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Journal articles on the topic 'Advanced oxidation protein product'

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Author: Grafiati
Published: 9 March 2023

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1

Baskol, Mevlut, Gulden Baskol, Derya Koçer, Omer Ozbakir, and Mehmet Yucesoy. "Advanced Oxidation Protein Products." Journal of Clinical Gastroenterology 42, no. 6 (July 2008): 687–91. http://dx.doi.org/10.1097/mcg.0b013e318074f91f.

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2

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 (February 15, 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 modification of proteins via the Maillard reaction, and further AGE-dependent oxidative stress. Here we show that the preparation of AGE-collagen by incubation with glucose under oxidative conditions in vitro leads not only to glycation and formation of the glycoxidation product Nε-(carboxymethyl)lysine (CML), but also to the formation of amino acid oxidation products on protein, including m-tyrosine, dityrosine, dopa, and valine and leucine hydroperoxides. The formation of both CML and amino acid oxidation products was prevented by anaerobic, anti-oxidative conditions. Amino acid oxidation products were also formed when glycated collagen, prepared under anti-oxidative conditions, was allowed to incubate under aerobic conditions that led to the formation of CML. These experiments demonstrate that amino acid oxidation products are formed in proteins during glycoxidation reactions and suggest that reactive oxygen species formed by redox cycling of dopa or by the metal-catalysed decomposition of amino acid hydroperoxides, rather than by redox activity or reactive oxygen production by AGEs on protein, might contribute to the induction of oxidative stress by AGE proteins.
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3

Deng, Quanwen, Can Bu, Liqian Mo, Bin Lv, Shaolian Song, Xiaoyan Xiao, Guo Dan, and Xixiao Yang. "Huang Gan Formula Eliminates the Oxidative Stress Effects of Advanced Oxidation Protein Products on the Divergent Regulation of the Expression of AGEs Receptors via the JAK2/STAT3 Pathway." Evidence-Based Complementary and Alternative Medicine 2017 (2017): 1–11. http://dx.doi.org/10.1155/2017/4520916.

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Chronic kidney disease (CKD) has a high prevalence and low cure rate and represents a significant health issue. Oxidative stress is common in CKD due to metabolic disorders, inflammation, and impaired renal function changing normal proteins into advanced oxidation protein products (AOPPs). Huang Gan formula (HGF) is a new type of traditional Chinese herbal medicine. Although we previously investigated the protective effects of HGF against oxidative stress, the mechanism of HGF in CKD is still not fully understood. In this study, we used western blotting, quantitative polymerase chain reaction, and biochemical assays to show that HGF significantly decreased AOPP-induced oxidative stress damage. Moreover, the protective effects of HGF might be associated with upregulation of the advanced glycation end product receptor 1 (AGE-R1) and downregulation of the receptor for advance glycation end products (RAGE). Treatment with HGF and the Janus kinase 2 (JAK2) inhibitor, AG4-90, significantly attenuated AOPP-induced JAK2/STAT3 protein levels. These findings indicate that HGF inhibits AOPP-mediated biological responses by inactivating the JAK2/STAT3 pathway. In conclusion, HGF eliminated AOPP-induced effects in human mesangial cells (HMCs) by interrupting JAK2/STAT3 signaling, which altered RAGE/AGE-R1 expression and reduced oxidative stress in CKD.
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4

Wölk, Michele, Theres Schröter, Ralf Hoffmann, and Sanja Milkovska-Stamenova. "Profiling of Low-Molecular-Weight Carbonyls and Protein Modifications in Flavored Milk." Antioxidants 9, no. 11 (November 23, 2020): 1169. http://dx.doi.org/10.3390/antiox9111169.

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Thermal treatments of dairy products favor oxidations, Maillard reactions, and the formation of sugar or lipid oxidation products. Additives including flavorings might enhance these reactions or even induce further reactions. Here we aimed to characterize protein modifications in four flavored milk drinks using samples along the production chain—raw milk, pasteurization, mixing with flavorings, heat treatment, and the commercial product. Therefore, milk samples were analyzed using a bottom up proteomics approach and a combination of data-independent (MSE) and data-dependent acquisition methods (DDA). Twenty-one small carbonylated lipids were identified by shotgun lipidomics triggering 13 protein modifications. Additionally, two Amadori products, 12 advanced glycation end products (AGEs), and 12 oxidation-related modifications were targeted at the protein level. The most common modifications were lactosylation, formylation, and carboxymethylation. The numbers and distribution of modification sites present in raw milk remained stable after pasteurization and mixing with flavorings, while the final heat treatment significantly increased lactosylation and hexosylation in qualitative and quantitative terms. The processing steps did not significantly affect the numbers of AGE-modified, oxidized/carbonylated, and lipid-carbonylated sites in proteins.
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5

Luceri, Cristina, Elisabetta Bigagli, Sara Agostiniani, Francesco Giudici, Daniela Zambonin, Stefano Scaringi, Ferdinando Ficari, Maura Lodovici, and Cecilia Malentacchi. "Analysis of Oxidative Stress-Related Markers in Crohn’s Disease Patients at Surgery and Correlations with Clinical Findings." Antioxidants 8, no. 9 (September 6, 2019): 378. http://dx.doi.org/10.3390/antiox8090378.

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Crohn’ disease (CD) patients are at high risk of postoperative recurrence and new tools for the assessment of disease activity are needed to prevent long-term complications. In these patients, the over-production of ROS generated by inflamed bowel tissue and inflammatory cells activates a pathogenic cascade that further exacerbates inflammation and leads to increased oxidative damage to DNA, proteins, and lipids. We measured the products of protein/lipid oxidation and the total antioxidant capacity (ferric reducing ability of plasma, FRAP) in the serum of CD patients with severe disease activity requiring surgery with the aim to characterize their redox status and identify associations between oxidative stress-related markers and their clinical characteristics. At the systemic level, CD was associated with increased levels of protein and lipid oxidation products when compared to healthy volunteers, even though the FRAP values were similar. Advanced oxidation protein product (AOPP) levels showed the highest difference between patients and the controls (11.25, 5.02–15.15, vs. 1.36, 0.75–2.70, median, interquartile range; p < 0.0001) and the analysis of receiver operating characteristic (ROC) curves, indicated for AOPP, the best area under the curve (AUC) value for CD prediction. Advanced glycated end-products (AGEs) were also significantly higher in CD patients (p < 0.01), which is of interest since AOPP and AGEs are both able to activate the membrane receptor for advanced glycation end products (RAGE) involved in inflammatory diseases. Thiobarbituric acid reactive substance (TBARS) levels were significantly higher in CD patients with ileal localization and aggressive disease behavior, in smokers, and in patients suffering from allergies. In conclusion, our data indicate that circulating oxidative stress biomarkers may be attractive candidates as disease predictors as well as for clinical or therapeutic monitoring of CD. Our results also suggest that AOPP/AGEs and RAGE signaling may represent a pathogenic factor and a potential therapeutic target in CD.
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6

Bayarsaikhan, Govigerel, Delger Bayarsaikhan, Jaewon Lee, and Bonghee Lee. "Targeting Scavenger Receptors in Inflammatory Disorders and Oxidative Stress." Antioxidants 11, no. 5 (May 9, 2022): 936. http://dx.doi.org/10.3390/antiox11050936.

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Oxidative stress and inflammation cannot be considered as diseases themselves; however, they are major risk factors for the development and progression of the pathogenesis underlying many illnesses, such as cancer, neurological disorders (including Alzheimer’s disease and Parkinson’s disease), autoimmune and metabolic disorders, etc. According to the results obtained from extensive studies, oxidative stress–induced biomolecules, such as advanced oxidation protein products, advanced glycation end products, and advanced lipoxidation end products, are critical for an accelerated level of inflammation and oxidative stress–induced cellular damage, as reflected in their strong affinity to a wide range of scavenger receptors. Based on the limitations of antioxidative and anti-inflammatory molecules in practical applications, targeting such interactions between harmful molecules and their cellular receptors/signaling with advances in gene engineering technology, such as CRISPR or TALEN, may prove to be a safe and effective alternative. In this review, we summarize the findings of recent studies focused on the deletion of scavenger receptors under oxidative stress as a development in the therapeutic approaches against the diseases linked to inflammation and the contribution of advanced glycation end products (AGEs), advanced lipid peroxidation products (ALEs), and advanced oxidation protein products (AOPPs).
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7

Ping, Mao, Wei Xiao, Liqian Mo, Xiaoyan Xiao, Shaolian Song, Waijiao Tang, and Xixiao Yang. "Paeonol Attenuates Advanced Oxidation Protein Product-Induced Oxidative Stress Injury in THP-1 Macrophages." Pharmacology 93, no. 5-6 (2014): 286–95. http://dx.doi.org/10.1159/000363577.

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8

Chooklin, Serge. "Advanced oxidation protein products in acute pancreatitis." Pancreatology 13, no. 3 (May 2013): S33. http://dx.doi.org/10.1016/j.pan.2013.04.106.

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9

Pandolfo, Gianluca, Giovanni Genovese, Antonio Bruno, Domenica Campolo, Valeria Tigano, Mariateresa Cristani, Marco Casciaro, Giovanni Pioggia, and Sebastiano Gangemi. "Advanced glycation end-products and advanced oxidation protein products in schizophrenia." Psychiatry Research 311 (May 2022): 114527. http://dx.doi.org/10.1016/j.psychres.2022.114527.

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10

Heymann-Szlachcinska, A., A. Wykretowicz, and J. Rybakowski. "Antidepressant treatment and advanced oxidation protein products in depressed patients." European Psychiatry 26, S2 (March 2011): 635. http://dx.doi.org/10.1016/s0924-9338(11)72341-0.

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IntroductionOxidative stress plays a role in producing advanced oxidation protein products (AOPP). High level of AOPP was observed in patients with such pathological conditions as ischemic heart disease, diabetes, cancer or neurodegenerative diseases.ObjectivesA role of oxidative stress in depression and in antidepressant treatment has been implicated. There have been no studies so far on AOPP in psychiatric diseases.Aim: An assessment of AOPP concentration, as a marker of oxidative stress, in patients with depression and the effect of antidepressant treatment.MethodsThirty-one patients hospitalized at Department of Adult Psychiatry, Poznan University of Medical Sciences, were studied. The first depressive episode was diagnosed in 5 patients, recurrent depressive disorder in 6 patients, and depression in the course of bipolar affective disorder in 20 patients. Patients were treated with venlafaxine (10), paroxetine (7), fluoxetine (5), clomipramine (4), citalopram (3), sertraline (1) and mianserine (1). Advanced oxidation protein products (AOPP) levels were measured twice: before treatment and in remission on maintenance doses of drugs. Control group consisted of 18 healthy volunteers, age- and gender matched.ResultsThere was no significant difference between depressed patients and healthy controls in the AOPP concentration before treatment. There was no correlation between AOPP levels and diagnosis, duration of illness, duration of the current episode and the age of illness’ onset. After antidepressant treatment, a significant decrease of AOPP concentration was found.ConclusionsThe results of the study may confirm previous data suggesting a decrease of some markers of oxidative stress after antidepressant treatment.
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11

Mukthapura, Anita, Avinash Shimogga, Vinodchandran K, Beena Shetty, and Gayathri Rao. "Oxidative Products of Proteins and Antioxidant Potential of Thiols in Gastric Carcinoma Patients." Journal of Medical Biochemistry 29, no. 2 (April 1, 2010): 102–6. http://dx.doi.org/10.2478/v10011-010-0013-z.

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Oxidative Products of Proteins and Antioxidant Potential of Thiols in Gastric Carcinoma PatientsIt has been suggested that oxidative stress defined as a shift in antioxidant/oxidant balance towards oxidants is associated with the pathogenesis of many diseases, including carcinogenesis. Reactive oxygen species can induce carcinogenesis via injury to macromolecules such as DNA, carbohydrates and proteins. Forty primary gastric carcinoma patients and 40 healthy controls were included in the study. Advanced oxidation protein products, total thiols, total protein, albumin in plasma, % hemolysis in RBC suspension and glutathione in both whole blood and plasma were estimated. Our studies demonstrated a significant increase in advanced oxidation protein products, % hemolysis (p=0.033), A:G ratio (p=0.003) and a highly significant decrease in blood glutathione (p=0.036), total thiols (p=0.001), plasma thiols other than glutathione and total antioxidant activity. The findings suggest that gastric carcinoma is associated with oxygen derived free radicals accumulation, and depletion of total antioxidant activity has lead to oxidative stress and advancement of oxidative-antioxidative disorders followed by progression of gastric cancer.
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12

Valle, Emanuela, Liviana Prola, Diana Vergnano, Roberta Borghi, Fiammetta Monacelli, Nicola Traverso, Natascia Bruni, et al. "Investigation of hallmarks of carbonyl stress and formation of end products in feline chronic kidney disease as markers of uraemic toxins." Journal of Feline Medicine and Surgery 21, no. 6 (July 17, 2018): 465–74. http://dx.doi.org/10.1177/1098612x18783858.

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Objectives Cats are commonly affected by chronic kidney disease (CKD). Many reactive carbonyl intermediates and end products originating from the oxidative stress pathways are recognised as uraemic toxins and may play a role in CKD progression. The aim of the present study is to confirm whether carbonyl end-product formation is higher in cats affected by CKD and to assess whether an angiotensin-converting enzyme inhibitor (ACEi) might affect these hallmarks. Methods Twenty-two cats were divided into three groups: a control group (CG), cats with CKD and cats with CKD treated with an ACEi. Serum levels of pentosidine, carboxymethyllysine, advanced oxidation protein products, malondialdehyde, methylglyoxal and hexanoyl-lysine were measured. In addition, biochemical parameters and systolic blood pressure were evaluated. After checking for normality, comparisons between groups were performed followed by multiple comparison tests. P values ⩽0.05 were considered significant. Correlations between concentrations of the considered biomarkers and of the other metabolic parameters were investigated. Results Advanced oxidation protein products, malondialdehyde and hexanoyl-lysine concentrations were significantly higher in CKD and ACEi-treated groups compared with the CG ( P <0.05). Carboxymethyllysine increased in the ACEi-treated group when compared with the CG, whereas intermediate values of these biomarkers were found in the CKD group ( P <0.05). The ACEi-treated group showed the highest values of carboxymethyllysine, advanced oxidation protein products and hexanoyl-lysine. By contrast, the CKD group had the highest concentration of malondialdehyde. No statistically significant difference was found in the levels of pentosidine or methylglyoxal. End products correlated with creatinine and urea and with each other. Conclusions and relevance Significantly high concentrations of both intermediate and end products of carbonyl/oxidative stress were detected in CKD cats. This is the first study to have concurrently taken into account several uraemic toxins and biochemical parameters in cats affected by CKD.
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13

Kalousová, M., T. Zima, V. Tesař, and J. Lachmanová. "Advanced Glycation End Products and Advanced Oxidation Protein Products in Hemodialyzed Patients." Blood Purification 20, no. 6 (2002): 531–36. http://dx.doi.org/10.1159/000066956.

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14

Pandey, Kanti Bhooshan, Mohd Murtaza Mehdi, Pawan Kumar Maurya, and Syed Ibrahim Rizvi. "Plasma Protein Oxidation and Its Correlation with Antioxidant Potential During Human Aging." Disease Markers 29, no. 1 (2010): 31–36. http://dx.doi.org/10.1155/2010/964630.

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Previous studies have indicated that the main molecular characteristic of aging is the progressive accumulation of oxidative damages in cellular macromolecules. Proteins are one of the main molecular targets of age-related oxidative stress, which have been observed during aging process in cellular systems. Reactive oxygen species (ROS) can lead to oxidation of amino acid side chains, formation of protein-protein cross-linkages, and oxidation of the peptide backbones. In the present study, we report the age-dependent oxidative alterations in biomarkers of plasma protein oxidation: protein carbonyls (PCO), advanced oxidation protein products (AOPPs) and plasma total thiol groups (T-SH) in the Indian population and also correlate these parameters with total plasma antioxidant potential. We show an age dependent decrease in T-SH levels and increase in PCO and AOPPs level. The alterations in the levels of these parameters correlated significantly with the total antioxidant capacity of the plasma. The levels of oxidized proteins in plasma provide an excellent biomarker of oxidative stress due to the relative long half-life of such oxidized proteins.
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15

Demirbilek, Melike Erol, Nedret Kilic, H. Ferhan Komurcu, and K. Okhan Akin. "Advanced Oxidation Protein Products in Aged with Dementia." American Journal of Immunology 3, no. 2 (February 1, 2007): 52–55. http://dx.doi.org/10.3844/ajisp.2007.52.55.

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16

Witko-Sarsat, Véronique, Valérie Gausson, and Béatrice Descamps-Latscha. "Are advanced oxidation protein products potential uremic toxins?" Kidney International 63 (May 2003): S11—S14. http://dx.doi.org/10.1046/j.1523-1755.63.s84.47.x.

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17

Xiang, Qian, Zhangrong Cheng, Juntan Wang, Xiaobo Feng, Wenbin Hua, Rongjin Luo, Bingjin Wang, et al. "Allicin Attenuated Advanced Oxidation Protein Product-Induced Oxidative Stress and Mitochondrial Apoptosis in Human Nucleus Pulposus Cells." Oxidative Medicine and Cellular Longevity 2020 (December 16, 2020): 1–17. http://dx.doi.org/10.1155/2020/6685043.

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Intervertebral disc degeneration (IDD) is one of the most common chronic degenerative musculoskeletal disorders. Oxidative stress-induced apoptosis of the nucleus pulposus (NP) cells plays a key role during IDD progression. Advanced oxidation protein products (AOPP), novel biomarkers of oxidative stress, have been reported to function in various diseases due to their potential for disrupting the redox balance. The current study is aimed at investigating the function of AOPP in the oxidative stress-induced apoptosis of human NP cells and the alleviative effects of allicin during this process which was known for its antioxidant properties. AOPP were demonstrated to hamper the viability and proliferation of NP cells in a time- and concentration-dependent manner and cause cell apoptosis markedly. High levels of reactive oxygen species (ROS) and lipid peroxidation product malondialdehyde (MDA) were detected in NP cells after AOPP stimulation, which resulted in depolarized mitochondrial transmembrane potential (MTP). Correspondingly, higher levels of AOPP were discovered in the human degenerative intervertebral discs (IVD). It was also found that allicin could protect NP cells against AOPP-mediated oxidative stress and mitochondrial dysfunction via suppressing the p38-MAPK pathway. These results disclosed a significant role of AOPP in the oxidative stress-induced apoptosis of NP cells, which could be involved in the primary pathogenesis of IDD. It was also revealed that allicin could be a promising therapeutic approach against AOPP-mediated oxidative stress during IDD progression.
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18

Sindhu, Prathima, Beena Shetty, K. Sudha, and Gayathri Rao. "Role of Redox Metals, Oxidative Protein Products and Antioxidant Potentials of Thiols in Diabetic Retinopathy." Journal of Medical Biochemistry 31, no. 2 (April 1, 2012): 126–30. http://dx.doi.org/10.2478/v10011-011-0045-z.

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Role of Redox Metals, Oxidative Protein Products and Antioxidant Potentials of Thiols in Diabetic RetinopathyOxidative stress has been proved in the pathogenesis of diabetes mellitus (DM) and diabetic retinopathy (DR) not only by the reactive oxygen species (ROS) but also due to non-enzymatic protein glycosylation, auto-oxidation of glucose, impaired glutathione metabolism, alteration in the antioxidants and advanced oxidative protein product formation. The current study was undertaken to establish the relationship between iron, copper and antioxidants like reduced glutathione (GSH), total thiols, and advanced oxidation protein products (AOPP) as well as total protein and albumin. The study group consisted of a total of 90 subjects which included non-diabetic healthy controls (n=30), diabetes mellitus patients (n=30), and diabetic retinopathy patients (n=30). All the parameters were measured using spectrophotometric methods. AOPP levels showed a very highly significant increase in DR patients and in DM patients compared to normal controls, the AOPP levels being higher in the DR compared to the DM patients (p= 0.001). The levels of thiols showed a very highly significant decrease in DR and DM as compared to normal subjects. The total proteins level showed a very highly significant decrease (P = 0.001) in DR and DM compared to normal. There was no change in the level of albumin. A significant increase in the levels of iron was observed in DR when compared to DM and control. The levels of copper in DR showed a very highly significant increase when compared to DM and controls (p = 0.001). Our study indicates a possible increase in the copper and iron-mediated generation of ROS thereby leading to increased consumption of antioxidants in the body.
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Balıkcı, Hasan Huseyin, Mustafa Karakaş, Muhammet Mustafa Gürdal, Murat Haluk Özkul, Özlem Bayram, Ali Alper Bayram, and Servet Yigit. "Advanced oxidation protein product level in children with chronic otitis media with effusion." International Journal of Pediatric Otorhinolaryngology 78, no. 3 (March 2014): 552–54. http://dx.doi.org/10.1016/j.ijporl.2014.01.007.

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20

Takagi, Yoshifumi, Atsunori Kashiwagi, Yasushi Tanaka, Takayuki Asahina, Ryuichi Kikkawa, and Yukio Shigeta. "Significance of fructose-induced protein oxidation and formation of advanced glycation end product." Journal of Diabetes and its Complications 9, no. 2 (April 1995): 87–91. http://dx.doi.org/10.1016/1056-8727(94)00022-g.

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21

Ansari, Nadeem A., Moinuddin, and Rashid Ali. "Glycated Lysine Residues: A Marker for Non-Enzymatic Protein Glycation in Age-Related Diseases." Disease Markers 30, no. 6 (2011): 317–24. http://dx.doi.org/10.1155/2011/718694.

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Nonenzymatic glycosylation or glycation of macromolecules, especially proteins leading to their oxidation, play an important role in diseases. Glycation of proteins primarily results in the formation of an early stage and stable Amadori-lysine product which undergo further irreversible chemical reactions to form advanced glycation endproducts (AGEs). This review focuses these products in lysine rich proteins such as collagen and human serum albumin for their role in aging and age-related diseases. Antigenic characteristics of glycated lysine residues in proteins together with the presence of serum autoantibodies to the glycated lysine products and lysine-rich proteins in diabetes and arthritis patients indicates that these modified lysine residues may be a novel biomarker for protein glycation in aging and age-related diseases.
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Liu, Shang Xi, Fan Fan Hou, Zhi Jian Guo, Ryoji Nagai, Wei Ru Zhang, Zhi Qiang Liu, Zhan Mei Zhou, et al. "Advanced Oxidation Protein Products Accelerate Atherosclerosis Through Promoting Oxidative Stress and Inflammation." Arteriosclerosis, Thrombosis, and Vascular Biology 26, no. 5 (May 2006): 1156–62. http://dx.doi.org/10.1161/01.atv.0000214960.85469.68.

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23

van Ypersele de Strihou, Charles, and Toshio Miyata. "Advanced Glycation and Advanced Oxidation Protein Products: The Effect of Peritoneal Dialysis." Peritoneal Dialysis International: Journal of the International Society for Peritoneal Dialysis 26, no. 2 (March 2006): 185–87. http://dx.doi.org/10.1177/089686080602600211.

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Krzystek-Korpacka, Malgorzata, Katarzyna Neubauer, Izabela Berdowska, Dorota Boehm, Bogdan Zielinski, Pawel Petryszyn, Grzegorz Terlecki, Leszek Paradowski, and Andrzej Gamian. "Enhanced formation of advanced oxidation protein products in IBD." Inflammatory Bowel Diseases 14, no. 6 (June 2008): 794–802. http://dx.doi.org/10.1002/ibd.20383.

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Semenova, Natalya V., Irina Madaeva, Anastasia Brichagina, Olga Nikitina, Sergey I. Kolesnikov, and Lyubov Kolesnikova. "Advanced Oxidation Protein Products in Menopausal Women with Insomnia." Free Radical Biology and Medicine 159 (November 2020): S110. http://dx.doi.org/10.1016/j.freeradbiomed.2020.10.279.

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Hanasand, Marita, Roald Omdal, Katrine B. Norheim, Lasse G. Gøransson, Cato Brede, and Grete Jonsson. "Improved detection of advanced oxidation protein products in plasma." Clinica Chimica Acta 413, no. 9-10 (May 2012): 901–6. http://dx.doi.org/10.1016/j.cca.2012.01.038.

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WOODS, Alan A., Stuart M. LINTON, and Michael J. DAVIES. "Detection of HOCl-mediated protein oxidation products in the extracellular matrix of human atherosclerotic plaques." Biochemical Journal 370, no. 2 (March 1, 2003): 729–35. http://dx.doi.org/10.1042/bj20021710.

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Oxidation is believed to play a role in atherosclerosis. Oxidized lipids, sterols and proteins have been detected in early, intermediate and advanced human lesions at elevated levels. The spectrum of oxidized side-chain products detected on proteins from homogenates of advanced human lesions has been interpreted in terms of the occurrence of two oxidative mechanisms, one involving oxygen-derived radicals catalysed by trace transition metal ions, and a second involving chlorinating species (HOCl or Cl2), generated by the haem enzyme myeloperoxidase (MPO). As MPO is released extracellularly by activated monocytes (and possibly macrophages) and is a highly basic protein, it would be expected to associate with polyanions such as the glycosaminoglycans of the extracellular matrix, and might result in damage being localized at such sites. In this study proteins extracted from extracellular matrix material obtained from advanced human atherosclerotic lesions are shown to contain elevated levels of oxidized amino acids [3,4-dihydroxyphenylalanine (DOPA), di-tyrosine, 2-hydroxyphenylalanine (o-Tyr)] when compared with healthy (human and pig) arterial tissue. These matrix-derived materials account for 83—96% of the total oxidized protein side-chain products detected in these plaques. Oxidation of matrix components extracted from healthy artery tissue, and model proteins, with reagent HOCl is shown to give rise to a similar pattern of products to those detected in advanced human lesions. The detection of elevated levels of DOPA and o-Tyr, which have been previously attributed to the occurrence of oxygen-radical-mediated reactions, by HOCl treatment, suggests an alternative route to the formation of these materials in plaques. This is believed to involve the formation and subsequent decomposition of protein chloramines.
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Rabbani, Naila, Fozia Shaheen, Attia Anwar, Jinit Masania, and Paul J. Thornalley. "Assay of methylglyoxal-derived protein and nucleotide AGEs." Biochemical Society Transactions 42, no. 2 (March 20, 2014): 511–17. http://dx.doi.org/10.1042/bst20140019.

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Glyoxalase- and methylglyoxal-related research has required the development of quantitative and reliable techniques for the measurement of methylglyoxal-derived glycation adducts of protein and DNA. There are also other glycation adducts, oxidation adducts and nitration adducts of proteins and oxidation adducts of DNA. Proteolysis of protein releases glycation, oxidation and nitration free adducts (glycated, oxidized and nitrated amino acids) in plasma and nuclease digestion of DNA releases glycated and oxidized nucleosides into plasma and other body fluids for excretion in urine. The gold standard method for quantifying these adducts is stable isotopic dilution analysis LC–MS/MS. Protein and DNA adduct residues are determined by assay of enzymatic hydrolysates of protein and DNA extracts prepared using cocktails of proteases and nucleases respectively. Free adducts are determined by analysis of ultrafiltrates of plasma, urine and other physiological fluids. Protein damage markers (13 glycation adducts, five oxidation adducts and 3-nitrotyrosine) and DNA damage markers (three glycation adducts and one oxidation adduct) are quantified using 25 μg of protein, 10 μg of DNA or 5 μl of physiological fluid. Protein and nucleotide AGE (advanced glycation end-product) assay protocols resistant to interferences is described.
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29

FU, Shanlin, Michael J. DAVIES, Roland STOCKER, and Roger T. DEAN. "Evidence for roles of radicals in protein oxidation in advanced human atherosclerotic plaque." Biochemical Journal 333, no. 3 (August 1, 1998): 519–25. http://dx.doi.org/10.1042/bj3330519.

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Oxidative damage might be important in atherogenesis. Oxidized lipids are present at significant concentrations in advanced human plaque, although tissue antioxidants are mostly present at normal concentrations. Indirect evidence of protein modification (notably derivatization of lysine) or oxidation has been obtained by immunochemical methods; the specificities of these antibodies are unclear. Here we present chemical determinations of six protein-bound oxidation products: dopa, o-tyrosine, m-tyrosine, dityrosine, hydroxyleucine and hydroxyvaline, some of which reflect particularly oxy-radical-mediated reaction pathways, which seem to involve mainly the participation of transition- metal ions. We compared the relative abundance of these oxidation products in normal intima, and in human carotid plaque samples with that observed after radiolytically generated hydroxyl radical attack on BSA in vitro. The close similarities in relative abundances in the latter two circumstances indicate that hydroxyl radical damage might occur in plaque. The relatively higher level of dityrosine in plaque than that observed after radiolysis suggests the additional involvement of HOCl-mediated reactions in advanced plaque.
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Atukeren, Pinar, Seval Aydin, Ezel Uslu, MKoray Gumustas, and Ufuk Cakatay. "Redox Homeostasis of Albumin in Relation to Alpha-Lipoic Acid and Dihydrolipoic Acid." Oxidative Medicine and Cellular Longevity 3, no. 3 (2010): 206–13. http://dx.doi.org/10.4161/oxim.3.3.11786.

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Albumin represents the predominant circulating antioxidant agent in plasma exposed to continuous oxidative stress and a change in serum albumin structure accounts for its antioxidant properties. Alterations in the redox status of albumin may result in impairments of its biological properties. Alpha-lipoic acid (LA), a naturally occurring thiol compound found in virtually all species, is a potent antioxidant with high efficacy which is also involved in the chelation of metal ions, regeneration of antioxidants, and repair of oxidatively damaged proteins. In human body LA is rapidly reduced to dihydrolipoic acid (DHLA) after intake into the cell. Both, LA and DHLA are amphipathic molecules which act as antioxidants both in hydrophilic and lipophilic environments. The present study aimed to investigate the antioxidant/pro-oxidant effects of LA and DHLA due to their concentrations in metal-catalyzed protein oxidation (MCO) of human serum albumin (HSA). Progressive oxidative modification of albumin was found in MCO system by an increased content of protein hydroperoxides (POOH), protein carbonyl groups (PCO) which is the former's major breakdown product, and other protein oxidation markers such as advanced oxidized protein products (AOPP) and protein thiol groups (P-SH). The possible antioxidant protective effects of LA and DHLA were observed with 25 µM and 50 µM; DHLA being more influential. Protein oxidation parameters were found to be lower and P-SH levels seemed higher. However, prooxidant effects of both LA and DHLA came on the scene with increased concentrations of 75 µM and 100 µM where the latter seemed the most hazardous with contradicted results. It is clear that the loss of biological activity of human serum albumin by MCO system appears of medical relevance and if LA exerts similar effects seen in the present study, it is possible that cellular prooxidant activity can also result consuming this unique antioxidant in certain doses.
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Pawlukianiec, Cezary, Małgorzata Ewa Gryciuk, Kacper Maksymilian Mil, Małgorzata Żendzian-Piotrowska, Anna Zalewska, and Mateusz Maciejczyk. "A New Insight into Meloxicam: Assessment of Antioxidant and Anti-Glycating Activity in In Vitro Studies." Pharmaceuticals 13, no. 9 (September 10, 2020): 240. http://dx.doi.org/10.3390/ph13090240.

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Meloxicam is a non-steroidal anti-inflammatory drug, which has a preferential inhibitory effect to cyclooxyganase-2 (COX-2). Although the drug inhibits prostaglandin synthesis, the exact mechanism of meloxicam is still unknown. This is the first study to assess the effect of meloxicam on protein glyco-oxidation as well as antioxidant activity. For this purpose, we used an in vitro model of oxidized bovine serum albumin (BSA). Glucose, fructose, ribose, glyoxal and methylglyoxal were used as glycating agents, while chloramine T was used as an oxidant. We evaluated the antioxidant properties of albumin (2,2-di-phenyl-1-picrylhydrazyl radical scavenging capacity, total antioxidant capacity and ferric reducing antioxidant power), the intensity of protein glycation (Amadori products, advanced glycation end products) and glyco-oxidation (dityrosine, kynurenine, N-formylkynurenine, tryptophan and amyloid-β) as well as the content of protein oxidation products (advanced oxidation protein products, carbonyl groups and thiol groups). We have demonstrated that meloxicam enhances the antioxidant properties of albumin and prevents the protein oxidation and glycation under the influence of various factors such as sugars, aldehydes and oxidants. Importantly, the antioxidant and anti-glycating activity is similar to that of routinely used antioxidants such as captopril, Trolox, reduced glutathione and lipoic acid as well as protein glycation inhibitors (aminoguanidine). Pleiotropic action of meloxicam may increase the effectiveness of anti-inflammatory treatment in diseases with oxidative stress etiology.
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Cheserek, Maureen Jepkorir, Gui-Rong Wu, Arsene Ntazinda, Yong-Hui Shi, Li-Ye Shen, and Guo-Wei Le. "Association Between Thyroid Hormones, Lipids and Oxidative Stress Markers in Subclinical Hypothyroidism / Povezanost Izme\U Tireoidnih Hormona, Lipida I Markera Oksidativnog Stresa U SubkliniĉKoj Hipotireozi." Journal of Medical Biochemistry 34, no. 3 (July 1, 2015): 323–31. http://dx.doi.org/10.2478/jomb-2014-0044.

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SummaryOxidative stress plays a role in the pathogenesis of many chronic diseases. It is recognized in overt hypothyroidism while its existence in subclinical hypothyroidism (SCH) is not well established. The aim of this study was to determine whether there was increased oxidation of lipids and proteins in SCH, and examine their association with lipids and thyroid hormones.Methods: Male adults (35-59 years) with SCH (n=467) and euthyroid controls (n=190) were studied. Anthropometric measurements, plasma lipids, thyroid stimulating hormone (TSH), free thyroxine (FT4), free triiodothyronine (FT3), total antioxidant capacity (T-AOC), lipid peroxidation products, malondialdehyde (MDA), advanced oxidation protein products (AOPP) and dityrosine concentrations were measured.Results: Plasma concentrations of MDA were significantly higher (p<0.05) in SCH (8.11±1.39 nmol/mL) compared with euthyroid controls (7.34±1.31 nmol/mL) while AOPP, dityrosine and T-AOC levels were not different. MDA was not associated with TSH (β=-0.019, P=0.759), FT4 (β=-0.062, P=0.323) and FT3 (β=-0.018, P=0.780) in SCH while levels increased with elevated total cholesterol (β=0.229, P=0.001), LDL (β=0.203, P=0.009) and triglycerides (β=0.159, P=0.036) after adjustment for ageand body mass index. T-AOC reduced (β=-0.327, P=0.030) with increased MDA in euthyroid controls and not in SCH (β=-0.068, P=0.349), while levels increased with elevated triglycerides in both groups.Conclusion: Oxidative stress was increased in subclinical hypothyroidism as evidenced by the elevated lipid peroxidation product, malondialdehyde, while protein oxidation was absent. Thus, reduction of oxidative stress may be beneficial in patients with subclinical hypothyroidism
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Karamalakova, Yanka, Ivaylo Stefanov, Ekaterina Georgieva, and Galina Nikolova. "Pulmonary Protein Oxidation and Oxidative Stress Modulation by Lemna minor L. in Progressive Bleomycin-Induced Idiopathic Pulmonary Fibrosis." Antioxidants 11, no. 3 (March 8, 2022): 523. http://dx.doi.org/10.3390/antiox11030523.

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Bleomycin (BLM) administration is associated with multifunctional proteins inflammations and induction of idiopathic pulmonary fibrosis (IPF). Lemna minor L. extract, a free-floating monocot macrophyte possesses antioxidant and anti-inflammatory potential. The aim of the study was to examine the protective effect of L. minor extract on lung protein oxidation and oxidative stress modulation by BLM-induced pulmonary fibrosis in Balb/c mice. For this purpose, the protein carbonyl content, advanced glycation end product, nitroxide protein oxidation (5-MSL), and lipid peroxidation (as MDA and ROS), in lung cells were examined. The histological examinations, collagen deposition, and quantitative measurements of IL-1β, IL-6, and TNF in lung tissues and blood were investigated. Intraperitoneal, BLM administration (0.069 U/mL; 0.29 U/kg b.w.) for 33 days, caused IPF induction in Balb/c mice. Pulmonary combining therapy was administered with L. minor at dose 120 mg/mL (0.187 mg/kg b.w.). L. minor histologically ameliorated BLM induced IPF in lung tissues. L. minor significantly modulated (p < 0.05) BLM-alterations induced in lung hydroxyproline, carbonylated proteins, 5-MSL-protein oxidation. Oxidative stress decreased levels in antioxidant enzymatic and non-enzymatic systems in the lung were significantly regulated (p < 0.05) by L. minor. L. minor decreased the IL-1β, IL-6, and TNF-α expression in lung tissues and plasma. The L. minor improves the preventive effect/defense response in specific pulmonary protein oxidation, lipid peroxidation, ROS identifications, and cytokine modulation by BLM-induced chronic inflammations, and could be a good antioxidant, anti-inflammatory, and anti-fibrotic alternative or IPF prevention involved in their pathogenesis.
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Witko-Sarsat, Véronique, Miriam Friedlander, Chantal Capeillère-Blandin, Thao Nguyen-Khoa, Anh Thu Nguyen, Johanna Zingraff, Paul Jungers, and Béatrice Descamps-Latscha. "Advanced oxidation protein products as a novel marker of oxidative stress in uremia." Kidney International 49, no. 5 (May 1996): 1304–13. http://dx.doi.org/10.1038/ki.1996.186.

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Liu, Youhua. "Advanced oxidation protein products: a causative link between oxidative stress and podocyte depletion." Kidney International 76, no. 11 (December 2009): 1125–27. http://dx.doi.org/10.1038/ki.2009.352.

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Demidchik, Lyudmila Andreevna, Valentina Vitalyevna Lee, Larissa Yevgenyevna Muravlyova, Vilen Borisovich Molotov-Luchanskiy, Ryszhan Yemelyevna Bakirova, Dmitriy Anatolyevich Klyuyev, and Yevgeniya Alexandrovna Kolesnikova. "Oxidative metabolism of neutrophils in patients with community-acquired pneumonia." Current Issues in Pharmacy and Medical Sciences 29, no. 1 (April 1, 2016): 5–7. http://dx.doi.org/10.1515/cipms-2016-0001.

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Abstract At the present time, available views show our limited knowledge of the peculiarities of the functional status of neutrophils and their metabolism in patients with community-acquired pneumonia (CAP). The studying of changes of metabolic status of neutrophils can broaden our views about pneumonia pathogenesis and define datum points of therapeutic effect. Purpose of our research: to define oxidative stress activity and the level of oxidative modification of proteins of neutrophils in CAP patients. Materials and methods: neutrophils obtained from 23 patients with community-acquired pneumonia. Control group consisting of 19 healthy volunteers. The reactive carbonyl derivatives of proteins and advanced oxidation protein products were defined so as to assess the oxidative damage of proteins. The malondialdehyde and nitrite ions were assessed as being indicators of the oxidative stress. The neutrophils of CAP patients with moderate severity were characterized by a tendency of evidencing decreasing content of advanced oxidation protein products, along with the statistically important enhanced levels of carbonyl derivatives and nitrite ions, while their malondialdehyde status practically leveled off with the control and had only an insignificant trend towards growth. We have demonstrated the accumulation of carbonyl derivatives and nitrite ions in the peripheral neutrophils of CAP patients. These results give evidence of an oxidative misbalance in the cells which contributes to the aggravation of the disease.
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Zhao, Yalei, Lingjian Zhang, Xiaoxi Ouyang, Zhengyi Jiang, Zhongyang Xie, Linxiao Fan, Danhua Zhu, and Lanjuan Li. "Advanced oxidation protein products play critical roles in liver diseases." European Journal of Clinical Investigation 49, no. 6 (March 20, 2019): e13098. http://dx.doi.org/10.1111/eci.13098.

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Zeng, Ji-Huan, Zhao-Ming Zhong, Xiao-Dan Li, Qian Wu, Shuai Zheng, Jian Zhou, Wen-Bin Ye, et al. "Advanced oxidation protein products accelerate bone deterioration in aged rats." Experimental Gerontology 50 (February 2014): 64–71. http://dx.doi.org/10.1016/j.exger.2013.11.014.

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39

Mishra, Jigeesha, Kanti Bhooshan Pandey, and Shailendra Kumar Srivastava. "Assessment of Protein Oxidation Status and Its Correlation with Antioxidant Potential in Preeclampsia." Asian Pacific Journal of Health Sciences 9, no. 2 (April 1, 2022): 226–29. http://dx.doi.org/10.21276/apjhs.2022.9.2.45.

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Objective: The objective of the study is to assess protein oxidation status and its correlation with antioxidant potential in serum during preeclampsia (PE). Materials and Methods: A casecontrol study was performed on 63 pregnant subjects (mean age = 30 tential in serpreeclamptic and 32 age-matched normotensive (control) pregnant women. Serum samples were analyzed for total protein, globulin, albumin, protein carbonyls (PCO), advanced oxidation protein products (AOPP), and ferric reducing antioxidant potential. Results: Compared to the control pregnant subjects, a compromised serum protein pattern, elevated PCO (P < 0.01), and AOPP (P < 0.02) were observed in PE pregnant women that were correlated significantly with the total antioxidant potential of serum. Conclusion: The results of the study suggest that PE pregnancies are susceptible to protein oxidation which may be due to diminished antioxidant potential during PE. The study concludes that oxidative modulation of proteins may be one of the major causative factors in complicating the maternal and fetal conditions during PE.
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SUZUKI, DAISUKE, TOSHIO MIYATA, NOBORU SAOTOME, KATSUNORI HORIE, REIKO INAGI, YOSHINARI YASUDA, KOJI UCHIDA, 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 (April 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 stress, was not found within diabetic glomeruli. Because CML, pentosidine, and MDA-lysine are all formed under oxidative stress by carbonyl amine chemistry between protein amino group and carbonyl compounds, their colocalization suggests a local oxidative stress and increased protein carbonyl modification in diabetic glomerular lesions. To address this hypothesis, human renal tissues from patients with DN or IgA nephropathy were examined with specific antibodies to characterize most, if not all, carbonyl modifications of proteins by autoxidation products of carbohydrates, lipids, and amino acids: CML (derived from carbohydrates, lipids, and amino acid), pentosidine (derived from carbohydrates), MDA-lysine (derived from lipids), 4-hydroxynonenal-protein adduct (derived from lipids), and acrolein-protein adduct (derived from lipids and amino acid). All of the protein adducts were identified in expanded mesangial matrix and nodular lesions in DN. In IgA nephropathy, another primary glomerular disease leading to end-stage renal failure, despite positive staining for MDA-lysine and 4-hydroxynonenal-protein adduct in the expanded mesangial area, CML, pentosidine, and acrolein-protein adduct immunoreactivities were only faint in glomeruli. These data suggest a broad derangement in nonenzymatic biochemistry in diabetic glomerular lesions, and implicate an increased local oxidative stress and carbonyl modification of proteins in diabetic glomerular tissue damage (“carbonyl stress”).
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Choromańska, Barbara, Piotr Myśliwiec, Tomasz Kozłowski, Magdalena Łuba, Piotr Wojskowicz, Jacek Dadan, Hanna Myśliwiec, et al. "Antioxidant Barrier and Oxidative Damage to Proteins, Lipids, and DNA/RNA in Adrenal Tumor Patients." Oxidative Medicine and Cellular Longevity 2021 (June 22, 2021): 1–19. http://dx.doi.org/10.1155/2021/5543531.

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This study is the first to assess redox balance, glutathione metabolism, and oxidative damage to RNA/DNA, proteins, and lipids in the plasma/serum and urine of patients with adrenal masses. The study included 70 patients with adrenal tumors divided into three subgroups: incidentaloma ( n = 30 ), pheochromocytoma ( n = 20 ), and Cushing’s/Conn’s adenoma ( n = 20 ), as well as 60 healthy controls. Blood and urine samples were collected before elective endoscopic adrenalectomy. Antioxidant defense capacity was significantly decreased (serum/plasma: superoxide dismutase (SOD), catalase (CAT) and reduced glutathione (GSH), uric acid (UA); urine: SOD, GSH, UA) in patients with adrenal masses. The oxidative damage to proteins (advanced glycation end products (AGE), advanced oxidation protein products (AOPP)) and lipids (lipid hydroperoxides (LOOH), and malondialdehyde (MDA)) was higher in the plasma and urine of these patients. Plasma MDA and DNA/RNA oxidation products, with high sensitivity and specificity, can help to diagnose pheochromocytoma. This biomarker differentiates patients with pheochromocytoma from Cushing’s/Conn’s adenoma as well as from heathy controls. Plasma RNA/DNA oxidation was also positively correlated with urine metanephrine. Oxidative stress can play a crucial role in adrenal tumors. However, further studies are required to clarify the role of redox signaling in adrenal masses.
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Yevgenyevna Muravlyova, Larissa, Vilen Borisovich Molotov-Luchankiy, Ryszhan Yemelyevna Bakirova, Anar Akylbekovna Turmukhambetova, Dmitriy Anatolyevich Klyuyev, Ludmila Andreevna Demidchik, and Yevgeniya Alexandrovna Kolesnikova. "The alteration in peripheral neutrophils of patients with chronic kidney disease." Current Issues in Pharmacy and Medical Sciences 28, no. 1 (March 1, 2015): 17–20. http://dx.doi.org/10.1515/cipms-2015-0034.

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Abstract Recent findings have demonstrated the impaired functions of neutrophils of patients with chronic renal failure. The purpose of our research was to study oxidative modified proteins, as well as the histone spectrum in neutrophils drawn from patients with chronic kidney disease, and to estimate the ability of neutrophils to form spontaneous neutrophil extracellular traps. In this work, we have assumed that metabolic alteration in neutrophils may develop at early stages of chronic kidney disease. Materials and methods: Neutrophils obtained from patients with various stages of chronic kidney disease and degrees of chronic renal failure were used. As control, blood samples obtained from 32 healthy individuals was employed. In the examined neutrophils, advanced oxidation protein products, protein reactive carbonyl derivatives, as well as nucleosomal histones were detected. The ability of neutrophils to form spontaneous neutrophil extracellular traps was estimated. Our results have demonstrated an increase of nucleosomal histones in neutrophils of all patients with chronic kidney disease. Moreover, our work fixes the rate of growth of intracellular advanced oxidation protein products and the decreasing of protein reactive carbonyl derivatives in neutrophils from patients with chronic kidney disease. Furthermore, we demonstrate the presence of the neutrophils with altered oxidative status and the decomposition of the histone spectrum in the circulation of patients with chronic kidney disease.
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Gryszczyńska, Bogna, Dorota Formanowicz, Magdalena Budzyń, Maria Wanic-Kossowska, Elżbieta Pawliczak, Piotr Formanowicz, Wacław Majewski, Krzysztof Wojciech Strzyżewski, Magdalena P. Kasprzak, and Maria Iskra. "Advanced Oxidation Protein Products and Carbonylated Proteins as Biomarkers of Oxidative Stress in Selected Atherosclerosis-Mediated Diseases." BioMed Research International 2017 (2017): 1–9. http://dx.doi.org/10.1155/2017/4975264.

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Objectives. The main question of this study was to evaluate the intensity of oxidative protein modification shown as advanced oxidation protein products (AOPP) and carbonylated proteins, expressed as protein carbonyl content (C=O) in abdominal aortic aneurysms (AAA), aortoiliac occlusive disease (AIOD), and chronic kidney disease (CKD). Design and Methods. The study was carried out in a group of 35 AAA patients and 13 AIOD patients. However, CKD patients were divided into two groups: predialysis (PRE) included 50 patients or hemodialysis (HD) consisted of 34 patients. AOPP and C=O were measured using colorimetric assay kit, while C-reactive protein concentration was measured by high-sensitivity assay (hsCRP). Results. The concentration of AOPP in both AAA and AIOD groups was higher than in PRE and HD groups according to descending order: AAA~AIOD > HD > PRE. The content of C=O was higher in the PRE group in comparison to AIOD and AAA according to the descending order: PRE~HD > AAA~AIOD. Conclusions. AAA, AIOD, and CKD-related atherosclerosis (PRE and HD) contribute to the changes in the formation of AOPP and C=O. They may promote modification of proteins in a different way, probably due to the various factors that influence oxidative stress here.
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Pérez-Ruiz, Irantzu, Susana Meijide, María-Luisa Hérnandez, Rosaura Navarro, Zaloa Larreategui, Marcos Ferrando, María-Begoña Ruiz-Larrea, and José-Ignacio Ruiz-Sanz. "Analysis of Protein Oxidative Modifications in Follicular Fluid from Fertile Women: Natural Versus Stimulated Cycles." Antioxidants 7, no. 12 (November 27, 2018): 176. http://dx.doi.org/10.3390/antiox7120176.

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Oxidative stress is associated with obstetric complications during ovarian hyperstimulation in women undergoing in vitro fertilization. The follicular fluid contains high levels of proteins, which are the main targets of free radicals. The aim of this work was to determine specific biomarkers of non-enzymatic oxidative modifications of proteins from follicular fluid in vivo, and the effect of ovarian stimulation with gonadotropins on these biomarkers. For this purpose, 27 fertile women underwent both a natural and a stimulated cycle. The biomarkers, glutamic semialdehyde (GSA), aminoadipic semialdehyde (AASA), Nε-(carboxymethyl)lysine (CML), and Nε-(carboxyethyl)lysine (CEL), were measured by gas-liquid chromatography coupled to mass spectrometry. Results showed that follicular fluid contained products of protein modifications by direct metal-catalyzed oxidation (GSA and AASA), glycoxidation (CML and CEL), and lipoxidation (CML). GSA was the most abundant biomarker (91.5%). The levels of CML amounted to 6% of the total lesions and were higher than AASA (1.3%) and CEL (1.2%). In the natural cycle, CEL was significantly lower (p < 0.05) than in the stimulated cycle, suggesting that natural cycles are more protected against protein glycoxidation. These findings are the basis for further research to elucidate the possible relevance of this follicular biomarker of advanced glycation end product in fertility programs.
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KIMOTO, Yumi, Akihiko SUGIYAMA, Masaaki NISHINOHARA, Atsushi ASANO, Aino MASUDA, Tairin OCHI, and Takashi TAKEUCHI. "Expressions of Protein Oxidation Markers, Dityrosine and Advanced Oxidation Protein Products in Cisplatin-Induced Nephrotoxicity in Rats." Journal of Veterinary Medical Science 73, no. 3 (2011): 403–7. http://dx.doi.org/10.1292/jvms.10-0371.

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Altunoglu, Esma, Gulcan Guntas, Fusun Erdenen, Esen Akkaya, Ibrahim Topac, Hulya Irmak, Himmet Derici, Hakan Yavuzer, Remise Gelisgen, and Hafize Uzun. "Ischemia-modified albumin and advanced oxidation protein products as potential biomarkers of protein oxidation in Alzheimer's disease." Geriatrics & Gerontology International 15, no. 7 (October 27, 2014): 872–80. http://dx.doi.org/10.1111/ggi.12361.

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Cekic, Sonja, Tatjana Cvetkovic, Ivan Jovanovic, Predrag Jovanovic, Gordana Stankovic-Babic, Milica Pesic, and Milena Vujanovic. "Association of advanced oxidation protein product, thiobarbituric acid reactive substances and total sulfhydryl groups with retinal blood vessels caliber." Srpski arhiv za celokupno lekarstvo 147, no. 11-12 (2019): 706–12. http://dx.doi.org/10.2298/sarh180227046c.

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Introduction/Objective. Intensive oxidative stress is proven in patients with diabetes mellitus and important in the development of a microvascular complication of type 2 diabetes mellitus. The aim of the study was to investigate the relationship between morphometric parameters of retinal blood vessels in patients with diabetic retinopathy (DR) and the levels of parameters of oxidative stress: advanced oxidation protein product (AOPP), thiobarbituric acid reactive substances (TBARS), and total sulfhydryl (SH) groups in blood samples. Methods. The patients (the group with DR and controls) were sex- and age-matched. Glycaemia, hemoglobin A1C HbA1C, total cholesterol and its fractions, and triglycerides were measured in blood samples. AOPP and total SH groups were determined in the plasma by specific methods. Modification of the thiobarbituric acid method was used for the determination of TBARS. The number and diameter of retinal blood vessels, as morphometric parameters on digital retinal photography, was determined by using the ImageJ software. Student?s t-test was used as the statistical method for the evaluation of differences between the morphometric and blood test parameters. The significance of differences in morphometric parameters of retinal blood was establish by one-way ANOVA. Results. Significantly higher levels of parameters of oxidative stress (AOPP and TBARS) were in the group of patients with DR than in the controls. This difference was also present among the patients with mild and severe forms of DR (AOPP F 77.03, p < 0.001) (TBARS F 63.28, p < 0.001). The diameter of retinal blood vessels correlated with levels of AOPP, but only in patients with mild DR. Conclusion. Parameters of oxidative stress, AOPP and TBARS, may be important for the follow-up of DR. In early stages in diabetic retinopathy, AOPP can be a valuable biomarker.
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Kerem, M., A. Bedirli, H. Pasaoglu, O. Pasaoglu, and K. Dikmen. "LB027 SERUM ADVANCED OXIDATIVE PROTEIN PRODUCT IN GASTRIC CANCER CACHEXIA." Clinical Nutrition Supplements 4, no. 2 (January 2009): 177. http://dx.doi.org/10.1016/s1744-1161(09)70408-9.

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Ma, Yongsheng, Lin Zhang, Shengzhong Rong, Hongyan Qu, Yannan Zhang, Dong Chang, Hongzhi Pan, and Wenbo Wang. "Relation between Gastric Cancer and Protein Oxidation, DNA Damage, and Lipid Peroxidation." Oxidative Medicine and Cellular Longevity 2013 (2013): 1–6. http://dx.doi.org/10.1155/2013/543760.

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Objects.The aim of this study is to evaluate protein oxidation, DNA damage, and lipid peroxidation in patients with gastric cancer and to investigate the relationship between oxidative stress and gastric cancer.Methods. We investigated changes in serum protein carbonyl (PC), advanced oxidation protein products (AOPP), and 3-nitrotyrosine (3-NT) levels, as indicators of protein oxidation, serum 8-hydroxydeoxyguanosine (8-OHdG), as a biomarker of DNA damage, and malondialdehyde (MDA), conjugated diene (CD), 4-hydroxynonenal (4-HNE), and 8-ISO-prostaglandinF2α(8-PGF) in serum, as lipid peroxidation markers in gastric cancer (GC) patients and healthy control.Results. Compared with control, a statistically significant higher values of 8-OHdG, PC, AOPP, and 3-NT were observed in the GC patients (P<0.05). The products of lipid peroxidation, MDA, CD, 4-HNE, and 8-PGF, were significantly lower in the GC patients compared to those of control (P<0.05). In addition, the products of oxidative stress were similar between the Helicobacter pylori positive and the negative subgroups of GC patients.Conclusions. GC patients were characterized by increased protein oxidation and DNA damage, and decreased lipid peroxidation. Assessment of oxidative stress and augmentation of the antioxidant defense system may be important for the treatment and prevention of gastric carcinogenesis.
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Poojary, Mahesha M., and Marianne N. Lund. "Chemical Stability of Proteins in Foods: Oxidation and the Maillard Reaction." Annual Review of Food Science and Technology 13, no. 1 (March 25, 2022): 35–58. http://dx.doi.org/10.1146/annurev-food-052720-104513.

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Protein is a major nutrient present in foods along with carbohydrates and lipids. Food proteins undergo a wide range of modifications during food production, processing, and storage. In this review, we discuss two major reactions, oxidation and the Maillard reaction, involved in chemical modifications of food proteins. Protein oxidation in foods is initiated by metal-, enzyme-, or light-induced processes. Food protein oxidation results in the loss of thiol groups and the formation of protein carbonyls and specific oxidation products of cysteine, tyrosine, tryptophan, phenylalanine, and methionine residues, such as disulfides, dityrosine, kynurenine, m-tyrosine, and methionine sulfoxide. The Maillard reaction involves the reaction of nucleophilic amino acid residues with reducing sugars, which yields numerous heterogeneous compounds such as α-dicarbonyls, furans, Strecker aldehydes, advanced glycation end-products, and melanoidins. Both protein oxidation and the Maillard reaction result in the loss of essential amino acids but may positively or negatively impact food structure and flavor.
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