System ◽  
Ubiquitin Proteasome

Aerobic exercise training improves oxidative stress and ubiquitin proteasome system activity in heart of spontaneously hypertensive rats

2015 ◽  
Vol 402 (1-2) ◽  
pp. 193-202 ◽  
Author(s):  
Luiz Henrique Soares de Andrade ◽  
Wilson Max Almeida Monteiro de Moraes ◽  
Eduardo Hiroshi Matsuo Junior ◽  
Elizabeth de Orleans Carvalho de Moura ◽  
Hanna Karen Moreira Antunes ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Exercise Training ◽  
Aerobic Exercise ◽  
Spontaneously Hypertensive Rats ◽  
Ubiquitin Proteasome System ◽  
Aerobic Exercise Training ◽  
Hypertensive Rats ◽  
Spontaneously Hypertensive ◽  
System Activity ◽  
Ubiquitin Proteasome

scholarly journals Neuroprotective Role of Camel α-Lactalbumin Via Regulating SIRT1/FOXO3a Pathway Against Rotenone-Induced Neurotoxicity

2021 ◽  
Author(s):  
Saba Ubaid ◽  
Shivani Pandey ◽  
Mohd. Sohail Akhtar ◽  
Mohammad Rumman ◽  
Babita Singh ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Ubiquitin Proteasome System ◽  
Protective Agent ◽  
Brain Disorder ◽  
Current Therapies ◽  
Ubiquitin Proteasome ◽  
Potential Activity ◽  
Apoptotic Pathways

Abstract Camel milk is rich in nutritional factors, such as α- Lactalbumin, and important for brain development. It is known to act as a potential therapeutic candidate for brain disorder via regulation of inflammatory and apoptotic pathways. Mechanisms that are critically involved with Parkinson’s disease (PD) are apoptosis, inflammation, and oxidative stress, and the aberrated ubiquitin-proteasome system. Adverse effects of current therapies are imposing the need for the development of natural neuroprotective agents that are very effective and have fewer or no side effects. The present study aimed to evaluate the potential activity of camel α-Lactalbumin (α-LA) in rotenone induced in-vitro PD model. In this study, we hypothesized the use of camel α-lactalbumin as an effective curative agent for PD. The mechanism of action of camel α-lactalbumin was investigated by assessing the effect of α-LA on the level of nitric oxide, NADH, MMP9, inflammatory markers, and on the expression level of SIRT1 and FOXO3a in SH-SY5Y cell line. Overall, the results revealed the potent neuroprotective efficacy of α-Lactalbumin in rotenone-induced PD model via effectively modulating apoptotic pathways, oxidative stress, and neuroinflammatory cascades. Conclusively, these findings confirmed that α-LA could be a biologically effective protective agent against rotenone induced neurotoxic impacts and neurobehavioral aberrations.

scholarly journals It Is All about (U)biquitin: Role of Altered Ubiquitin-Proteasome System and UCHL1 in Alzheimer Disease

2016 ◽  
Vol 2016 ◽  
pp. 1-12 ◽  
Author(s):  
Antonella Tramutola ◽  
Fabio Di Domenico ◽  
Eugenio Barone ◽  
Marzia Perluigi ◽  
D. Allan Butterfield
Keyword(s):  
Oxidative Stress ◽  
Alzheimer Disease ◽  
Ubiquitin Proteasome System ◽  
Oxidative Modification ◽  
Age Related ◽  
Ubiquitin Proteasome ◽  
Proteasome Pathway ◽  
And Function ◽  
Cellular Components

Free radical-mediated damage to macromolecules and the resulting oxidative modification of different cellular components are a common feature of aging, and this process becomes much more pronounced in age-associated pathologies, including Alzheimer disease (AD). In particular, proteins are particularly sensitive to oxidative stress-induced damage and these irreversible modifications lead to the alteration of protein structure and function. In order to maintain cell homeostasis, these oxidized/damaged proteins have to be removed in order to prevent their toxic accumulation. It is generally accepted that the age-related accumulation of “aberrant” proteins results from both the increased occurrence of damage and the decreased efficiency of degradative systems. One of the most important cellular proteolytic systems responsible for the removal of oxidized proteins in the cytosol and in the nucleus is the proteasomal system. Several studies have demonstrated the impairment of the proteasome in AD thus suggesting a direct link between accumulation of oxidized/misfolded proteins and reduction of this clearance system. In this review we discuss the impairment of the proteasome system as a consequence of oxidative stress and how this contributes to AD neuropathology. Further, we focus the attention on the oxidative modifications of a key component of the ubiquitin-proteasome pathway, UCHL1, which lead to the impairment of its activity.

scholarly journals Potential involvement of ubiquitin-proteasome system dysfunction associated with oxidative stress in the pathogenesis of sickle cell disease

2018 ◽  
Vol 182 (4) ◽  
pp. 559-566 ◽  
Author(s):  
Prashant Warang ◽  
Takujiro Homma ◽  
Riddhi Pandya ◽  
Anuja Sawant ◽  
Nikhil Shinde ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Sickle Cell Disease ◽  
Sickle Cell ◽  
Ubiquitin Proteasome System ◽  
Cell Disease ◽  
Ubiquitin Proteasome

scholarly journals Proteasome Inhibitor Lactacystin Induces Cholinergic Degeneration

2010 ◽  
Vol 37 (2) ◽  
pp. 229-234 ◽  
Author(s):  
Hai-Yan Zhou ◽  
Yu-Yan Tan ◽  
Zhi-Quan Wang ◽  
Gang Wang ◽  
Guo-Qiang Lu ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Membrane Potential ◽  
Mitochondrial Membrane Potential ◽  
Mitochondrial Membrane ◽  
Apoptotic Cell ◽  
Annexin V ◽  
Proteasome Inhibition ◽  
Ubiquitin Proteasome System ◽  
Cells In Culture ◽  
Ubiquitin Proteasome

Objective:Ubiquitin proteasome system dysfunction is believed to play an important role in the development of Parkinson's disease (PD), and almost all studies till now have mainly focused on the susceptibility of dopaminergic neurons to proteasome inhibition. However, in fact, there are many other types of neurons such as cholinergic ones involved in PD. In our present study, we attempt to figure out what effect the failure of ubiquitin proteasome function would execute on cholinergic cells in culture.Methods:We treated cholinergic cells in culture with various doses of lactacystin. Then MTT assay was used to evaluate the cellular viability and the Annexin V-PI method was used to detect apoptosis. Both cellular soluble and insoluble polyubiquitinated proteins were detected by western blot. Furthermore, the mitochondrial membrane potential was analyzed using JC-1 and the intracellular production of reactive oxygen species (ROS) was determined using the fluorescent probe CM-H2DCFDA.Results:We found that low doses of lactacystin were enough to induce significant apoptotic cell death, disturb the mitochondrial membrane potential, and cause oxidative stress. We also found that the amounts of polyubiquitinated proteins dramatically increased with high doses, although the loss of cells did not increase accordingly.Conclusions:Our results suggest that cholinergic cells are sensitive to ubiquitin proteasome system dysfunction, which exerts its toxic effect by causing mitochondrial dysfunction and subsequent oxidative stress, not through polyubiquitinated proteins accumulation.

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