Role of RNA Oxidation in Neurodegenerative Diseases

Liu, Ziqian; Chen, Xiatian; Li, Zhe; Ye, Wei; Ding, Hongyan; Li, Peifeng; Aung, Lynn Htet Htet

doi:10.3390/ijms21145022

Cited by 23 publications

(19 citation statements)

References 97 publications

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“…On the other hand, ROS can also damage DNA, causing strand breaks or oxidative DNA lesions. As an example, the ● OH-induced nucleic acid oxidative damage can yield a variety of base lesions, among which 8-oxo-2′deoxyguanosine (8-OHdG) and 8-oxo-guanosine have received the most attention [ 23 , 24 ]. The accumulation of unrepaired or defectively repaired DNA damage could eventually promote various disorders, among which cancer is the prominent disease.…”

Section: Reactive Oxygen Species—friend or Foe?mentioning

confidence: 99%

The NRF2, Thioredoxin, and Glutathione System in Tumorigenesis and Anticancer Therapies

et al. 2020

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Cancer remains an elusive, highly complex disease and a global burden. Constant change by acquired mutations and metabolic reprogramming contribute to the high inter- and intratumor heterogeneity of malignant cells, their selective growth advantage, and their resistance to anticancer therapies. In the modern era of integrative biomedicine, realizing that a personalized approach could benefit therapy treatments and patients’ prognosis, we should focus on cancer-driving advantageous modifications. Namely, reactive oxygen species (ROS), known to act as regulators of cellular metabolism and growth, exhibit both negative and positive activities, as do antioxidants with potential anticancer effects. Such complexity of oxidative homeostasis is sometimes overseen in the case of studies evaluating the effects of potential anticancer antioxidants. While cancer cells often produce more ROS due to their increased growth-favoring demands, numerous conventional anticancer therapies exploit this feature to ensure selective cancer cell death triggered by excessive ROS levels, also causing serious side effects. The activation of the cellular NRF2 (nuclear factor erythroid 2 like 2) pathway and induction of cytoprotective genes accompanies an increase in ROS levels. A plethora of specific targets, including those involved in thioredoxin (TRX) and glutathione (GSH) systems, are activated by NRF2. In this paper, we briefly review preclinical research findings on the interrelated roles of the NRF2 pathway and TRX and GSH systems, with focus given to clinical findings and their relevance in carcinogenesis and anticancer treatments.

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Section: Reactive Oxygen Species—friend or Foe?mentioning

confidence: 99%

The NRF2, Thioredoxin, and Glutathione System in Tumorigenesis and Anticancer Therapies

et al. 2020

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“…The binding of protein hydrolysates to metal ions results in antioxidant effects (Wang, et al, 2020) since the peptides present in these hydrolysates bind to the transition metals that stop promoting oxidative damage, cell degeneration, breakage or oxidation of nucleic acids (Kurutas, 2016;Liu, et al, 2020).…”

Section: Resultsmentioning

confidence: 99%

Antioxidant activity, inhibition of angiotensin I converting enzyme (ACE) and antibacterial activity of buffalo caseinate protein hydrolysates and their fractions

Santos

Silva²,

Nascimento

et al. 2020

RSD

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In the present study, buffalo milk caseinate hydrolysates produced by bromelain, neutrase, papain and trypsin were ultra-filtered and different fractions were assessed for antioxidant, inhibition of angiotensin converting enzyme and antimicrobial activity. Biological potential was assessed by a number of metrics: ability to remove radicals of 2,2'-azino-bis (3-ethylbenzthiazoline-6-sulfonic acid), 2,2'-diphenyl-1-picrylhydrazyl (DPPH) and hydroxyls; copper and iron chelation; antidiabetic properties; antihypertensive assay; and antibacterial activity against Escherichia coli ATCC 25922, Listeria monocytogenes ATCC 19114, Salmonella typhimurium ATCC 14028 and Staphylococcus aureus ATCC 25923 strains. The tests for scavenging of hydroxyl radicals and DPPH revealed a greater potential in the 3–10 kDa fractions. Iron chelation activity >70% was observed in all the fractions, including <3 kDa. Copper chelation was >60% in fractions >10 kDa. α-Amylase inhibition and antihypertensive activity was optimal in the <3 kDa fraction. Antibacterial activity ranged between 3.28 and 100% inhibition against microorganisms tested, the fraction <3 kDa showed a greater inhibitory potential. The antihypertensive activity of fractions ranged between 39.35 and 89.58%. All treatments were able to produce hydrolysates and fractions with biological potential and, so the ultrafiltration method proved to be effective in the separation of peptides with different molar masses and potential use in the food or pharmaceutical industry.

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“…A chronic increase in ROS production causes oxidative stress and contributes to the accumulation of DNA damage (e.g., mutations and chromosomal aneuploidies), RNA damage, and further mitochondrial damage ( Korovila et al, 2017 ). All of which contribute to the increase in aggregation-prone proteins with aging ( Faggioli et al, 2012 ; Forsberg et al, 2012 ; Liu et al, 2020 ). Furthermore, proteins can be directly damaged by oxidation, which induces structural changes and makes proteins more aggregation-prone ( Serebryany et al, 2016 ; Lévy et al, 2019 ).…”

Section: Protein Homeostasis Declines With Agingmentioning

confidence: 99%

Regulation of Age-Related Protein Toxicity

Pras

Nollen

2021

Front. Cell Dev. Biol.

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Proteome damage plays a major role in aging and age-related neurodegenerative diseases. Under healthy conditions, molecular quality control mechanisms prevent toxic protein misfolding and aggregation. These mechanisms include molecular chaperones for protein folding, spatial compartmentalization for sequestration, and degradation pathways for the removal of harmful proteins. These mechanisms decline with age, resulting in the accumulation of aggregation-prone proteins that are harmful to cells. In the past decades, a variety of fast- and slow-aging model organisms have been used to investigate the biological mechanisms that accelerate or prevent such protein toxicity. In this review, we describe the most important mechanisms that are required for maintaining a healthy proteome. We describe how these mechanisms decline during aging and lead to toxic protein misassembly, aggregation, and amyloid formation. In addition, we discuss how optimized protein homeostasis mechanisms in long-living animals contribute to prolonging their lifespan. This knowledge might help us to develop interventions in the protein homeostasis network that delay aging and age-related pathologies.

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Role of RNA Oxidation in Neurodegenerative Diseases

Cited by 23 publications

References 97 publications

The NRF2, Thioredoxin, and Glutathione System in Tumorigenesis and Anticancer Therapies

The NRF2, Thioredoxin, and Glutathione System in Tumorigenesis and Anticancer Therapies

Antioxidant activity, inhibition of angiotensin I converting enzyme (ACE) and antibacterial activity of buffalo caseinate protein hydrolysates and their fractions

Regulation of Age-Related Protein Toxicity

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