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Journal articles on the topic 'Oxidative modification of proteins'

Author: Grafiati

Published: 28 May 2022

Last updated: 30 July 2025

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1

Azarova, D. Y., A. D. Vasilyeva, L. V. Yurina, et al. "Hypochlorite-induced oxidative modification of fibrinogen." Issues of Legal Regulation in Veterinary Medicine, no. 2 (July 11, 2022): 125–27. http://dx.doi.org/10.52419/issn2782-6252.2022.2.125.

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Fibrinogen (FG) is a protein that plays a key role in the hemostasis system and is most susceptible to oxidative modification compared to other plasma proteins. FG undergoes post-translational modifications that can potentially disrupt its structure and function.For the first time, using high resolution mass spectrometry (HPLC/MS/MS), the consequences of hypochlorite (HOCl)- induced FG oxidation were studied, and a list of FG amino acid residue oxidatively modifications. Samples of nonoxidized and treated with 50 μM HOCL fibrinogen were analyzed by mass spectrometry and it was found that many

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Štikarová, Jana, Roman Kotlín, Tomáš Riedel, et al. "The Effect of Reagents Mimicking Oxidative Stress on Fibrinogen Function." Scientific World Journal 2013 (2013): 1–8. http://dx.doi.org/10.1155/2013/359621.

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Fibrinogen is one of the plasma proteins most susceptible to oxidative modification. It has been suggested that modification of fibrinogen may cause thrombotic/bleeding complications associated with many pathophysiological states of organism. We exposed fibrinogen molecules to three different modification reagents—malondialdehyde, sodium hypochlorite, and peroxynitrite—that are presented to various degrees in different stages of oxidative stress. We studied the changes in fibrin network formation and platelet interactions with modified fibrinogens under flow conditions. The fastest modificatio

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3

Burgoyne, Joseph R., and Philip Eaton. "Contemporary techniques for detecting and identifying proteins susceptible to reversible thiol oxidation." Biochemical Society Transactions 39, no. 5 (2011): 1260–67. http://dx.doi.org/10.1042/bst0391260.

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Elevated protein oxidation is a widely reported hallmark of most major diseases. Historically, this ‘oxidative stress’ has been considered causatively detrimental, as the protein oxidation events were interpreted simply as damage. However, recent advances have changed this antiquated view; sensitive methodology for detecting and identifying proteins susceptible to oxidation has revealed a fundamental role for this modification in physiological cell signalling during health. Reversible protein oxidation that is dynamically coupled with cellular reducing systems allows oxidative protein modifica

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4

Kale, Ravindra, Annette E. Hebert, Laurie K. Frankel, Larry Sallans, Terry M. Bricker, and Pavel Pospíšil. "Amino acid oxidation of the D1 and D2 proteins by oxygen radicals during photoinhibition of Photosystem II." Proceedings of the National Academy of Sciences 114, no. 11 (2017): 2988–93. http://dx.doi.org/10.1073/pnas.1618922114.

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The Photosystem II reaction center is vulnerable to photoinhibition. The D1 and D2 proteins, lying at the core of the photosystem, are susceptible to oxidative modification by reactive oxygen species that are formed by the photosystem during illumination. Using spin probes and EPR spectroscopy, we have determined that both O2•− and HO• are involved in the photoinhibitory process. Using tandem mass spectroscopy, we have identified a number of oxidatively modified D1 and D2 residues. Our analysis indicates that these oxidative modifications are associated with formation of HO• at both the Mn4O5C

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Perry, G., D. A. Zelasko, L. M. Sayre, and M. A. Smith. "Oxidative Damage to Axonal Cytoskeletal Proteins." Microscopy and Microanalysis 3, S2 (1997): 43–44. http://dx.doi.org/10.1017/s1431927600007108.

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Proteins of the axonal cytoskeleton, particularly neurofilament and microtubule-associated protein τ, should be particularly sensitive to the effects of oxidative modification due to their high content of lysine, an amino acid that is particularly susceptible to direct oxidization as well as adduction by carbonyls produced from lipid and sugar oxidation. To understand the susceptibility of the cytoskeleton to oxidative modification and whether such modification is related to the physiological function of the cytoskeleton, we undertook a cytological analysis of motor neurons isolated from mouse

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Kurhaluk, Natalia, Małgorzata Dubik-Tota, Krzysztof Tota, and Halina Tkaczenko. "THE INFLUENCE OF AGE, PHYSICAL ACTIVITY, SMOKING AND THE PRESENCE OF MYOCARDIAL INFARCTION AND THYROID DISEASES IN THE FAMILY ON THE LEVEL OF ALDEHYDIC AND KETONIC DERIVATIVES OF OXIDATIVE MODIFICATION OF PROTEINS IN THE BLOOD OF WOMEN AND MEN WITH MYOCARDIAL INFARCTS AND HYPOTHYROIDISM." Biota. Human. Technology, no. 1 (May 20, 2024): 117–42. http://dx.doi.org/10.58407/bht.1.24.11.

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The importance of thyroid hormones in maintaining homeostasis of the cardiovascular system can be inferred from clinical and experimental data showing that even subtle changes in thyroid hormone concentrations - such as those observed in subclinical hypothyroidism or hyperthyroidism and low triiodothyronine syndrome - adversely affect the cardiovascular system. Some potential mechanisms linking the two conditions are dyslipidemia, endothelial dysfunction, changes in blood pressure, and the direct effects of thyroid hormones on the myocardium. Purpose: analysis of changes in the concentration o

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7

Yan, Liang-Jun. "Protein Redox Modification as a Cellular Defense Mechanism against Tissue Ischemic Injury." Oxidative Medicine and Cellular Longevity 2014 (2014): 1–12. http://dx.doi.org/10.1155/2014/343154.

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Protein oxidative or redox modifications induced by reactive oxygen species (ROS) or reactive nitrogen species (RNS) not only can impair protein function, but also can regulate and expand protein function under a variety of stressful conditions. Protein oxidative modifications can generally be classified into two categories: irreversible oxidation and reversible oxidation. While irreversible oxidation usually leads to protein aggregation and degradation, reversible oxidation that usually occurs on protein cysteine residues can often serve as an “on and off” switch that regulates protein functi

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8

Levine, Rodney L., and Earl R. Stadtman. "Oxidative modification of proteins during aging." Experimental Gerontology 36, no. 9 (2001): 1495–502. http://dx.doi.org/10.1016/s0531-5565(01)00135-8.

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9

FU, Shanlin, Min-Xin FU, W. John BAYNES, R. Suzanne THORPE, and T. Roger DEAN. "Presence of dopa and amino acid hydroperoxides in proteins modified with advanced glycation end products (AGEs): amino acid oxidation products as a possible source of oxidative stress induced by AGE proteins." Biochemical Journal 330, no. 1 (1998): 233–39. http://dx.doi.org/10.1042/bj3300233.

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Glycation and subsequent Maillard or browning reactions of glycated proteins, leading to the formation of advanced glycation end products (AGEs), are involved in the chemical modification of proteins during normal aging and have been implicated in the pathogenesis of diabetic complications. Oxidative conditions accelerate the browning of proteins by glucose, and AGE proteins also induce oxidative stress responses in cells bearing AGE receptors. These observations have led to the hypothesis that glycation-induced pathology results from a cycle of oxidative stress, increased chemical modificatio

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10

Rosca, Mariana G., Tiberiu G. Mustata, Michael T. Kinter, et al. "Glycation of mitochondrial proteins from diabetic rat kidney is associated with excess superoxide formation." American Journal of Physiology-Renal Physiology 289, no. 2 (2005): F420—F430. http://dx.doi.org/10.1152/ajprenal.00415.2004.

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Chronic hyperglycemia causes structural alterations of proteins through the Maillard reaction. In diabetes, methylglyoxal (MGO)-induced hydroimidazolones are the predominant modification. In contrast to acute hyperglycemia, mitochondrial respiration is depressed in chronic diabetes. To determine whether MGO-derived protein modifications result in abnormalities in mitochondrial bioenergetics and superoxide formation, proteomics and functional studies were performed in renal cortical mitochondria isolated from rats with 2, 6, and 12 mo of streptozotocin-induced diabetes. MGO-modified proteins be

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11

Chen, Jiaxin, Jinhai Zhao, Baohua Kong, Qian Chen, Qian Liu, and Chengguo Liu. "Comparative Study of Oxidative Structural Modifications of Unadsorbed and Adsorbed Proteins in Whey Protein Isolate-Stabilized Oil-in-Water Emulsions under the Stress of Primary and Secondary Lipid Oxidation Products." Foods 10, no. 3 (2021): 593. http://dx.doi.org/10.3390/foods10030593.

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The impact of typical primary or secondary lipid oxidation (LPO) products, selected as linoleic acid 13-hydroperoxide (13-HPODE) and malondialdehyde (MDA), on the structural modification of unadsorbed or adsorbed proteins in whey protein isolate (WPI)-stabilized oil-in-water (O/W) emulsions during storage up to 48 h at 37 °C in the dark was investigated. The results showed that either 13-HPODE and MDA could lead to structural modifications of unadsorbed or adsorbed proteins with a concentration-dependent manner and time relationship, respectively. Moreover, higher levels of MDA rendered a high

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12

Fomina, M. A., A. M. Kudlaeva, S. A. Isakov та A. N. Ryabkov. "Influence of L-Nω-nitroarginine methyl ester and sodium nitroprusside in vitro on the oxidative modification of rat lysosome proteins". Kazan medical journal 98, № 6 (2017): 1005–11. http://dx.doi.org/10.17750/kmj2017-1005.

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Aim. To investigate in vitro effects of 5 mM L-Nω-nitroarginine methyl ester and 0.1 mM sodium nitroprusside on oxidative modification of lysosomal proteins of liver of intact sexually mature female rats of Wistar line. Methods. In the control groups in vitro incubation of isolated lysosomes in the isolation medium for 1, 2 and 4 hours was carried out. Experimental groups were incubated similarly in solutions of 5 mM L-Nω-nitroarginine methyl ester and 0.1 mM sodium nitroprusside. Protein oxidative modification was measured in sedimentary fraction according to R.L. Levine’s method in E.E. Dubi

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13

Nosareva, O. L., and E. A. Stepovaya. "Role of oxidative modification of proteins in the regulation and realization of cell death of blood lymphocytes under the conditions of blocking glutathione synthesis under oxidative stress." Medical Immunology (Russia) 26, no. 4 (2024): 671–76. http://dx.doi.org/10.15789/1563-0625-roo-16615.

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Lymphocytes are key cells in inflammation. The realization of inflammation accompanied by the development of oxidative stress depends on metabolic processes occurring in blood lymphocytes. Experimental studies of molecular control of the redox status and apoptotic death of blood lymphocytes are relevant to study the role of lymphocytes in the pathogenesis of inflammation. The glutathione system plays a leading role in maintaining the redox status and oxidative modification of blood lymphocyte proteins. The study of molecular mechanisms of oxidative modification of proteins under the conditions

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14

Zagorulya, I. P., V. E. Vysokogorskyi, O. N. Lazareva, and G. V. Ignatieva. "Oxidative modification of milk proteins at pasteurization." Dairy Industry, no. 7 (2019): 28–29. http://dx.doi.org/10.31515/1019-8946-2019-7-28-29.

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15

Chakravarti, Bulbul, and Deb N. Chakravarti. "Oxidative Modification of Proteins: Age-Related Changes." Gerontology 53, no. 3 (2007): 128–39. http://dx.doi.org/10.1159/000097865.

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16

Hensley, Kenneth, and Robert A. Floyd. "Oxidative Modification of Proteins in Cell Signaling." Antioxidants & Redox Signaling 7, no. 5-6 (2005): 523–25. http://dx.doi.org/10.1089/ars.2005.7.523.

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17

Mele, M. C., and E. Meucci. "Homocysteine and oxidative modification of plasma proteins." Amino Acids 11, no. 1 (1996): 99–104. http://dx.doi.org/10.1007/bf00805725.

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18

Ren, Yuwei, Feng Wang, Ruiping Sun, et al. "N-glycosylation Modification Reveals Insights into the Oxidative Reactions of Liver in Wuzhishan Pigs." Molecules 29, no. 22 (2024): 5222. http://dx.doi.org/10.3390/molecules29225222.

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Although porcine liver contributes to their growth and development by nutrition production and energy supply, oxidative stress-induced hepatocyte damage is inevitable during metabolism. N-glycosylation is a common modification in oxidation; nevertheless, the effects of N-glycosylation on pig liver oxidative reactions remain undefined. In this study, liver proteins with N-glycosylation were detected in Wuzhishan (WZS) pigs between 4 and 8 months old and Large White (LW) pigs at 4 months old based on LC-MS/MS. The results showed that the number of differentially expressed proteins (DEPs) was lar

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19

Tuharov, Yurij, and Kateryna Dvorshchenko. "OXIDATIVE MODIFICATION OF PROTEINS IN BLOOD PLASMA OF PATIENTS WITH OSTEOARTHRITIS AFTER SARS-CoV2 INFECTION." Bulletin of Taras Shevchenko National University of Kyiv. Series: Biology 97, no. 2 (2024): 22–27. http://dx.doi.org/10.17721/1728.2748.2024.97.22-27.

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Background. The outbreak of severe acute respiratory syndrome caused by SARS-CoV-2 (severe acute respiratory syndrome-related coronavirus 2) in 2019 caused the development of pandemic of coronavirus disease 2019 (COVID-19). Since its onset, many symptoms of the disease have been associated with acute SARS-CoV-2 infection, as well as with long-term sequelae in patients with COVID-19. Among these symptoms are various categories of diseases of the musculoskeletal system, including osteoarthritis. It is known that the osteoarthritis development is associated with oxidative stress and excessive pro

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20

Vyushina, A. V., A. V. Pritvorova, S. G. Pivina, V. K. Akulova, and N. E. Ordyan. "The Effect of Various Types of Mother Stress on the Some Components of the Brain Redox System in Male and Female Rats on the 20th Day of the Embryonic Development Period." Nejrohimiâ 41, no. 4 (2024): 362–71. https://doi.org/10.31857/s1027813324040077.

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The effect of prenatal stress, post-traumatic stress disorder, and their combined effect in rat mothers on the condition of the pituitary-adrenal system and the brain redox balance in 20-day-old embryos was studied. Mother’s prenatal stress result in increase the level’s corticosterone in the blood and decrease the level of reduced glutathione in the brain of male embryos. In female embryos, the level of Fenton-induced products of proteins oxidative modification increased and the reduced glutathione level in the brain decreased. Modeling of post-traumatic stress disorder in mother result in an

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21

Cadenas-Garrido, Paula, Ailén Schonvandt-Alarcos, Lourdes Herrera-Quintana, et al. "Using Redox Proteomics to Gain New Insights into Neurodegenerative Disease and Protein Modification." Antioxidants 13, no. 1 (2024): 127. http://dx.doi.org/10.3390/antiox13010127.

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Antioxidant defenses in biological systems ensure redox homeostasis, regulating baseline levels of reactive oxygen and nitrogen species (ROS and RNS). Oxidative stress (OS), characterized by a lack of antioxidant defenses or an elevation in ROS and RNS, may cause a modification of biomolecules, ROS being primarily absorbed by proteins. As a result of both genome and environment interactions, proteomics provides complete information about a cell’s proteome, which changes continuously. Besides measuring protein expression levels, proteomics can also be used to identify protein modifications, loc

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Yang, Mei-Ling, Sean Connolly, Li Wen, Kevan Herold, and Mark Mamula. "Identification of posttranslational modified autoantigens in Type 1 diabetes. (P4152)." Journal of Immunology 190, no. 1_Supplement (2013): 172.3. http://dx.doi.org/10.4049/jimmunol.190.supp.172.3.

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Abstract Autoimmune diseases such as lupus, rheumatoid arthritis, multiple sclerosis, and type 1 diabetes (T1D) frequently target self proteins that undergo posttranslational protein modifications. Oxidative stress, which is implicated in the pathogenesis of T1D, leads to various protein modifications including isoaspartyl (isoAsp) and carbonyl formation. We have previously identified that isoAsp protein modification can trigger T cell autoimmunity in both human and murine models of lupus. However, the role of oxidative stress-induced posttranslational modifications in T1D is still poorly unde

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23

Ketsa, O. V., M. V. Zazulyk та M. V. Himchak. "Інтенсивність окисних процесів у мікросомній фракції печінки щурів за умов різного забезпечення поліненасиченими жирними кислотами". Visnyk of Dnipropetrovsk University. Biology, medicine 5, № 1 (2014): 12–16. http://dx.doi.org/10.15421/021403.

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The effect of fat compositions with the varying ratio of polyunsaturated fatty acids (PUFAs) of families ω-3 and ω-6 on oxidation process intensity in microsomal fraction of rat liver has been investigated. The aim of the study was to investigate the level of markers of oxidative modification of lipids and proteins in microsomal fraction of rat liver. Fat components in the experiment diets were presented by sunflower oil, soybean oil and fish oil. Rats were fed using one of the fillowing 5 diets for the period of 4 weeks: 1) AIN-93 diet with 7% sunflower oil and fish oil, with the inclusion of

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Pitt, Andrew R., and Corinne M. Spickett. "Mass spectrometric analysis of HOCl- and free-radical-induced damage to lipids and proteins." Biochemical Society Transactions 36, no. 5 (2008): 1077–82. http://dx.doi.org/10.1042/bst0361077.

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In inflammatory diseases, release of oxidants leads to oxidative damage to biomolecules. HOCl (hypochlorous acid), released by the myeloperoxidase/H2O2/Cl− system, can cause formation of phospholipid chlorohydrins, or α-chloro-fatty aldehydes from plasmalogens. It can attack several amino acid residues in proteins, causing post-translational oxidative modifications of proteins, but the formation of 3-chlorotyrosine is one of the most stable markers of HOCl-induced damage. Soft-ionization MS has proved invaluable for detecting the occurrence of oxidative modifications to both phospholipids and

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Sadowska-Bartosz, Izabela, Monika Adamczyk-Sowa, Sabina Galiniak, Sebastian Mucha, Krystyna Pierzchala, and Grzegorz Bartosz. "Oxidative modification of serum proteins in multiple sclerosis." Neurochemistry International 63, no. 5 (2013): 507–16. http://dx.doi.org/10.1016/j.neuint.2013.08.009.

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26

LUSHCHAK, V., and D. GOSPODARYOV. "Catalases protect cellular proteins from oxidative modification in." Cell Biology International 29, no. 3 (2005): 187–92. http://dx.doi.org/10.1016/j.cellbi.2004.11.001.

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27

Starke-Reed, Pamela E., Cynthia N. Oliver, John M. Carney, and Earl R. Stadtman. "Modification of proteins during oxidative stress and aging." Free Radical Biology and Medicine 15, no. 5 (1993): 479. http://dx.doi.org/10.1016/0891-5849(93)90215-g.

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28

Zhao, Jinjin, Miaomiao Han, Qingzhi Wu, Xiaoying Mao, Jian Zhang, and Zhenkang Lu. "Effect of Oxidative Modification by Peroxyl Radical on the Characterization and Identification of Oxidative Aggregates and In Vitro Digestion Products of Walnut (Juglans regia L.) Protein Isolates." Foods 11, no. 24 (2022): 4104. http://dx.doi.org/10.3390/foods11244104.

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Walnut protein is a key plant protein resource due to its high nutritional value, but walnuts are prone to oxidation during storage and processing. This article explored the oxidative modification and digestion mechanism of walnut protein isolates by peroxyl radical and obtained new findings. SDS-PAGE and spectral analysis were used to identify structural changes in the protein after oxidative modification, and LC-MS/MS was used to identify the digestion products. The findings demonstrated that as the AAPH concentration increased, protein carbonyl content increased from 2.36 to 5.12 nmol/mg, w

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29

Semko, G. O., O. A. Sokol, and H. K. Kondakova. "OXIDATIVE MODIFICATION OF BLOOD PLASMA PROTEINS OF PATIENTS WITH PSORIASIS VULGARIS." Dermatology and Venerology, no. 3 (2022): 7–9. http://dx.doi.org/10.33743/2308-1066-2022-3-7-9.

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The aim is to study the state of indicators of oxidative modification of proteins in the blood plasma of patients with psoriasis vulgaris. Materials and Methods. 18 patients with psoriasis vulgaris (average age – 44.4 years) and a group of healthy donors – 22 persons, who made up the control group – were examined. Oxidative modification of proteins was determined in blood plasma by reaction with 2,4-dinitrophenylhydrazine. Results In patients with psoriasis vulgaris, significant violations of the processes of oxidative modification of blood plasma proteins (spontaneous and metal-catalyzed) wer

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Hawkins, Clare L. "Hypochlorous acid-mediated modification of proteins and its consequences." Essays in Biochemistry 64, no. 1 (2019): 75–86. http://dx.doi.org/10.1042/ebc20190045.

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Abstract Myeloperoxidase (MPO) is a mammalian heme peroxidase released by activated immune cells, which forms chemical oxidants, including hypochlorous acid (HOCl), to kill bacteria and other invading pathogens. In addition to this important role in the innate immune system, there is significant evidence from numerous chronic inflammatory pathologies for the elevated production of HOCl and associated oxidative modification of proteins and damage to host tissue. Proteins are major targets for HOCl in biological systems, owing to their abundance and the high reactivity of several amino acid side

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Čolak, Emina. "New Markers of Oxidative Damage to Macromolecules." Journal of Medical Biochemistry 27, no. 1 (2008): 1–16. http://dx.doi.org/10.2478/v10011-007-0049-x.

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New Markers of Oxidative Damage to Macromolecules The presence of free radicals in biological material has been discovered some 50 years ago. In physiological conditions, free radicals, in the first place the ones of oxygen and nitrogen, are continuously synthesized and involved in the regulation of a series of physiological processes. The excess of free radicals is efficiently eliminated from the body in order to prevent their toxic effects. Toxic effects of free radicals may be classified into three groups: a) change of intracellular redox potential, b) oxidative modification of lipids, prot

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Vrettou, Sofia, and Brunhilde Wirth. "S-Glutathionylation and S-Nitrosylation in Mitochondria: Focus on Homeostasis and Neurodegenerative Diseases." International Journal of Molecular Sciences 23, no. 24 (2022): 15849. http://dx.doi.org/10.3390/ijms232415849.

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Redox post-translational modifications are derived from fluctuations in the redox potential and modulate protein function, localization, activity and structure. Amongst the oxidative reversible modifications, the S-glutathionylation of proteins was the first to be characterized as a post-translational modification, which primarily protects proteins from irreversible oxidation. However, a growing body of evidence suggests that S-glutathionylation plays a key role in core cell processes, particularly in mitochondria, which are the main source of reactive oxygen species. S-nitrosylation, another

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Shakhristova, Ye V., Ye A. Stepovaya, V. V. Ivanov, O. L. Nosareva, N. V. Ryazantseva, and V. V. Novitsky. "OXIDATIVE MODIFICATION OF PROTEINS AND GLUTATHIONE SYSTEM IN ADIPOCYTES UNDER DIABETES." Bulletin of Siberian Medicine 13, no. 3 (2014): 84–90. http://dx.doi.org/10.20538/1682-0363-2014-3-84-90.

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Currently, diabetes ranks third in relation to medical and social significance after cardiovascular diseases and cancer and is the leading cause of blindness; it greatly increases the risk of myocardial infarction, coronary heart disease, nephropathy and hypertension in patients with this disorder; therefore clinical and experimental studies aimed at investigation of diabetes emergence and development mechanisms are urgent.The aim of the study was to investigate the status of oxidative modification of proteins and glutathionedependent antioxidant defense system in adipocytes of rats with allox

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Olszowski, S., E. Olszowska, T. Stelmaszyńska, A. Krawczyk, J. Marcinkiewicz, and N. Baczek. "Oxidative modification of ovalbumin." Acta Biochimica Polonica 43, no. 4 (1996): 661–72. http://dx.doi.org/10.18388/abp.1996_4462.

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Stimulated neutrophils (PMNL) are a source of the active oxygen species: O2, H2O2 and HOCl/OCl- which in turn can act on proteins yielding a variety of mixed oxidation products. A system is proposed in which a model protein-ovalbumin (OVA) first undergoes chlorination by HOCl/OCl- and next is oxidised by H2O2. The modification of functional groups (-NH2, -SH, -S-S-, > C = O, Tyr and Trp) in OVA was monitored as well as their accessibility to promote aggregation. Chlorination resulted in additional inter- or intra -S-S- bond formation followed by a decrease in the total sulfhydryl group cont

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Kumar, Aditya, Ankush Prasad, Michaela Sedlářová, et al. "Tocopherol controls D1 amino acid oxidation by oxygen radicals in Photosystem II." Proceedings of the National Academy of Sciences 118, no. 4 (2021): e2019246118. http://dx.doi.org/10.1073/pnas.2019246118.

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Photosystem II (PSII) is an intrinsic membrane protein complex that functions as a light-driven water:plastoquinone oxidoreductase in oxygenic photosynthesis. Electron transport in PSII is associated with formation of reactive oxygen species (ROS) responsible for oxidative modifications of PSII proteins. In this study, oxidative modifications of the D1 and D2 proteins by the superoxide anion (O2•−) and the hydroxyl (HO•) radicals were studied in WT and a tocopherol cyclase (vte1) mutant, which is deficient in the lipid-soluble antioxidant α-tocopherol. In the absence of this antioxidant, high-

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Verveha, B. M., B. V. Gutyj, S. H. Lishchuk, M. I. Holubiev, and R. V. Mylostyvyi. "Oxidative modification of proteins and antioxidant status in blood of the rats with experimental acute generalized peritonitis against the background of streptozotocin-induced diabetes." Regulatory Mechanisms in Biosystems 14, no. 2 (2023): 260–65. http://dx.doi.org/10.15421/022338.

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Modern aspects of the pathogenesis of acute inflammation of the peritoneum that is concurrent with diabetes involves analysis of metabolic mechanisms, in particular peroxidaton of proteins – antioxidant defense. Therefore, the objective of our study was to examine the interrelation between the processes of free-radical oxidation of proteins and antioxidant system in the dynamics of development of acute generalized peritonitis against the background of streptozotocin-induced diabetes. The study was performed on 56 non-linear white mature male rats. Diabetes mellitus was modeled by a single intr

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Jonak, Katarzyna, Ida Suppanz, Julian Bender, Agnieszka Chacinska, Bettina Warscheid, and Ulrike Topf. "Ageing-dependent thiol oxidation reveals early oxidation of proteins with core proteostasis functions." Life Science Alliance 7, no. 5 (2024): e202302300. http://dx.doi.org/10.26508/lsa.202302300.

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Oxidative post-translational modifications of protein thiols are well recognized as a readily occurring alteration of proteins, which can modify their function and thus control cellular processes. The development of techniques enabling the site-specific assessment of protein thiol oxidation on a proteome-wide scale significantly expanded the number of known oxidation-sensitive protein thiols. However, lacking behind are large-scale data on the redox state of proteins during ageing, a physiological process accompanied by increased levels of endogenous oxidants. Here, we present the landscape of

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Shevelkova, Anna Aleksandrovna, and Anna Vadimovna Vyushina. "Oxidative modification of proteins and content of reduced thiols in blood in physiological pregnancy." Journal of obstetrics and women's diseases 61, no. 4 (2012): 109–12. http://dx.doi.org/10.17816/jowd614109-112.

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We studied the level of oxidative modification of proteins and the state of the antioxidant system in 17 healthy pregnant and 33 healthy nonpregnant women. Absence of any reliable differences in the levels of oxidative modification of proteins in both groups and considerable decrease of the reduced thiols' level in pregnant women were found. This is apparently explained as the reduced thiols are used more actively in physiological pregnancy

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Clemen, Ramona, and Sander Bekeschus. "Oxidatively Modified Proteins: Cause and Control of Diseases." Applied Sciences 10, no. 18 (2020): 6419. http://dx.doi.org/10.3390/app10186419.

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Proteins succumb to numerous post-translational modifications (PTMs). These relate to enzymatic or non-enzymatic reactions taking place in either the intracellular or extracellular compartment. While intracellular oxidative changes are mainly due to redox stress, extracellular PTMs may be induced in an inflammatory micro milieu that is rich in reactive species. The increasing recognition of oxidative modifications as a causing agent or side-effect of pathophysiological states and diseases puts oxidative PTMS (oxPTMs) into the spotlight of inflammation research. Pathological hyper-modification

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Tramutola, Antonella, Fabio Di Domenico, Eugenio Barone, Marzia Perluigi, and D. Allan Butterfield. "It Is All about (U)biquitin: Role of Altered Ubiquitin-Proteasome System and UCHL1 in Alzheimer Disease." Oxidative Medicine and Cellular Longevity 2016 (2016): 1–12. http://dx.doi.org/10.1155/2016/2756068.

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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 acce

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Campolo, Nicolás, Federico M. Issoglio, Darío A. Estrin, Silvina Bartesaghi, and Rafael Radi. "3-Nitrotyrosine and related derivatives in proteins: precursors, radical intermediates and impact in function." Essays in Biochemistry 64, no. 1 (2020): 111–33. http://dx.doi.org/10.1042/ebc20190052.

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Abstract Oxidative post-translational modification of proteins by molecular oxygen (O2)- and nitric oxide (•NO)-derived reactive species is a usual process that occurs in mammalian tissues under both physiological and pathological conditions and can exert either regulatory or cytotoxic effects. Although the side chain of several amino acids is prone to experience oxidative modifications, tyrosine residues are one of the preferred targets of one-electron oxidants, given the ability of their phenolic side chain to undergo reversible one-electron oxidation to the relatively stable tyrosyl radical

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Tiulienieva, O. A. "Histochemical Study of the Processes of Protein Oxidative Modification and Limited Proteolysis in the Endothelium of Myometrial Vessels in the Projection of the Utero-Placental Bed during Iron-Deficiency Anemia in Pregnancy." Ukraïnsʹkij žurnal medicini, bìologìï ta sportu 6, no. 4 (2021): 58–63. http://dx.doi.org/10.26693/jmbs06.04.058.

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Utero-placental bed is the cumulation of gestationally altered endometrium at the place of ovum attachment to the uterine wall. As far as the protein oxidative modification and limited proteolysis in iron deficiency anemia are due to the fact that in conditions of hypoxia, free radical processes in the blood and tissues are enhanced, and iron deficiency is additionally able to cause hemodynamic disorders because of endothelial dysfunction in the vessels of the utero-placental area. The purpose of the study was to establish histochemical features of protein oxidative modification and limited pr

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Tiulienieva, O. A., I. S. Davydenko, A. V. Hoian, and V. O. Tiulienieva. "Histochemical Evaluation of the Processes of Protein Oxidative Modification in the Extravillous Cytotrophoblast of the Utero-Placental Bed during Iron-Deficiency Anemia in Pregnancy." Ukraïnsʹkij žurnal medicini, bìologìï ta sportu 6, no. 1 (2021): 46–51. http://dx.doi.org/10.26693/jmbs06.01.046.

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Utero-placental bed is the cumulation of gestationally altered endometrium at the place of ovum attachment to the uterine wall. The key mechanism of this process is the cytotrophoblastic invasion. During iron deficiency anemia, an increase in the specific volume of the extravascular invasive trophoblast is taking place. Concern for the protein oxidative modification in iron deficiency anemia is due to the fact that in conditions of hypoxia, free radical processes in the blood and tissues are enhanced, and iron deficiency is additionally able to modify this problem. The purpose of the study was

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Dvorshchenko, Kateryna, and Sergiy Borodin. "OXIDATIVE MODIFICATION OF PROTEINS IN THE SYNOVIAL FLUID OF PATIENTS WITH OSTEOARTHRITIS AFTER SARS-CoV 2-INFECTION." Bulletin of Taras Shevchenko National University of Kyiv. Series: Biology 93, no. 2 (2023): 5–9. http://dx.doi.org/10.17721/1728.2748.2023.93.5-9.

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The pandemic of coronavirus disease 2019 (COVID-19) caused by the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) has made a serious public health threat worldwide. It has caused many complications and deaths, so millions of people are at risk in more and more countries. A special group consists of patients with chronic diseases, particularly osteoarthritis. It is known that the development of osteoarthritis is associated with oxidative stress and excessive production of free radicals. Proteins are highly sensitive to free radical oxidation, so their oxidation level reflects the o

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SUZUKI, DAISUKE, TOSHIO MIYATA, NOBORU SAOTOME, et al. "Immunohistochemical Evidence for an Increased Oxidative Stress and Carbonyl Modification of Proteins in Diabetic Glomerular Lesions." Journal of the American Society of Nephrology 10, no. 4 (1999): 822–32. http://dx.doi.org/10.1681/asn.v104822.

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Abstract. Advanced glycation end products (AGE) include a variety of protein adducts whose accumulation has been implicated in tissue damage associated with diabetic nephropathy (DN). It was recently demonstrated that among AGE, glycoxidation products, whose formation is closely linked to oxidation, such as carboxymethyllysine (CML) and pentosidine, accumulate in expanded mesangial matrix and nodular lesions in DN, in colocalization with malondialdehyde-lysine (MDA-lysine), a lipoxidation product, whereas pyrraline, another AGE structure whose deposition is rather independent from oxidative st

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Bruckdorfer, Richard, and Catherine Rice-Evans. "Haem proteins and oxidative modification of low-density lipoproteins." Free Radical Biology and Medicine 9 (January 1990): 68. http://dx.doi.org/10.1016/0891-5849(90)90408-b.

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Gergondey, Rachel, Camille Garcia, Christophe H. Marchand, Stephane D. Lemaire, Jean-Michel Camadro, and Françoise Auchère. "Modulation of the specific glutathionylation of mitochondrial proteins in the yeast Saccharomyces cerevisiae under basal and stress conditions." Biochemical Journal 474, no. 7 (2017): 1175–93. http://dx.doi.org/10.1042/bcj20160927.

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The potential biological consequences of oxidative stress and changes in glutathione levels include the oxidation of susceptible protein thiols and reversible covalent binding of glutathione to the –SH groups of proteins by S-glutathionylation. Mitochondria are central to the response to oxidative stress and redox signaling. It is therefore crucial to explore the adaptive response to changes in thiol-dependent redox status in these organelles. We optimized the purification protocol of glutathionylated proteins in the yeast Saccharomyces cerevisiae and present a detailed proteomic analysis of t

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Baraibar, Martin A., Liang Liu, Emad K. Ahmed, and Bertrand Friguet. "Protein Oxidative Damage at the Crossroads of Cellular Senescence, Aging, and Age-Related Diseases." Oxidative Medicine and Cellular Longevity 2012 (2012): 1–8. http://dx.doi.org/10.1155/2012/919832.

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Protein damage mediated by oxidation, protein adducts formation with advanced glycated end products and with products of lipid peroxidation, has been implicated during aging and age-related diseases, such as neurodegenerative diseases. Increased protein modification has also been described upon replicative senescence of human fibroblasts, a valid model for studying agingin vitro. However, the mechanisms by which these modified proteins could impact on the development of the senescent phenotype and the pathogenesis of age-related diseases remain elusive. In this study, we performedin silicoappr

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Zergeroglu, Murat A., Michael J. McKenzie, R. Andrew Shanely, Darin Van Gammeren, Keith C. DeRuisseau, and Scott K. Powers. "Mechanical ventilation-induced oxidative stress in the diaphragm." Journal of Applied Physiology 95, no. 3 (2003): 1116–24. http://dx.doi.org/10.1152/japplphysiol.00824.2002.

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Prolonged mechanical ventilation (MV) results in oxidative damage in the diaphragm; however, it is unclear whether this MV-induced oxidative injury occurs rapidly or develops slowly over time. Furthermore, it is unknown whether both soluble (cytosolic) and insoluble (myofibrillar) proteins are equally susceptible to oxidation during MV. These experiments tested two hypotheses: 1) MV-induced oxidative injury in the diaphragm occurs within the first 6 h after the initiation of MV; and 2) MV is associated with oxidative modification of both soluble and insoluble proteins. Adult Sprague-Dawley rat

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Sánchez-Gómez, Francisco J., Cristina Espinosa-Díez, Megha Dubey, Madhu Dikshit, and Santiago Lamas. "S-glutathionylation: relevance in diabetes and potential role as a biomarker." Biological Chemistry 394, no. 10 (2013): 1263–80. http://dx.doi.org/10.1515/hsz-2013-0150.

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Abstract Glutathione is considered the main regulator of redox balance in the cellular milieu due to its capacity for detoxifying deleterious molecules. The oxidative stress induced as a result of a variety of stimuli promotes protein oxidation, usually at cysteine residues, leading to changes in their activity. Mild oxidative stress, which may take place in physiological conditions, induces the reversible oxidation of cysteines to sulfenic acid form, while pathological conditions are associated with higher rates of reactive oxygen species production, inducing the irreversible oxidation of cys

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