Dietary antioxidants as a source of hydrogen peroxide

Grzesik, Michalina; Bartosz, Grzegorz; Stefaniuk, Ireneusz; Pichla, Monika; Namieśnik, Jacek; Sadowska-Bartosz, Izabela

doi:10.1016/j.foodchem.2018.11.109

Cited by 70 publications

(82 citation statements)

References 30 publications

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“…It is a surprising effect, pointing to the cautious design of experiments and the interpretation of experimental results. We could suggest two reasons for an explanation of this effect (i) during prolonged incubation, more and more catechins are taken up by erythrocytes, which may lead to increase in the osmolarity of cell interior and thus easier hemolysis in hypotonic solutions due to a greater difference in osmolarity between cell interior and exterior; however, this effect does not seem significant at low concentration of catechins employed; (ii) as demonstrated previously, catechins generate hydrogen peroxide during prolonged incubation [34,35]. Hydrogen peroxide may damage the erythrocyte membrane and increase its fragility, including osmotic fragility.…”

Section: Discussionmentioning

confidence: 79%

Interaction of Catechins with Human Erythrocytes

et al. 2020

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The aim of this study was to characterize the interaction of chosen catechins ((+)-catechin, (−)-epigallocatechin (EGC), and (−)-epigallocatechin gallate (EGCG)) with human erythrocytes and their protective effects against oxidative damage of erythrocytes. Uptake of the catechins by erythrocytes was studied by fluorimetry, their interaction with erythrocyte membrane was probed by changes in erythrocyte osmotic fragility and in membrane fluidity evaluated with spin labels, while protection against oxidative damage was assessed by protection against hemolysis induced by permanganate and protection of erythrocyte membranes against lipid peroxidation and protein thiol group oxidation. Catechin uptake was similar for all the compounds studied. Accumulation of catechins in the erythrocyte membrane was demonstrated by the catechin-induced increase in osmotic resistance and rigidification of the erythrocyte membrane detected by spin labels 5-doxyl stearic acid and 16-doxyl stearic acid. (−)-Epigallocatechin and EGCG inhibited erythrocyte acetylcholinesterase (mixed-type inhibition). Catechins protected erythrocytes against permanganate-induced hemolysis, oxidation of erythrocyte protein thiol groups, as well as membrane lipid peroxidation. These results contribute to the knowledge of the beneficial effects of catechins present in plant-derived food and beverages.

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Section: Discussionmentioning

confidence: 79%

Interaction of Catechins with Human Erythrocytes

et al. 2020

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“…Demethylation of JmjC-type enzymes proceeds with a side reaction that produces succinate from α-ketglutarate (α-KG) [ 19 ]. Therefore, reduction of succinate and/or elevation of α-KG positively affected KDM2A activity [ 14 ].…”

Section: Resultsmentioning

confidence: 99%

“…Gallic acid functions as an antioxidant to exert a wide range of pharmacological properties including anti-obesity, anti-inflammation, and anti-cancer activities [ 18 ]. On the other hand, reactive oxygen species (ROS) was also generated when gallic acid was added to the cell culture medium [ 19 ]. Gallic acid autoxidation produced significant levels of H 2 O 2 and O 2 • − (superoxide), and the number of apoptotic cells increased depending on the gallic acid concentration.…”

Section: Introductionmentioning

confidence: 99%

Production of ROS by Gallic Acid Activates KDM2A to Reduce rRNA Transcription

Tanaka

Obinata

Konishi

et al. 2020

Cells

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Metformin, which is suggested to have anti-cancer effects, activates KDM2A to reduce rRNA transcription and proliferation of cancer cells. Thus, the specific activation of KDM2A may be applicable to the treatment of cancers. In this study, we screened a food-additive compound library to identify compounds that control cell proliferation. We found that gallic acid activated KDM2A to reduce rRNA transcription and cell proliferation in breast cancer MCF-7 cells. Gallic acid accelerated ROS production and activated AMPK. When ROS production or AMPK activity was inhibited, gallic acid did not activate KDM2A. These results suggest that both ROS production and AMPK activation are required for activation of KDM2A by gallic acid. Gallic acid did not reduce the succinate level, which was required for KDM2A activation by metformin. Metformin did not elevate ROS production. These results suggest that the activation of KDM2A by gallic acid includes mechanisms distinct from those by metformin. Therefore, signals from multiple intracellular conditions converge in KDM2A to control rRNA transcription. Gallic acid did not induce KDM2A-dependent anti-proliferation activity in non-tumorigenic MCF10A cells. These results suggest that the mechanism of KDM2A activation by gallic acid may be applicable to the treatment of breast cancers.

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“…Polyphenols showing inhibitory effect on TPO activity used in the study and IC50 value, which was calculated at fitted models as the concentration of the tested compound that gave 50% of the maximum response based on a dose-dependent mode of action were presented in Table 3. The results obtained by Grzesik et al [20] showed antiradical properties in grapes (which are a source of quercetin) [21] for a solution concentration of 50 µg/mL at the level of 43.06% in the case of skin, 16.75%-seeds, and 7.01%-flesh. Chlorogenic acid exhibited ABTS radical scavenging activity at a IC 50 value of 0.267 mM, which was higher than the results obtained for quercetin (0.447 mM) and rutin (0.292 mM) but lower than for rosmarinic acid (0.151 mM).…”

Section: Tpo Inhibitory Studiesmentioning

confidence: 94%

Thyroid Peroxidase Activity is Inhibited by Phenolic Compounds—Impact of Interaction

et al. 2019

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The aim of this study was to estimate the mode of thyroid peroxidase (TPO) inhibition by polyphenols: Chlorogenic acid, rosmarinic acid, quercetin, and rutin. All the tested polyphenols inhibited TPO; the IC50 values ranged from 0.004 mM to 1.44 mM (for rosmarinic acid and rutin, respectively). All these pure phytochemical substances exhibited different modes of TPO inhibition. Rutin and rosmarinic acid showed competitive, quercetin—uncompetitive and chlorogenic acid—noncompetitive inhibition effect on TPO. Homology modeling was used to gain insight into the 3D structure of TPO and molecular docking was applied to study the interactions of the inhibitors with their target at the molecular level. Moreover, the type and strength of mutual interactions between the inhibitors (expressed as the combination index, CI) were analyzed. Slight synergism, antagonism, and moderate antagonism were found in the case of the combined addition of the pure polyphenols. Rutin and quercetin as well as rutin and rosmarinic acid acted additively (CI = 0.096 and 1.06, respectively), while rutin and chlorogenic acid demonstrated slight synergism (CI = 0.88) and rosmarinic acid with quercetin and rosmarinic acid with chlorogenic acid showed moderate antagonism (CI = 1.45 and 1.25, respectively). The mixture of chlorogenic acid and quercetin demonstrated antagonism (CI = 1.79). All the polyphenols showed in vitro antiradical ability against 2,2′-azinobis-(3-ethylbenzothiazoline-6-sulfonic acid), ABTS. The highest ability (expressed as IC50) was exhibited by rosmarinic acid (0.12 mM) and the lowest value was ascribed to quercetin (0.45 mM).

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Dietary antioxidants as a source of hydrogen peroxide

Cited by 70 publications

References 30 publications

Interaction of Catechins with Human Erythrocytes

Interaction of Catechins with Human Erythrocytes

Production of ROS by Gallic Acid Activates KDM2A to Reduce rRNA Transcription

Thyroid Peroxidase Activity is Inhibited by Phenolic Compounds—Impact of Interaction

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