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Clinical Oral Investigations Jul 2023The aim of this systematic review was to evaluate the prognosis of at-home dental bleaching using low concentration bleaching products. (Review)
Review
OBJECTIVES
The aim of this systematic review was to evaluate the prognosis of at-home dental bleaching using low concentration bleaching products.
MATERIALS AND METHODS
This review was conducted was performed following the recommendations of the 2020 PRISMA statement and was registered in the International Prospective Register of Systematic Reviews (PROSPERO-CRD42022360530). The PICO question was "What is the prognosis of home teeth whitening treatment?". An advanced electronic search was made in three databases: PubMed, Web of Science, and Embase.
RESULTS
The database search led to the retrieval of 225 articles. After elimination of duplicate references, the titles and abstracts of the articles were analyzed with respect to the eligibility criteria, and 24 studies were included for the development of the systematic review.
CONCLUSIONS
Most authors state that the color remains stable between 1 and 2.5 years regardless of the type of bleaching agent or the forms of administration, and color stability in cases of severe discolorations presents a higher degree of recurrence.
CLINICAL RELEVANCE
Given the growing demand for dental cosmetic treatments, the following systematic review may aid the clinician's continuing education and evidence-based practice by providing knowledge on the field of at-home dental bleaching agents and their long-term effects.
Topics: Humans; Hydrogen Peroxide; Tooth Bleaching Agents; Tooth Bleaching; Prognosis; Bleaching Agents
PubMed: 37273018
DOI: 10.1007/s00784-023-05069-0 -
Nature Communications Jun 2023The cystine transporter solute carrier family 7 member 11 (SLC7A11; also called xCT) protects cancer cells from oxidative stress and is overexpressed in many cancers....
The cystine transporter solute carrier family 7 member 11 (SLC7A11; also called xCT) protects cancer cells from oxidative stress and is overexpressed in many cancers. Here we report a surprising finding that, whereas moderate overexpression of SLC7A11 is beneficial for cancer cells treated with HO, a common oxidative stress inducer, its high overexpression dramatically increases HO-induced cell death. Mechanistically, high cystine uptake in cancer cells with high overexpression of SLC7A11 in combination with HO treatment results in toxic buildup of intracellular cystine and other disulfide molecules, NADPH depletion, redox system collapse, and rapid cell death (likely disulfidptosis). We further show that high overexpression of SLC7A11 promotes tumor growth but suppresses tumor metastasis, likely because metastasizing cancer cells with high expression of SLC7A11 are particularly susceptible to oxidative stress. Our findings reveal that SLC7A11 expression level dictates cancer cells' sensitivity to oxidative stress and suggests a context-dependent role for SLC7A11 in tumor biology.
Topics: Cystine; Cell Line, Tumor; Hydrogen Peroxide; Oxidative Stress; Disulfides; Amino Acid Transport System y+; Neoplasms
PubMed: 37339981
DOI: 10.1038/s41467-023-39401-9 -
Nature Communications Sep 2023Ferroptosis suppressor protein 1 (FSP1, also known as AIMF2, AMID or PRG3) is a recently identified glutathione-independent ferroptosis suppressor, but its underlying...
Ferroptosis suppressor protein 1 (FSP1, also known as AIMF2, AMID or PRG3) is a recently identified glutathione-independent ferroptosis suppressor, but its underlying structural mechanism remains unknown. Here we report the crystal structures of Gallus gallus FSP1 in its substrate-free and ubiquinone-bound forms. The structures reveal a FAD-binding domain and a NAD(P)H-binding domain, both of which are shared with AIF and NADH oxidoreductases, and a characteristic carboxy-terminal domain as well. We demonstrate that the carboxy-terminal domain is crucial for the catalytic activity and ferroptosis inhibition of FSP1 by mediating the functional dimerization of FSP1, and the formation of two active sites located on two sides of FAD, which are responsible for ubiquinone reduction and a unique FAD hydroxylation respectively. We also identify that FSP1 can catalyze the production of HO and the conversion of FAD to 6-hydroxy-FAD in the presence of oxygen and NAD(P)H in vitro, and 6-hydroxy-FAD directly inhibits ferroptosis in cells. Together, these findings further our understanding on the catalytic and ferroptosis suppression mechanisms of FSP1 and establish 6-hydroxy-FAD as an active cofactor in FSP1 and a potent radical-trapping antioxidant in ferroptosis inhibition.
Topics: Ferroptosis; Hydrogen Peroxide; NAD; Ubiquinone; Catalysis
PubMed: 37739943
DOI: 10.1038/s41467-023-41626-7 -
Redox Biology Nov 2023Nicotinamide adenine dinucleotide phosphate (NADPH) oxidases (NOXs) are enzymes that generate superoxide anion (O•) and hydrogen peroxide (HO), and that are widely... (Review)
Review
Nicotinamide adenine dinucleotide phosphate (NADPH) oxidases (NOXs) are enzymes that generate superoxide anion (O•) and hydrogen peroxide (HO), and that are widely distributed in mammalian tissues. Many bioactives, especially plant (poly)phenols are being studied for their capacity to regulate NOXs. The modulation of these enzymes are of central relevance to maintain redox homeostasis and regulate cell signaling. In in vitro and ex vivo assays, and in experimental animal models, different (poly)phenols are able to modulate NOX-dependent generation of O• and HO. Mechanistically, most of the known effects of (poly)phenols and of their metabolites on NOX1, NOX2, and NOX4, include the modulation of: i) the expression of the different constituent subunits, and/or ii) posttranslational modifications involved in the assembly and translocation of the protein complexes. Very limited evidence is available on a direct action of (poly)phenols on NOX active site (electron-transferring protein). Moreover, it is suggested that the regulation by (poly)phenols of systemic events, e.g. inflammation, is frequently associated with their capacity to regulate NOX activation. Although of physiological significance, more studies are needed to understand the specific targets/mechanisms of NOX regulation by (poly)phenols, and the (poly)phenol chemical structures and moieties directly involved in the observed effects. It should be kept in mind the difficulties of NOX's studies associated with the complexity of NOXs biochemistry and the methodological limitations of O• and HO the determinations. Studies relating human ingestion of specific (poly)phenols, with NOX activity and disease conditions, are guaranteed to better understand the health importance of (poly)phenol consumption and the involvement of NOXs as biological targets.
Topics: Animals; Humans; Reactive Oxygen Species; Phenols; Hydrogen Peroxide; Phenol; NADPH Oxidases; NADPH Oxidase 1; Mammals
PubMed: 37857000
DOI: 10.1016/j.redox.2023.102927 -
The Journal of Biological Chemistry Dec 2023Pyruvate dehydrogenase (PDH) and α-ketoglutarate dehydrogenase (KGDH) are vital entry points for monosaccharides and amino acids into the Krebs cycle and thus integral... (Review)
Review
Pyruvate dehydrogenase (PDH) and α-ketoglutarate dehydrogenase (KGDH) are vital entry points for monosaccharides and amino acids into the Krebs cycle and thus integral for mitochondrial bioenergetics. Both complexes produce mitochondrial hydrogen peroxide (mHO) and are deactivated by electrophiles. Here, we provide an update on the role of PDH and KGDH in mitochondrial redox balance and their function in facilitating metabolic reprogramming for the propagation of oxidative eustress signals in hepatocytes and how defects in these pathways can cause liver diseases. PDH and KGDH are known to account for ∼45% of the total mHO formed by mitochondria and display rates of production several-fold higher than the canonical source complex I. This mHO can also be formed by reverse electron transfer (RET) in vivo, which has been linked to metabolic dysfunctions that occur in pathogenesis. However, the controlled emission of mHO from PDH and KGDH has been proposed to be fundamental for oxidative eustress signal propagation in several cellular contexts. Modification of PDH and KGDH with protein S-glutathionylation (PSSG) and S-nitrosylation (PSNO) adducts serves as a feedback inhibitor for mHO production in response to glutathione (GSH) pool oxidation. PSSG and PSNO adduct formation also reprogram the Krebs cycle to generate metabolites vital for interorganelle and intercellular signaling. Defects in the redox modification of PDH and KGDH cause the over generation of mHO, resulting in oxidative distress and metabolic dysfunction-associated fatty liver disease (MAFLD). In aggregate, PDH and KGDH are essential platforms for emitting and receiving oxidative eustress signals.
Topics: Hydrogen Peroxide; Ketoglutarate Dehydrogenase Complex; Oxidation-Reduction; Oxidative Stress; Pyruvate Dehydrogenase Complex; Humans; Hepatocytes; Mitochondria, Liver; Non-alcoholic Fatty Liver Disease; Animals; Mice
PubMed: 37898400
DOI: 10.1016/j.jbc.2023.105399 -
International Journal of Molecular... Oct 2023Maintaining normal functions of ovarian granulosa cells (GCs) is essential for oocyte development and maturation. The dysfunction of GCs impairs nutrition supply and...
Maintaining normal functions of ovarian granulosa cells (GCs) is essential for oocyte development and maturation. The dysfunction of GCs impairs nutrition supply and estrogen secretion by follicles, thus negatively affecting the breeding capacity of farm animals. Impaired GCs is generally associated with declines in Nicotinamide adenine dinucleotide (NAD) levels, which triggers un-controlled oxidative stress, and the oxidative stress, thus, attack the subcellular structures and cause cell damage. β-nicotinamide mononucleotide (NMN), a NAD precursor, has demonstrated well-known antioxidant properties in several studies. In this study, using two types of ovarian GCs (mouse GCs (mGCs) and human granulosa cell line (KGN)) as cell models, we aimed to investigate the potential effects of NMN on gene expression patterns and antioxidant capacity of both mGCs and KGN that were exposed to hydrogen peroxide (HO). As shown in results of the study, mGCs that were exposed to HO significantly altered the gene expression patterns, with 428 differentially expressed genes (DEGs) when compared with those of the control group. Furthermore, adding NMN to HO-cultured mGCs displayed 621 DEGs. The functional enrichment analysis revealed that DEGs were mainly enriched in key pathways like cell cycle, senescence, and cell death. Using RT-qPCR, CCK8, and β-galactosidase staining, we found that HO exposure on mGCs obviously reduced cell activity/mRNA expressions of antioxidant genes, inhibited cell proliferation, and induced cellular senescence. Notably, NMN supplementation partially prevented these HO-induced abnormalities. Moreover, these similar beneficial effects of NMN on antioxidant capacity were confirmed in the KGN cell models that were exposed to HO. Taken together, the present results demonstrate that NMN supplementation protects against HO-induced impairments in gene expression pattern, cell cycle arrest, and cell death in ovarian GCs through boosting NAD levels and provide potential strategies to ameliorate uncontrolled oxidative stress in ovarian GCs.
Topics: Female; Humans; Mice; Animals; Nicotinamide Mononucleotide; Hydrogen Peroxide; NAD; Antioxidants; Granulosa Cells; Cell Cycle Checkpoints
PubMed: 37958650
DOI: 10.3390/ijms242115666 -
Nature Communications Aug 2023Polymerization in living systems has become an effective strategy to regulate cell functions and behavior. However, the requirement of high concentrations of monomers,...
Polymerization in living systems has become an effective strategy to regulate cell functions and behavior. However, the requirement of high concentrations of monomers, the existence of complicated intracorporal interferences, and the demand for extra external stimulations hinder their further biological applications. Herein, a nanocompartment-confined strategy that provides a confined and secluded environment for monomer enrichment and isolation is developed to achieve high polymerization efficiency, reduce the interference from external environment, and realize broad-spectrum polymerizations in living systems. For exogenous photopolymerization, the light-mediated free-radical polymerization of sodium 4-styrenesulfonate induces a 2.7-fold increase in the reaction rate with the protection of a confined environment. For endogenous hydrogen peroxide-responsive polymerization, p‑aminodiphenylamine hydrochloride embedded in a nanocompartment not only performs a 6.4-fold higher reaction rate than that of free monomers, but also activates an effective second near-infrared photoacoustic imaging-guided photothermal immunotherapy at tumor sites. This nanocompartment-confined strategy breaks the shackles of conventional polymerization, providing a universal platform for in vivo synthesis of polymers with diverse structures and functions.
Topics: Polymerization; Hydrogen Peroxide; Immunotherapy; Polymers
PubMed: 37634028
DOI: 10.1038/s41467-023-40935-1 -
Journal of Oleo Science 2024External stimuli-responsive worm-like micelles (WLMs) have the potential for a wide range of applications. In particular, sugar (a polyol compound)-responsive WLMs have... (Review)
Review
External stimuli-responsive worm-like micelles (WLMs) have the potential for a wide range of applications. In particular, sugar (a polyol compound)-responsive WLMs have the potential for use in smartdrug release systems. Phenylboronic acid (PBA) functions as a cis-diol sensor in a similar manner it does as a glucose sensor. Thus, WLMs, primarily composed of surfactants and PBA, are expected to function as cis-diol-responsive viscoelastic systems. PBA also reacts irreversibly with hydrogen peroxide (HO ) and is converted into phenol and boric acid. HO is one of reactive oxygen species crucial for several physiological processes. Therefore, HO -responsive WLMs have the potential for various applications. In this review, we describe cis-diol- and HO -responsive micellar systems composed of cetyltrimethylammonium bromide and PBA moieties that shift their viscosities in response to stimuli.
Topics: Micelles; Hydrogen Peroxide; Carbohydrates; Sugars
PubMed: 38556294
DOI: 10.5650/jos.ess22420 -
Redox Biology Sep 2023Tumor hypoxia promotes malignant progression and therapeutic resistance in glioblastoma partly by increasing the production of hydrogen peroxide (HO), a type of reactive...
Tumor hypoxia promotes malignant progression and therapeutic resistance in glioblastoma partly by increasing the production of hydrogen peroxide (HO), a type of reactive oxygen species critical for cell metabolic responses due to its additional role as a second messenger. However, the catabolic pathways that prevent HO overload and subsequent tumor cell damage in hypoxic glioblastoma remain unclear. Herein, we present a hypoxia-coordinated HO regulatory mechanism whereby excess HO in glioblastoma induced by hypoxia is diminished by glutathione peroxidase 1 (GPx1), an antioxidant enzyme detoxifying HO, via the binding of hypoxia-inducible factor-1α (HIF-1α) to GPx1 promoter. Depletion of GPx1 results in HO overload and apoptosis in glioblastoma cells, as well as growth inhibition in glioblastoma xenografts. Moreover, tumor hypoxia increases exosomal GPx1 expression, which assists glioblastoma and endothelial cells in countering HO or radiation-induced apoptosis in vitro and in vivo. Clinical data explorations further demonstrate that GPx1 expression was positively correlated with tumor grade and expression of HIF-1α, HIF-1α target genes, and exosomal marker genes; by contrast, it was inversely correlated with the overall survival outcome in human glioblastoma specimens. Our analyses validate that the redox balance of HO within hypoxic glioblastoma is clinically relevant and could be maintained by HIF-1α-promoted or exosome-related GPx1.
Topics: Humans; Cell Hypoxia; Cell Line, Tumor; Endothelial Cells; Glioblastoma; Glutathione Peroxidase GPX1; Hydrogen Peroxide; Hypoxia; Hypoxia-Inducible Factor 1, alpha Subunit; Oxidative Stress
PubMed: 37572455
DOI: 10.1016/j.redox.2023.102831 -
Proceedings of the National Academy of... Aug 2023Cell-to-cell communication is fundamental to multicellular organisms and unicellular organisms living in a microbiome. It is thought to have evolved as a stress- or...
Cell-to-cell communication is fundamental to multicellular organisms and unicellular organisms living in a microbiome. It is thought to have evolved as a stress- or quorum-sensing mechanism in unicellular organisms. A unique cell-to-cell communication mechanism that uses reactive oxygen species (ROS) as a signal (termed the "ROS wave") was identified in flowering plants. This process is essential for systemic signaling and plant acclimation to stress and can spread from a small group of cells to the entire plant within minutes. Whether a similar signaling process is found in other organisms is however unknown. Here, we report that the ROS wave can be found in unicellular algae, amoeba, ferns, mosses, mammalian cells, and isolated hearts. We further show that this process can be triggered in unicellular and multicellular organisms by a local stress or HO treatment and blocked by the application of catalase or NADPH oxidase inhibitors and that in unicellular algae it communicates important stress-response signals between cells. Taken together, our findings suggest that an active process of cell-to-cell ROS signaling, like the ROS wave, evolved before unicellular and multicellular organisms diverged. This mechanism could have communicated an environmental stress signal between cells and coordinated the acclimation response of many different cells living in a community. The finding of a signaling process, like the ROS wave, in mammalian cells further contributes to our understanding of different diseases and could impact the development of drugs that target for example cancer or heart disease.
Topics: Animals; Reactive Oxygen Species; Hydrogen Peroxide; Signal Transduction; Cell Communication; Plants; Mammals
PubMed: 37494396
DOI: 10.1073/pnas.2305496120