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Journal articles on the topic 'Glycation'
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Rabbani, Naila, Maryam Al-Motawa, and Paul J. Thornalley. "Protein Glycation in Plants—An Under-Researched Field with Much Still to Discover." International Journal of Molecular Sciences 21, no. 11 (May 30, 2020): 3942. http://dx.doi.org/10.3390/ijms21113942.
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Recent research has identified glycation as a non-enzymatic post-translational modification of proteins in plants with a potential contributory role to the functional impairment of the plant proteome. Reducing sugars with a free aldehyde or ketone group such as glucose, fructose and galactose react with the N-terminal and lysine side chain amino groups of proteins. A common early-stage glycation adduct formed from glucose is Nε-fructosyl-lysine (FL). Saccharide-derived reactive dicarbonyls are arginine residue-directed glycating agents, forming advanced glycation endproducts (AGEs). A dominant dicarbonyl is methylglyoxal—formed mainly by the trace-level degradation of triosephosphates, including through the Calvin cycle of photosynthesis. Methylglyoxal forms the major quantitative AGE, hydroimidazolone MG-H1. Glucose and methylglyoxal concentrations in plants change with the developmental stage, senescence, light and dark cycles and also likely biotic and abiotic stresses. Proteomics analysis indicates that there is an enrichment of the amino acid residue targets of glycation, arginine and lysine residues, in predicted functional sites of the plant proteome, suggesting the susceptibility of proteins to functional inactivation by glycation. In this review, we give a brief introduction to glycation, glycating agents and glycation adducts in plants. We consider dicarbonyl stress, the functional vulnerability of the plant proteome to arginine-directed glycation and the likely role of methylglyoxal-mediated glycation in the activation of the unfolded protein response in plants. The latter is linked to the recent suggestion of protein glycation in sugar signaling in plant metabolism. The overexpression of glyoxalase 1, which suppresses glycation by methylglyoxal and glyoxal, produced plants resistant to high salinity, drought, extreme temperature and other stresses. Further research to decrease protein glycation in plants may lead to improved plant growth and assist the breeding of plant varieties resistant to environmental stress and senescence—including plants of commercial ornamental and crop cultivation value.
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Thornalley, P. J. "The enzymatic defence against glycation in health, disease and therapeutics: a symposium to examine the concept." Biochemical Society Transactions 31, no. 6 (December 1, 2003): 1341–42. http://dx.doi.org/10.1042/bst0311341.
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Glycation of proteins, nucleotides and basic phospholipids by glucose, glyoxal, methylglyoxal, 3-deoxyglucosone and other saccharide derivatives is potentially damaging to the proteome and mutagenic. It is now recognized that there is an enzymatic defence against glycation – a group of enzymes that suppress the physiological levels of potent glycating agents and repair glycated proteins: glyoxalase I, aldehyde reductases and dehydrogenases, amadoriase and fructosamine 3-phosphokinase. The enzymatic defence against glycation influences morbidity and the efficiency of drug therapy in certain diseases. Improved understanding of the balance between glycation and the enzymatic anti-glycation defence will advance disease diagnosis and therapy.
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Khan, Hamda, Mohd Waseem, Mohammad Faisal, Abdulrahman A. Alatar, Ahmed A. Qahtan, and Saheem Ahmad. "Inhibitory Effect of Multimodal Nanoassemblies against Glycative and Oxidative Stress in Cancer and Glycation Animal Models." BioMed Research International 2021 (April 9, 2021): 1–17. http://dx.doi.org/10.1155/2021/8892156.
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In recent years, there has been a progress in the study of glycation reaction which is one the possible reason for multiple metabolic disorders. Glycation is a nonenzymatic reaction between nucleic acids, lipids, and proteins resulting into the formation of early glycation products that may further lead to the accumulation of advanced glycation end products (AGEs). The precipitation of AGEs in various cells, tissues, and organs is one of the factors for the initiation and progression of various metabolic derangements including the cancer. The AGE interaction with its receptor “RAGE” activates the inflammatory pathway; yet, the downregulation of RAGE and its role in these pathways are not clear. We explore the effect of anticancer novel nanoassemblies on AGEs to determine its role in the regulation of the expression of RAGE, NFƙB, TNF-α, and IFN-γ. This paper is based on the in vivo and in vitro study in glycation and lung cancer model systems. Upon the treatment of nanoassemblies in both the model systems, we observed a protective effect of nanoassemblies over the inhibition of glycative and oxidative stress via mRNA expression analysis. The mRNA expression results corroborated with the reactive oxygen species (ROS), carboxy-methyl-lysine (CML), and fluorescence studies. In this study, we found that the presence of common factors for glycation and lung cancer is oxidative and glycative stress. This oxidation and glycation might be responsible for the initiation of inflammation which may further lead to uncontrolled growth of cells leading to cancer. This can be a strong association between lung cancer and glycation reaction. The intervention of the anticancer and antiglycation effects of multimodal nanoassemblies throughout the study promises a new pathway for cancer research.
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Kumar, P. Anil, M. Satish Kumar, and G. Bhanuprakash Reddy. "Effect of glycation on α-crystallin structure and chaperone-like function." Biochemical Journal 408, no. 2 (November 14, 2007): 251–58. http://dx.doi.org/10.1042/bj20070989.
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The chaperone-like activity of α-crystallin is considered to play an important role in the maintenance of the transparency of the eye lens. However, in the case of aging and in diabetes, the chaperone function of α-crystallin is compromized, resulting in cataract formation. Several post-translational modifications, including non-enzymatic glycation, have been shown to affect the chaperone function of α-crystallin in aging and in diabetes. A variety of agents have been identified as the predominant sources for the formation of AGEs (advanced glycation end-products) in various tissues, including the lens. Nevertheless, glycation of α-crystallin with various sugars has resulted in divergent results. In the present in vitro study, we have investigated the effect of glucose, fructose, G6P (glucose 6-phosphate) and MGO (methylglyoxal), which represent the major classes of glycating agents, on the structure and chaperone function of α-crystallin. Modification of α-crystallin with all four agents resulted in the formation of glycated protein, increased AGE fluorescence, protein cross-linking and HMM (high-molecular-mass) aggregation. Interestingly, these glycation-related profiles were found to vary with different glycating agents. For instance, CML [Nϵ-(carboxymethyl)lysine] was the predominant AGE formed upon glycation of α-crystallin with these agents. Although fructose and MGO caused significant conformational changes, there were no significant structural perturbations with glucose and G6P. With the exception of MGO modification, glycation with other sugars resulted in decreased chaperone activity in aggregation assays. However, modification with all four sugars led to the loss of chaperone activity as assessed using an enzyme inactivation assay. Glycation-induced loss of α-crystallin chaperone activity was associated with decreased hydrophobicity. Furthermore, α-crystallin isolated from glycated TSP (total lens soluble protein) had also increased AGE fluorescence, CML formation and diminished chaperone activity. These results indicate the susceptibility of α-crystallin to non-enzymatic glycation by various sugars and their derivatives, whose levels are elevated in diabetes. We also describes the effects of glycation on the structure and chaperone-like activity of α-crystallin.
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Inagi, Reiko. "Glycative stress and glyoxalase in kidney disease and aging." Biochemical Society Transactions 42, no. 2 (March 20, 2014): 457–60. http://dx.doi.org/10.1042/bst20140007.
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Glycation is one of the important reactions regulating physiological state, and glycative stress, namely an overwhelming and unfavourable glycation state, is established as a pathological factor. Glycative stress is closely associated with not only various kidney diseases, but also kidney aging. Accumulating evidence, including studies in my laboratory, demonstrates that progression of renal tubular damage and its aging is correlated with the decrease in the activity of anti-glycative stress enzyme Glo1 (glyoxalase I) in the kidney. The reduction of glycative and oxidative stresses by Glo1 overexpression is beneficial for prevention of kidney disease and treatment, suggesting the novel therapeutic approaches targeting Glo1. The present review is focused on the impact of glycative stress and Glo1 on protein homoeostasis and discusses further the cross-talk between glycative stress and UPR (unfolded protein response), which controls the protein homoeostasis state.
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Khan, Mohd W. A., Ahmed A. Otaibi, Arwa F. M. Alhumaid, Abdulmohsen K. D. Alsukaibi, Asma K. Alshamari, Eida M. Alshammari, Salma A. Al-Zahrani, Ahmed Y. M. Almudyani, and Subuhi Sherwani. "Garlic Extract: Inhibition of Biochemical and Biophysical Changes in Glycated HSA." Applied Sciences 11, no. 22 (November 21, 2021): 11028. http://dx.doi.org/10.3390/app112211028.
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Glycation of various biomolecules contributes to structural changes and formation of several high molecular weight fluorescent and non-fluorescent, advanced glycation end products (AGEs). AGEs and glycation are involved in various health complications. Synthetic medicines, including metformin, have several adverse effects. Natural products and their derivatives are used in the treatment of various diseases due to their significant therapeutic qualities. Allium sativum (garlic) is used in traditional medicines because of its antioxidant, anti-inflammatory, and anti-diabetic properties. This study aimed to determine the anti-glycating and AGEs inhibitory activities of garlic. Biochemical and biophysical analyses were performed for in vitro incubated human serum albumin (HSA) with 0.05 M of glucose for 1, 5, and 10 weeks. Anti-glycating and AGEs inhibitory effect of garlic was investigated in glycated samples. Increased biochemical and biophysical changes were observed in glycated HSA incubated for 10 weeks (G-HSA-10W) as compared to native HSA (N-HSA) as well as glycated HSA incubated for 1 (G-HSA-1W) and 5 weeks (G-HSA-5W). Garlic extract with a concentration of ≥6.25 µg/mL exhibited significant inhibition in biophysical and biochemical changes of G-HSA-10W. Our findings demonstrated that garlic extract has the ability to inhibit biochemical and biophysical changes in HSA that occurred due to glycation. Thus, garlic extract can be used against glycation and AGE-related health complications linked with chronic diseases in diabetic patients due to its broad therapeutic potential.
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Das, Sourav, Sharat Sarmah, Zaved Hazarika, Mostofa Ataur Rohman, Pallavi Sarkhel, Anupam Nath Jha, and Atanu Singha Roy. "Targeting the heme protein hemoglobin by (−)-epigallocatechin gallate and the study of polyphenol–protein association using multi-spectroscopic and computational methods." Physical Chemistry Chemical Physics 22, no. 4 (2020): 2212–28. http://dx.doi.org/10.1039/c9cp05301h.
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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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Sattar, Naila Abdul, Fatma Hussain, Tahira Iqbal, and Munir Ahmad Sheikh. "Determination of in vitro antidiabetic effects of Zingiber officinale Roscoe." Brazilian Journal of Pharmaceutical Sciences 48, no. 4 (December 2012): 601–7. http://dx.doi.org/10.1590/s1984-82502012000400003.
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Aqueous extracts of Zingiber officinale rhizomes were studied to evaluate their antidiabetic effects on protein glycation and on the diffusion of glucose in vitro in the present study. Zingiber officinale rhizome aqueous extract were examined at concentrations of 5, 10, 20 and 40 g/L. The antidiabetic effects were found to be dose-dependent. Antidiabetic potential of Zingiber officinale was mainly through inhibition of the glucose diffusion and to a limited extent by reducing the glycation. However, further studies are needed to determine in vitro effects of therapeutic potential by restraining postprandial glucose absorptions and plasma protein glycations in diabetic subjects.
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Biedrzycki, Grzegorz, Blanka Wolszczak-Biedrzycka, Justyna Dorf, Daniel Michalak, Małgorzata Żendzian-Piotrowska, Anna Zalewska, and Mateusz Maciejczyk. "Antioxidant and Anti-Glycation Potential of H2 Receptor Antagonists—In Vitro Studies and a Systematic Literature Review." Pharmaceuticals 16, no. 9 (September 8, 2023): 1273. http://dx.doi.org/10.3390/ph16091273.
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Background: Histamine H2 receptor antagonists are a group of drugs that inhibit gastric juice secretion in gastrointestinal diseases. However, there is evidence to suggest that H2 blockers have a broader spectrum of activity. The antioxidant properties of H2 blockers have not been fully elucidated, and their anti-glycation potential has not been studied to date. Therefore, this is the first study to compare the antioxidant and antiglycation potentials of the most popular H2 antagonists (ranitidine, cimetidine, and famotidine) on protein glycoxidation in vitro. Methods: Bovine serum albumin (BSA) was glycated using sugars (glucose, fructose, galactose, and ribose) as well as aldehydes (glyoxal and methylglyoxal). Results: In the analyzed group of drugs, ranitidine was the only H2 blocker that significantly inhibited BSA glycation in all tested models. The contents of protein carbonyls, protein glycoxidation products (↓dityrosine, ↓N-formylkynurenine), and early (↓Amadori products) and late-stage (↓AGEs) protein glycation products decreased in samples of glycated BSA with the addition of ranitidine relative to BSA with the addition of the glycating agents. The anti-glycation potential of ranitidine was comparable to those of aminoguanidine and Trolox. In the molecular docking analysis, ranitidine was characterized by the lowest binding energy for BSA sites and could compete with protein amino groups for the addition of carbonyl groups. H2 blockers also scavenge free radicals. The strongest antioxidant properties are found in ranitidine, which additionally has the ability to bind transition metal ions. The systematic literature review also revealed that the anti-glycation effects of ranitidine could be attributed to its antioxidant properties. Conclusions: Ranitidine showed anti-glycation and antioxidant properties. Further research is needed, particularly in patients with diseases that promote protein glycation.
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Adeniran, Oluwaseyefunmi Iyabo, Lesibana Samuel Sethoga, Leshweni Jeremia Shai, and Sechene Stanley Gololo. "Anti-glycation and phytochemical properties of cinnamon stem-bark water extract." Asian Journal of Chemistry 35, no. 9 (August 31, 2023): 2235–40. http://dx.doi.org/10.14233/ajchem.2023.28084.
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The study evaluated the ability of cinnamon stem-bark water extract (CWE) to break established cross-links formed between proteins and advanced glycation end-products (AGEs) as well as its anti-glycation effect. The extract showed a dose-dependent anti-glycation effect against total fluorescent AGEs (FAGEs) derived from both glucose and fructose. CWE recorded a uniform IC50 value of 0.13 mg/mL for both glucose and fructose-derived FAGEs while aminoguanidine, a well-known synthetic anti-glycative agent gave IC50 values of 0.14 mg/mL for the glucose and 0.17 mg/mL for the fructose derived FAGEs. The anti-glycative effect of CWE was also significantly higher than aminoguanidine against total immunogenic AGE (TIAGEs) in both sugar models (p < 0.001). While CWE and aminoguanidine showed weak protein cross-link breaking activity selectively on fructose-derived protein cross-links already formed, none whatsoever was detected exerted on the established glucose-derived protein cross-links. Phytochemical screening revealed the presence of several important secondary metabolites which may have contributed to the anti-glycative effect of CWE. Gas chromatography mass spectrometry enabled the identification of (+)-alpha-tocopherol acetate, a chain breaker, in the methanol fraction of CWE. Although CWE showed great potential for inhibition of formation of major types of AGEs, it appears to be poor in breaking established cross-links formed between proteins and AGEs.
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Scott, Gary F., Anh Q. Nguyen, Brandon H. Cherry, Roger A. Hollrah, Isabella Salinas, Arthur G. Williams, Myoung-Gwi Ryou, and Robert T. Mallet. "Featured Article: Pyruvate preserves antiglycation defenses in porcine brain after cardiac arrest." Experimental Biology and Medicine 242, no. 10 (March 31, 2017): 1095–103. http://dx.doi.org/10.1177/1535370217703353.
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Cardiac arrest (CA) and cardiocerebral resuscitation (CCR)-induced ischemia–reperfusion imposes oxidative and carbonyl stress that injures the brain. The ischemic shift to anaerobic glycolysis, combined with oxyradical inactivation of glyceraldehyde 3-phosphate dehydrogenase (GAPDH), provokes excessive formation of the powerful glycating agent, methylglyoxal. The glyoxalase (GLO) system, comprising the enzymes glyoxalase 1 (GLO1) and GLO2, utilizes reduced glutathione (GSH) supplied by glutathione reductase (GR) to detoxify methylglyoxal resulting in reduced protein glycation. Pyruvate, a natural antioxidant that augments GSH redox status, could sustain the GLO system in the face of ischemia–reperfusion. This study assessed the impact of CA-CCR on the cerebral GLO system and pyruvate’s ability to preserve this neuroprotective system following CA. Domestic swine were subjected to 10 min CA, 4 min closed-chest CCR, defibrillation and 4 h recovery, or to a non-CA sham protocol. Sodium pyruvate or NaCl control was infused (0.1 mmol/kg/min, intravenous) throughout CCR and the first 60 min recovery. Protein glycation, GLO1 content, and activities of GLO1, GR, and GAPDH were analyzed in frontal cortex biopsied at 4 h recovery. CA-CCR produced marked protein glycation which was attenuated by pyruvate treatment. GLO1, GR, and GAPDH activities fell by 86, 55, and 30%, respectively, after CA-CCR with NaCl infusion. Pyruvate prevented inactivation of all three enzymes. CA-CCR sharply lowered GLO1 monomer content with commensurate formation of higher molecular weight immunoreactivity; pyruvate preserved GLO1 monomers. Thus, ischemia–reperfusion imposed by CA-CCR disabled the brain’s antiglycation defenses. Pyruvate preserved these enzyme systems that protect the brain from glycation stress. Impact statement Recent studies have demonstrated a pivotal role of protein glycation in brain injury. Methylglyoxal, a by-product of glycolysis and a powerful glycating agent in brain, is detoxified by the glutathione-catalyzed glyoxalase (GLO) system, but the impact of cardiac arrest (CA) and cardiocerebral resuscitation (CCR) on the brain’s antiglycation defenses is unknown. This study in a swine model of CA and CCR demonstrated for the first time that the intense cerebral ischemia–reperfusion imposed by CA-resuscitation disabled glyoxalase-1 and glutathione reductase (GR), the source of glutathione for methylglyoxal detoxification. Moreover, intravenous administration of pyruvate, a redox-active intermediary metabolite and antioxidant in brain, prevented inactivation of glyoxalase-1 and GR and blunted protein glycation in cerebral cortex. These findings in a large mammal are first evidence of GLO inactivation and the resultant cerebral protein glycation after CA-resuscitation, and identify novel actions of pyruvate to minimize protein glycation in postischemic brain.
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Khan, Mohd W. A., Ahmed A. Otaibi, Abdulmohsen K. D. Alsukaibi, Eida M. Alshammari, Salma A. Al-Zahrani, Subuhi Sherwani, Wahid A. Khan, Ritika Saha, Smita R. Verma, and Nessar Ahmed. "Biophysical, Biochemical, and Molecular Docking Investigations of Anti-Glycating, Antioxidant, and Protein Structural Stability Potential of Garlic." Molecules 27, no. 6 (March 14, 2022): 1868. http://dx.doi.org/10.3390/molecules27061868.
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Garlic has been reported to inhibit protein glycation, a process that underlies several disease processes, including chronic complications of diabetes mellitus. Biophysical, biochemical, and molecular docking investigations were conducted to assess anti-glycating, antioxidant, and protein structural protection activities of garlic. Results from spectral (UV and fluorescence) and circular dichroism (CD) analysis helped ascertain protein conformation and secondary structure protection against glycation to a significant extent. Further, garlic showed heat-induced protein denaturation inhibition activity (52.17%). It also inhibited glycation, advanced glycation end products (AGEs) formation as well as lent human serum albumin (HSA) protein structural stability, as revealed by reduction in browning intensity (65.23%), decrease in protein aggregation index (67.77%), and overall reduction in cross amyloid structure formation (33.26%) compared with positive controls (100%). The significant antioxidant nature of garlic was revealed by FRAP assay (58.23%) and DPPH assay (66.18%). Using molecular docking analysis, some of the important garlic metabolites were investigated for their interactions with the HSA molecule. Molecular docking analysis showed quercetin, a phenolic compound present in garlic, appears to be the most promising inhibitor of glucose interaction with the HSA molecule. Our findings show that garlic can prevent oxidative stress and glycation-induced biomolecular damage and that it can potentially be used in the treatment of several health conditions, including diabetes and other inflammatory diseases.
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Ali, Ahmad, Tejashree Anil More, Amaritpal Kaur Hoonjan, and Subramanian Sivakami. "Antiglycating potential of acesulfame potassium: an artificial sweetener." Applied Physiology, Nutrition, and Metabolism 42, no. 10 (October 2017): 1054–63. http://dx.doi.org/10.1139/apnm-2017-0119.
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Sweeteners have replaced the natural sugars in the food and beverage industry because of many reasons, such as hyperglycemia and cost. Saccharin, sucralose, aspartame and acesulfame-K are the most commonly used sweeteners. In the present study, the abovementioned artificial sweeteners were used to assess their glycating properties by established methods such as browning, fructosamine assay, determination of carbonyl content, protein aggregation, and measurement of fluorescence. Amadori and advanced glycation end products (AGEs) are formed as a result of the interaction between carbonyl groups of reducing sugars and amino groups of proteins and other macromolecules during glycation. The objective of this study was to investigate the influence of artificial sweeteners on the formation of AGEs and protein oxidation in an in vitro model of glucose-mediated protein glycation. The results indicated that the abovementioned artificial sweeteners do not enhance the process of glycation. On the other hand, acesulfame-K was found to have antiglycating potential as it caused decreased formation of Amadori products and AGEs. Further studies are essential in the characterization of Amadori products and AGEs produced as a result of interaction between sweeteners and proteins, which are interfered with by sweeteners. This study is significant in understanding the probable role of artificial sweeteners in the process of glycation and the subsequent effect on macromolecular alteration.
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Colaco, Camilo A. L. S., and Charles R. Harrington. "Glycation." NeuroReport 5, no. 8 (April 1994): 859–61. http://dx.doi.org/10.1097/00001756-199404000-00001.
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Thornalley, Paul J. "Measurement of Protein Glycation, Glycated Peptides, and Glycation Free Adducts." Peritoneal Dialysis International: Journal of the International Society for Peritoneal Dialysis 25, no. 6 (November 2005): 522–33. http://dx.doi.org/10.1177/089686080502500603.
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Protein glycation adducts, early glycation adducts, such as N∊-fructosyl-lysine, and advanced glycation end products (AGEs) are uremic toxins. Glycation adducts are found in plasma and tissue proteins (glycation adduct residues), in peptides (glycation adduct peptide residues), and glycated amino acids (glycation free adducts). The latter two analyte groups arise from proteolysis of glycated proteins and glycation of peptides and amino acids. Quantitation of glycation adducts in uremia is difficult because of the presence of many different AGEs at low concentrations in different forms in the presence of many potential interferences. Application of liquid chromatography with tandem mass spectrometric (LC-MS/MS) detection to plasma, urine, and dialysate samples of uremic patients has provided a comprehensive and quantitative analysis of glycation adducts in uremia. Glycation free adducts accumulate markedly in the plasma of uremic patients and are eliminated in the peritoneal dialysate. Multiple glycation adducts, and also protein oxidation and nitration adducts, may be quantified concurrently. Glycation free adducts are the major form of glycation adduct eliminated in dialysate. LC-MS/MS may now be used to quantify concentrations, extents of protein modification, clearances, and excretion rates of glycation adducts in uremia.
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Stoynev, Georgi, Ljuba Srebreva, Roumyana Gugova, Evgeny Golovinsky, and Ivan Ivanov. "Inhibitory Effect of Some Acetyl Esters and Acetamides on Glycation of the Histone H1." Zeitschrift für Naturforschung C 63, no. 7-8 (August 1, 2008): 526–32. http://dx.doi.org/10.1515/znc-2008-7-810.
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Non-enzymatic glycosylation (glycation) is a spontaneous set of reactions between reducing sugars and free amino groups in proteins or other biomolecules leading to the formation of fluorescent and coloured compounds known as advanced glycation end products (AGEs). AGEs cause structural changes of key proteins in humans, and therefore they are related with a number of physiological processes and diseases such as aging, atherosclerosis, cataract, arthritis, Alzheimer’s disease. Two main strategies have been employed to prevent the formation of AGEs: a) low carbohydrate diet and b) pharmacological intervention. The latter includes treatment with reactive compounds which might be either sugar competitors (type A), carbonyl traps (type B) or free radical trapping antioxidants (type C). Acetylsalicylic acid (ASA, aspirin) is a good example of sugar competitor capable of inhibiting glycation by acetylating ε-amino groups of lysine residues in proteins. Taking into consideration the inhibiting effect of ASA on glycation we designed to study the antiglycation activity of other acetyl group-containing compounds (acetamides and acetyl esters) using the lysine-rich protein histone H1 as a model. The glycation of the histone H1 was carried out by either fructose or a complex mixture of glycating agents obtained from E. coli and monitored by fluorescent spectroscopy, SDS-PAGE and measurement of the content of reactive carbonyl groups in the target protein. Our results showed that the inhibitory effect of phenyl acetate, acetanilide, 4-acetamidophenylacetic acid and isopropenyl acetate was comparable to that of ASA. Based on the obtained results we conclude that these compounds act as free radical scavengers protecting proteins from the damaging effect of reactive oxygen species produced during the formation of AGEs.
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Muthenna, Puppala, Chandrasekhar Akileshwari, and G. Bhanuprakash Reddy. "Ellagic acid, a new antiglycating agent: its inhibition of Nϵ-(carboxymethyl)lysine." Biochemical Journal 442, no. 1 (January 27, 2012): 221–30. http://dx.doi.org/10.1042/bj20110846.
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Non-enzymatic glycation is a complex series of reactions between reducing sugars and amino groups of proteins. Accumulation of AGEs (advanced glycation end-products) due to non-enzymatic glycation has been related to several diseases associated with aging and diabetes. The formation of AGEs is accelerated in hyperglycaemic conditions, which alters the structure and function of long-lived proteins, thereby contributing to long-term diabetic complications. The present study describes AGE inhibition and the mechanism of action of a new antiglycating agent, EA (ellagic acid), a flavonoid present in many dietary sources. Inhibition of AGE formation by EA was demonstrated with different proteins, namely eye lens TSP (total soluble protein), Hb (haemoglobin), lysozyme and BSA, using different glycating agents such as fructose, ribose and methylglyoxal by a set of complementary methods. These results suggest that the antiglycating action of EA seems to involve, apart from inhibition of a few fluorescent AGEs, predominantly inhibition of CEL [Nϵ-(carboxyethyl)lysine] through scavenging of the dicarbonyl compounds. Furthermore, MALDI–TOF-MS (matrix-assisted laser-desorption ionisation–time-of-flight MS) analysis confirms inhibition of the formation of CEL on lysozyme on in vitro glycation by EA. Prevention of glycation-mediated β-sheet formation in Hb and lysozyme by EA confirm its antiglycating ability. Inhibition of glycosylated Hb formation in human blood under ex vivo high-glucose conditions signifies the physiological antiglycating potential of EA. We have also determined the effectiveness of EA against loss of eye lens transparency through inhibition of AGEs in the lens organ culture system. These findings establish the antiglycating potential of EA and its in vivo utility in controlling AGE-mediated diabetic pathologies.
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YAGI, Masayuki, Wakako TAKABE, Kaori ISHIZAKI, and Yoshikazu YONEI. "The Evaluation of Glycative Stress and Anti-glycation Effect." Oleoscience 18, no. 2 (2018): 67–73. http://dx.doi.org/10.5650/oleoscience.18.67.
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Nishinaka, Takashi, Shuji Mori, Yui Yamazaki, Atsuko Niwa, Hidenori Wake, Tadashi Yoshino, Masahiro Nishibori, and Hideo Takahashi. "A comparative study of sulphated polysaccharide effects on advanced glycation end-product uptake and scavenger receptor class A level in macrophages." Diabetes and Vascular Disease Research 17, no. 1 (January 2020): 147916411989697. http://dx.doi.org/10.1177/1479164119896975.
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Advanced glycation end-products, especially toxic advanced glycation end-products derived from glyceraldehyde (advanced glycation end-product-2) and glycolaldehyde (advanced glycation end-product-3), are biologically reactive compounds associated with diabetic complications. We previously demonstrated that toxic advanced glycation end-products were internalised into macrophage-like RAW264.7 cells through scavenger receptor-1 class A (CD204). Toxic advanced glycation end-product uptake was inhibited by fucoidan, a sulphated polysaccharide and antagonistic ligand for scavenger receptors, suggesting that sulphated polysaccharides are emerging candidates for treatment of advanced glycation end-product–related diseases. In this study, we compared the effects of six types of sulphated and non-sulphated polysaccharides on toxic advanced glycation end-product uptake in RAW264.7 cells. Fucoidan, carrageenan and dextran sulphate attenuated toxic advanced glycation end-product uptake. Fucoidan and carrageenan inhibited advanced glycation end-product-2–induced upregulation of SR-A, while advanced glycation end-product-3–induced upregulation of scavenger receptor-1 class A was only suppressed by fucoidan. Dextran sulphate did not affect scavenger receptor-1 class A levels in toxic advanced glycation end-product–treated cells. Chondroitin sulphate, heparin and hyaluronic acid failed to attenuate toxic advanced glycation end-product uptake. Heparin and hyaluronic acid had no effect on scavenger receptor-1 class A levels, while chondroitin sulphate inhibited advanced glycation end-product-3–induced upregulation of scavenger receptor-1 class A. Taken together, fucoidan and carrageenan, but not the other sulphated polysaccharides examined, had inhibitory activities on toxic advanced glycation end-product uptake and toxic advanced glycation end-product–induced upregulation of scavenger receptor-1 class A, possibly because of structural differences among sulphated polysaccharides.
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THORNALLEY, Paul J., Sinan BATTAH, Naila AHMED, Nikolaos KARACHALIAS, Stamatina AGALOU, Roya BABAEI-JADIDI, and Anne DAWNAY. "Quantitative screening of advanced glycation endproducts in cellular and extracellular proteins by tandem mass spectrometry." Biochemical Journal 375, no. 3 (November 1, 2003): 581–92. http://dx.doi.org/10.1042/bj20030763.
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Glycation of proteins forms fructosamines and advanced glycation endproducts. Glycation adducts may be risk markers and risk factors of disease development. We measured the concentrations of the early glycation adduct fructosyl-lysine and 12 advanced glycation endproducts by liquid chromatography with tandem mass spectrometric detection. Underivatized analytes were detected free in physiological fluids and in enzymic hydrolysates of cellular and extracellular proteins. Hydroimidazolones were the most important glycation biomarkers quantitatively; monolysyl adducts (Nε-carboxymethyl-lysine and Nε-1-carboxyethyl-lysine) were found in moderate amounts, and bis(lysyl)imidazolium cross-links and pentosidine in lowest amounts. Quantitative screening showed high levels of advanced glycation endproducts in cellular protein and moderate levels in protein of blood plasma. Glycation adduct accumulation in tissues depended on the particular adduct and tissue type. Low levels of free advanced glycation endproducts were found in blood plasma and levels were 10–100-fold higher in urine. Advanced glycation endproduct residues were increased in blood plasma and at sites of vascular complications development in experimental diabetes; renal glomeruli, retina and peripheral nerve. In clinical uraemia, the concentrations of plasma protein advanced glycation endproduct residues increased 1–7-fold and free adduct concentrations increased up to 50-fold. Comprehensive screening of glycation adducts revealed the relative and quantitative importance of α-oxoaldehyde-derived advanced glycation endproducts in physiological modification of proteins–particularly hydroimidazolones, the efficient renal clearance of free adducts, and the marked increases of glycation adducts in diabetes and uraemia–particularly free advanced glycation endproducts in uraemia. Increased levels of these advanced glycation endproducts were associated with vascular complications in diabetes and uraemia.
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Yim, Moon B., Hyung-Soon Yim, Cheolju Lee, Sa-Ouk Kang, and P. Boon Chock. "Protein Glycation." Annals of the New York Academy of Sciences 928, no. 1 (January 25, 2006): 48–53. http://dx.doi.org/10.1111/j.1749-6632.2001.tb05634.x.
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Wautier, Jean-Luc, and Ann Marie Schmidt. "Protein Glycation." Circulation Research 95, no. 3 (August 6, 2004): 233–38. http://dx.doi.org/10.1161/01.res.0000137876.28454.64.
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Senavirathna, Lakmini, Cheng Ma, Ru Chen, and Sheng Pan. "Proteomic Investigation of Glyceraldehyde-Derived Intracellular AGEs and Their Potential Influence on Pancreatic Ductal Cells." Cells 10, no. 5 (April 24, 2021): 1005. http://dx.doi.org/10.3390/cells10051005.
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Glyceraldehyde-derived advanced glycation end products (AGEs) play an important role in the pathogenesis of many diseases including cancer. Accumulation of intracellular AGEs could stimulate cancer induction and facilitate cancer progression. We evaluated the toxic effect of glyceraldehyde-derived intracellular AGEs on normal and malignant pancreatic ductal cells by assessing the cell viability, toxicity, and oxidative stress, followed by proteomic analysis. Our functional studies showed that pancreatic cancer cells (PANC-1 and MIA PaCa-2) were more resistant to glyceraldehyde treatment compared to normal pancreatic ductal epithelial cells (HPDE), while cytotoxicity effects were observed in all cell types. Furthermore, using 13C isotopic labeled glyceraldehyde, the proteomic data revealed a dose-dependent increment of the number of glycation adducts in both these cell types. HPDE cells showed a higher number of intracellular AGEs compared to cancer cells. At a molecular level, the glycations in the lysine residues of proteins showed a concurrent increase with the concentration of the glyceraldehyde treatment, while the arginine glycations appeared to be less affected by the glyceraldehyde doses. Further pathway analysis of these glycated proteins suggested that the glycated proteins participate in important biological processes that are major hallmarks of cancer initiation and progression, including metabolic processes, immune response, oxidative stress, apoptosis, and S100 protein binding.
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Yoon, Sohyun, Minkyung Kim, Seoungwoo Shin, Jieun Woo, Dahee Son, Dehun Ryu, Jiseon Yoo, Deokhoon Park, and Eunsun Jung. "Effect of Cirsium japonicum Flower Extract on Skin Aging Induced by Glycation." Molecules 27, no. 7 (March 24, 2022): 2093. http://dx.doi.org/10.3390/molecules27072093.
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Advanced glycation end products (AGEs) have recently been increasingly discussed as one factor of skin aging. In this study, we investigated the effects of Cirsium japonicum flower (CFE) extract on glycation in relation to skin aging and skin elasticity. Moreover, we learned the main active constituent of CFE that has effects against glycation. To demonstrate the effects of CFE on glycation, we carried out an in vitro glycation study, 3-dimensional culture, and clinical study. As a result, CFE inhibited formation of AGEs in both bovine serum albumin (BSA)/glucose glycation system and aldehyde-derived glycation system. Moreover, CFE reduced Nε-(carboxymethyl), lysine (CML), and carbonylated proteins that increased by glycation. Furthermore, CFE broke crosslinks of collagen–AGEs and inhibited the increase of matrix metalloproteinase-1 (MMP-1) gene expression by AGEs. In the 3D culture condition, CFE restored the reduction of collagen gel contraction by glycation. Moreover, apigenin was detected as the main active constituent in CFE that has anti-glycation effects. In the clinical study, we confirmed that CFE has effects on skin wrinkles and skin elasticity. Our findings suggest that CFE can be used as a cosmetic or cosmeceutical ingredient for improving skin elasticity and wrinkles. Regulation of AGEs can be an interesting target for anti-aging.
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Roberts, Norman B., Alieu B. Amara, Michael Morris, and Brian N. Green. "Long-Term Evaluation of Electrospray Ionization Mass Spectrometric Analysis of Glycated Hemoglobin." Clinical Chemistry 47, no. 2 (February 1, 2001): 316–21. http://dx.doi.org/10.1093/clinchem/47.2.316.
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Abstract Background: Electrospray ionization mass spectrometry (ESIMS) has been successfully applied to the identification of hemoglobin (Hb) variants and the presence of glucose adducts (mass difference of 162 Da) on the separate Hb α and β chains. To establish the potential of ESIMS as a routine and/or a reference method for the quantification of glycohemoglobin (HbA1c), we carried out a detailed evaluation over a 4-month period in a routine laboratory environment. Methods: We optimized a procedure using ESIMS suitable for the routine quantitative analysis of HbA1c. We determined reliability and reproducibility over 4 months and assessed the potential for automated sample injection. We then compared values of 1022 blood samples from diabetic patients with a routine HPLC-based ion-exchange procedure (HA-8140; Menarini). Results: Results of HbA1c measurement by ESIMS were available within 3 min. The analytical imprecision (CV) was 1.6–5.0% for both manual and automated injections. Data collection over the m/z 980-1400 range confirmed lower glycation of the α chain relative to the β chain (0.66:1). Only one glycation was observed per globin chain. The overall glycohemoglobin (i.e., the average of α- and β-chain glycations) measured by ESIMS (x) on 1022 blood samples was lower than by HPLC (y): y = 1.0432x + 0.4815. However, the β-chain glycation measured by ESIMS was up to 20% higher than the value measured by ion-exchange HPLC and showed a close conformity, particularly at 5–10% HbA1c, with the ion-exchange Diabetes Control and Complications Trial (DCCT)-corrected and the United Kingdom National External Quality Assessment Scheme DCCT mean return values. Conclusions: ESIMS provides a precise measurement of HbA1c and, in particular, glycation of the β chain. The method is robust and could be proposed as a procedure to substantiate HbA1c measurement and/or calibration.
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Grzebyk, Ewa, and Agnieszka Piwowar. "Inhibition of glycoxidative modification of proteins by some substances of natural origin." Herba Polonica 62, no. 1 (March 1, 2016): 66–82. http://dx.doi.org/10.1515/hepo-2016-0006.
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Summary Introduction: Advanced glycation end-products (AGE) and advanced oxidation protein products (AOPP) are the main products of glycoxidative modification in diabetes. Objective: The aim of this study was to identify the natural substance with the strongest antiglycoxidative properties among dietary supplements or medicines available without prescription in Poland. Methods: Bovine serum albumin (BSA), vitamin C (VC), aminoguanidine (A), quercetin (Q) and green tea (GT) were tested in vitro in comparison to controls in glycation, oxidation and glycoxidation processes. The decreased AGE and AOPP concentrations were measured as markers of these processes. Results: AGE level was reduced by 72% by VC and at least by 43% by all examined substances in the glycation process. AOPP was reduced by 99% by VC and at least by 40% by all examined substances in the oxidation process. Formation of AGE/AOPP was inhibited by 61% by Q and by 97% by A, and at least 49/88% by all examined substances, respectively. This lowering of AGE/AOPP level was statistically significant (p<0.001) for all test substances in comparison to the positive control C(+). Conclusion: All examined substances are able to inhibit glycative, oxidative and glycoxidative modification of proteins in different degrees depending on their concentration.
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Gomes, Ricardo A., Luís M. A. Oliveira, Mariana Silva, Carla Ascenso, Alexandre Quintas, Gonçalo Costa, Ana V. Coelho, et al. "Protein glycation in vivo: functional and structural effects on yeast enolase." Biochemical Journal 416, no. 3 (November 26, 2008): 317–26. http://dx.doi.org/10.1042/bj20080632.
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Protein glycation is involved in structure and stability changes that impair protein functionality, which is associated with several human diseases, such as diabetes and amyloidotic neuropathies (Alzheimer's disease, Parkinson's disease and Andrade's syndrome). To understand the relationship of protein glycation with protein dysfunction, unfolding and β-fibre formation, numerous studies have been carried out in vitro. All of these previous experiments were conducted in non-physiological or pseudo-physiological conditions that bear little to no resemblance to what may happen in a living cell. In vivo, glycation occurs in a crowded and organized environment, where proteins are exposed to a steady-state of glycation agents, namely methylglyoxal, whereas in vitro, a bolus of a suitable glycation agent is added to diluted protein samples. In the present study, yeast was shown to be an ideal model to investigate glycation in vivo since it shows different glycation phenotypes and presents specific protein glycation targets. A comparison between in vivo glycated enolase and purified enolase glycated in vitro revealed marked differences. All effects regarding structure and stability changes were enhanced when the protein was glycated in vitro. The same applies to enzyme activity loss, dimer dissociation and unfolding. However, the major difference lies in the nature and location of specific advanced glycation end-products. In vivo, glycation appears to be a specific process, where the same residues are consistently modified in the same way, whereas in vitro several residues are modified with different advanced glycation end-products.
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Pun, Pamela Boon Li, and Michael P. Murphy. "Pathological Significance of Mitochondrial Glycation." International Journal of Cell Biology 2012 (2012): 1–13. http://dx.doi.org/10.1155/2012/843505.
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Glycation, the nonenzymatic glycosylation of biomolecules, is commonly observed in diabetes and ageing. Reactive dicarbonyl species such as methylglyoxal and glyoxal are thought to be major physiological precursors of glycation. Because these dicarbonyls tend to be formed intracellularly, the levels of advanced glycation end products on cellular proteins are higher than on extracellular ones. The formation of glycation adducts within cells can have severe functional consequences such as inhibition of protein activity and promotion of DNA mutations. Although several lines of evidence suggest that there are specific mitochondrial targets of glycation, and mitochondrial dysfunction itself has been implicated in disease and ageing, it is unclear if glycation of biomolecules specifically within mitochondria induces dysfunction and contributes to disease pathology. We discuss here the possibility that mitochondrial glycation contributes to disease, focussing on diabetes, ageing, cancer, and neurodegeneration, and highlight the current limitations in our understanding of the pathological significance of mitochondrial glycation.
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Dalbanjan, N. P., A. J. Kadapure, P. Huded, V. B. Chachadi, S. Nayaka, and Praveen Kumar S.K. "Assessing the in vitro anti-glycation efficacy of vitamins A, C, D, E." Ukrainian Biochemical Journal 94, no. 4 (November 10, 2022): 61–66. http://dx.doi.org/10.15407/ubj94.04.061.
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Accreted sugars in the blood react with protein’s amino group via Schiff base to form Amadori compounds. Further, these compounds execute irreversible chemical modifications generating advanced glycation end products (AGEs). The current study investigated the effects of vitamins in a glycation-prone in vitro environment. Glycation model was reached by incubating BSA with 0.1 M glucose/fructose in 0.1 M phosphate-buffered saline. Intrinsic (tyrosine/tryptophan) and AGEs fluorescence was monitored with fluorescence spectrophotometer. Ellman’s test depicted that native BSA contains more free thiol groups than glycated BSA. It was shown that BSA is more susceptible to glycation in the presence of fructose than glucose, and vitamin D followed by vitamin E and A can significantly rescue the BSA from glycation progression. Keywords: advanced glycation end products, anti-glycation, BSA, Ellman’s test, fluorescence, vitamins
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Bakunina, Natalya Sergeyevna, Ruslan Ivanovich Glushakov, Natalya Igorevna Tapilskaya, and Petr Dmitriyevich Shabanov. "Pharmacology of polyprenols as adaptogens reducing glycation processes." Reviews on Clinical Pharmacology and Drug Therapy 11, no. 4 (December 15, 2013): 44–53. http://dx.doi.org/10.17816/rcf11444-53.
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Nowadays a significant attention is currently given to the process of glycation which plays an important role in the pathogenesis of vascular complications of diabetes and different neurodegenerative diseases. As a result of inconvertible transformation of early glycation products, stable compounds with different structure are produced - advanced glycation end-products (AGE), which have special patterns leading to pathological development. There are specific receptors of AGE which include phagocyte receptor, RAGE-receptor for advanced glycation end products, and galectin-3. It is necessary to find methods for prevention of development negative processes induced by glycation. It can be administration of glycation inhibitors or the use of compounds, leading to reduction of the level of glycation products, as well as intensification of metabolic processes, which also promotes reduction of glycation. It can also be inhibition of interlocking with receptor and/or post-receptor signaling pathways, which can theoretically reduce the risk of negative phenomena, induced by glycation products. Polyprenols are biologically highly functional active compounds taking part in the process of polysaccharides, glycoproteins, peptidoglycanes and carbohydrate-containing biopolymers biosynthesis. Polyprenols are perspective drugs that can be applied in various fields of experimental and clinical medicine.
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Federico, Giovanni, Martina Gori, Emioli Randazzo, and Francesco Vierucci. "Skin advanced glycation end-products evaluation in infants according to the type of feeding and mother’s smoking habits." SAGE Open Medicine 4 (January 1, 2016): 205031211668212. http://dx.doi.org/10.1177/2050312116682126.
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Objectives: This study was conducted to assess whether formula-fed infants had increased skin advanced glycation end-products compared with breastfed ones. We also evaluated the effect of maternal smoke during pregnancy and lactation on infant skin advanced glycation end-products accumulation. Methods: Advanced glycation end-product–linked skin autofluorescence was measured in 101 infants. Results: In infants born from non-smoking mothers, advanced glycation end-products were higher in formula-fed subjects than in breastfed subjects (0.80 (0.65–0.90) vs 1.00 (0.85–1.05), p < 0.001). Advanced glycation end-products in breastfed infants from smoking mothers were higher than in those from non-smoking mothers (0.80 (0.65–0.90) vs 1.00 (0.90–1.17), p = 0.009). Conclusion: Formula-fed infants had increased amounts of advanced glycation end-products compared with the breastfed ones, confirming that breast milk represents the best food for infants. Breastfed infants from mothers smoking during pregnancy and lactation had increased skin advanced glycation end-products, suggesting that smoke-related advanced glycation end-products transfer throughout breast milk. Moreover, advanced glycation end-products may already increase during gestation, possibly affecting fetal development. Thus, we reinforced that smoking must be stopped during pregnancy and lactation.
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Austin, G. E., R. H. Mullins, and L. G. Morin. "Non-enzymic glycation of individual plasma proteins in normoglycemic and hyperglycemic patients." Clinical Chemistry 33, no. 12 (December 1, 1987): 2220–24. http://dx.doi.org/10.1093/clinchem/33.12.2220.
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Abstract Diabetic patients in poor glycemic control show increased glycation of total plasma proteins, but little is yet known about the relative extents to which the various individual proteins are glycated. Thus, we studied the non-enzymic glycation of several major plasma proteins and plasma protein fractions in normal and diabetic patients. In vivo glycation for most plasma proteins was very low in non-diabetic patients, only gamma globulin showing more than 5% glycation. In diabetic plasmas, glycation was much greater, immunoglobulins again showing the greatest proportion, followed in descending order by albumin, complement C3, fibrinogen, transferrin, haptoglobin, and alpha-1-antitrypsin. When plasma proteins were glycated in vitro, this order was IgG greater than complement C3 greater than albumin greater than transferrin greater than haptoglobin greater than alpha-1-antitrypsin. In general, proteins with the longest biological half-lives, such as IgG and albumin, showed the greatest in vivo glycation. On the other hand, proteins with high intrinsic glycability, such as complement C3, showed moderate glycation, despite a short half-life. Except for albumin, more basic proteins showed greater glycation than acidic proteins, but there was poor correlation between mole percent lysine and glycation. Evidently the relative extents of glycation of different plasma proteins are a complex function of integrated glucose concentrations over time and of the half-life and chemical characteristics of each protein.
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Kennedy, D. M., A. W. Skillen, and C. H. Self. "Colorimetric assay of glycoprotein glycation free of interference from glycosylation residues." Clinical Chemistry 39, no. 11 (November 1, 1993): 2309–11. http://dx.doi.org/10.1093/clinchem/39.11.2309.
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Abstract We have developed a colorimetric assay for determining the degree of glycation of serum proteins that is unaffected by glycosylation residues. This was accomplished by reducing the proteins with sodium borohydride prior to periodate oxidation. Previous periodate-based methods, which offer several advantages over other glycation assays, cannot determine glycoprotein glycation because interference from sialic residues in the glycan chain can lead to overestimation of the amount of glycation products. Without reduction, glycation of fetuin was double that of asialofetuin glycated under identical conditions. We found that borohydride reduction before periodate oxidation increases the amount of formaldehyde released in proportion to the extent of glycation, irrespective of the degree of glycosylation. Using two glycoproteins and an unglycosylated protein, we showed how measurement of the formaldehyde increase enables the extent of glycoprotein glycation to be determined without removal of interfering sugars.
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Jagadeeshaprasad, Mashanipalya G., Vinashya Venkatasubramani, Ambika G. Unnikrishnan, and Mahesh J. Kulkarni. "Albumin Abundance and Its Glycation Status Determine Hemoglobin Glycation." ACS Omega 3, no. 10 (October 10, 2018): 12999–3008. http://dx.doi.org/10.1021/acsomega.8b01702.
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Miyazawa, Teruo, Kiyotaka Nakagawa, Satoko Shimasaki, and Ryoji Nagai. "Lipid glycation and protein glycation in diabetes and atherosclerosis." Amino Acids 42, no. 4 (October 19, 2010): 1163–70. http://dx.doi.org/10.1007/s00726-010-0772-3.
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Perera, HKI, and DCR Wijetunge. "A novel in vitro method to detect inhibitors of protein glycation." Asian Journal of Medical Sciences 5, no. 3 (February 24, 2014): 15–21. http://dx.doi.org/10.3126/ajms.v5i3.8670.
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Background: Protein glycation generates advanced glycation end products (AGEs) which are implicated in the pathogenesis of chronic complications associated with diabetes. Identifi cation of medicinal plants with protein glycation inhibitory potential will enhance the opportunity to delay or inhibit diabetic complications with minimum side effects. Techniques available to identify protein glycation inhibitors require expensive specialized equipment. Objective: Objective of this study was to develop a relatively simple in vitro method to identify the protein glycation inhibitory potential of compounds or medicinal plants. Methods: Bovine serum albumin (BSA) was incubated with different concentrations of glucose or fructose or ribose for 31 days at pH 7.4. Standard inhibitor aminoguanidine (AG) was used as a positive control. Effect on the BSA migration under different experimental conditions was compared using polyacrylamide gel electrophoresis under native conditions (PAGE). Murraya koenigii leaf extract was analyzed for its effect on protein glycation. Results: We demonstrated many aspects of protein glycation including the effect of sugar concentration, type of the sugar and incubation period on protein glycation using this comparatively simpler method, which was previously, demonstrated using more sophisticated and expensive equipment. Migration of the BSA band towards the anode was proportionate to the degree of protein glycation. Further, we were innovative in demonstrating the inhibitory effect of AG on protein glycation using PAGE. BSA migration was comparatively slower when AG was included in the presence of sugar, indicating its inhibitory effects. We also revealed the protein glycation inhibitory potential of Murraya koenigii leaf extract, which was greater than that of AG at the concentrations used in the study. Conclusion: We have developed novel simple in vitro method using PAGE to identify inhibitors of protein glycation. Asian Journal of Medical Science, Volume-5(3) 2014: 15-21 http://dx.doi.org/10.3126/ajms.v5i3.8670
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Furtak, Kh Ye, H. Ya Hachkova, and N. O. Sybirna. "The effect of Galega officinalis L. extract on the content of the advanced glycation end products and their receptors in rat leukocytes under experimental diabetes mellitus." Studia Biologica 15, no. 4 (December 2021): 49–58. http://dx.doi.org/10.30970/sbi.1504.672.
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Background. Diabetes mellitus intensifies non-enzymatic glycosylation (glycation) of biomolecules under conditions of chronic hyperglycemia and facilitates accumulation of advanced glycation end products. Disorders of the cells of various tissues are caused by binding of advanced glycation end products to the corresponding receptors, the level of receptors for advanced glycation end products increases under conditions of hyperglycemia. The interaction between receptors for advanced glycation end products and advanced glycation end products leads to the formation of excessive reactive oxygen species, changes in intracellular signaling, gene expression, increased secretion of pro-inflammatory cytokines and contributes to the development of diabetic complications. The search for factors of natural origin that will slow down the development of specific complications of diabetes, determines the feasibility of studies of the corrective ability of biologically active substances isolated from medicinal plants for the process of glycation of proteins in diabetes. Materials and methods. Experimental diabetes mellitus was induced by intraperitoneal administration of streptozotocin. Separation of blood leukocytes was performed in Ficoll density gradient. To determine the extent of advanced glycation end products and receptor for advanced glycation end products in leukocyte immunoperoxidase labeling was performed. Results. A decrease in the content of advanced glycation end products in leukocytes under conditions of experimental diabetes mellitus was found. The obtained data indicate a possible contravention of glucose uptake by leukocytes in the studied pathology. At the same time, an increase in exposure to the receptor for advanced glycation end products leukocyte membranes in response to chronic hyperglycemia has been demonstrated. The ability of alkaloid free fraction of Galega officinalis extract to reduce the content of receptors for end products of glycation on the membranes of immunocompetent cells in diabetic animals has been confirmed, which may be due to the presence of biologically active substances with hypoglycemic action in its composition. Conclusion. Corrective effect of alkaloid free fraction of Galega officinalis L. extract on the content of receptor for advanced glycation end products in diabetes mellitus is mediated by its normalizing effect on carbohydrate metabolism.
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Kalant, N., S. McCormick, and M. A. Parniak. "Non-enzymic glycation of collagen inhibits binding of oxidized low-density lipoprotein." Biochemical Journal 293, no. 3 (August 1, 1993): 661–66. http://dx.doi.org/10.1042/bj2930661.
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We have examined the effect of non-enzymic glycation of native soluble collagen, in solution or in gels, on binding of oxidized low-density lipoprotein (LDL). We found the following. (1) Glycation markedly inhibited binding of LDL. This is contrary to results previously reported; the difference may be attributable to the use of detergent- and heat-denatured collagen, covalently bound to agarose beads, in the earlier study. (2) With increased duration of glycation, collagen solution would not gel, and preformed gels dissolved. (3) [14C]Glucose bound to collagen gels dissociated slowly, even at pH 5, suggesting that it was not present as a Schiff's base; in addition, ketoamines, pentosidine and fluorescent advanced glycation products were not detectable in glycated collagen gels, although they accumulated in tendon collagen glycated under the same conditions. It is hypothesized that the difference in glycation effects between gel and tendon may be due to the strength of cross-linking before glycation: the increase in intermolecular distance in collagen fibrils which results from glycation disrupts the fibrils in gels, preventing binding of LDL and formation of glycation-dependent cross-links, whereas the extensive cross-linking in tendon maintains the intermolecular distances within a range which permits formation of glycation cross-links.
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Liu, Yan, Wenxiang Gu, Wenyi Zhang, and Jianan Wang. "Predict and Analyze Protein Glycation Sites with the mRMR and IFS Methods." BioMed Research International 2015 (2015): 1–6. http://dx.doi.org/10.1155/2015/561547.
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Glycation is a nonenzymatic process in which proteins react with reducing sugar molecules. The identification of glycation sites in protein may provide guidelines to understand the biological function of protein glycation. In this study, we developed a computational method to predict protein glycation sites by using the support vector machine classifier. The experimental results showed that the prediction accuracy was 85.51% and an overall MCC was 0.70. Feature analysis indicated that the composition ofk-spaced amino acid pairs feature contributed the most for glycation sites prediction.
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Yan, Yingfei, Daniel Hemmler, and Philippe Schmitt-Kopplin. "HILIC-MS for Untargeted Profiling of the Free Glycation Product Diversity." Metabolites 12, no. 12 (November 25, 2022): 1179. http://dx.doi.org/10.3390/metabo12121179.
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Glycation products produced by the non-enzymatic reaction between reducing carbohydrates and amino compounds have received increasing attention in both food- and health-related research. Although liquid chromatography mass spectrometry (LC-MS) methods for analyzing glycation products already exist, only a few common advanced glycation end products (AGEs) are usually covered by quantitative methods. Untargeted methods for comprehensively analyzing glycation products are still lacking. The aim of this study was to establish a method for simultaneously characterizing a wide range of free glycation products using the untargeted metabolomics approach. In this study, Maillard model systems consisting of a multitude of heterogeneous free glycation products were chosen for systematic method optimization, rather than using a limited number of standard compounds. Three types of hydrophilic interaction liquid chromatography (HILIC) columns (zwitterionic, bare silica, and amide) were tested due to their good retention for polar compounds. The zwitterionic columns showed better performance than the other two types of columns in terms of the detected feature numbers and detected free glycation products. Two zwitterionic columns were selected for further mobile phase optimization. For both columns, the neutral mobile phase provided better peak separation, whereas the acidic condition provided a higher quality of chromatographic peak shapes. The ZIC-cHILIC column operating under acidic conditions offered the best potential to discover glycation products in terms of providing good peak shapes and maintaining comparable compound coverage. Finally, the optimized HILIC-MS method can detect 70% of free glycation product features despite interference from the complex endogenous metabolites from biological matrices, which showed great application potential for glycation research and can help discover new biologically important glycation products.
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Rabbani, Naila, and Paul J. Thornalley. "Dicarbonyl proteome and genome damage in metabolic and vascular disease." Biochemical Society Transactions 42, no. 2 (March 20, 2014): 425–32. http://dx.doi.org/10.1042/bst20140018.
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Methylglyoxal is a potent protein-glycating agent. It is an arginine-directed glycating agent and often modifies functionally important sites in proteins. Glycation forms mainly MG-H1 [Nδ-(5-hydro-5-methyl-4-imidazolon-2-yl)ornithine] residues. MG-H1 content of proteins is quantified by stable isotopic dilution analysis–MS/MS and also by immunoblotting with specific monoclonal antibodies. Methylglyoxal-modified proteins undergo cellular proteolysis and release MG-H1 free adduct for excretion. MG-H1 residues have been found in proteins of animals, plants, bacteria, fungi and protoctista. MG-H1 is often the major advanced glycation end-product in proteins of tissues and body fluids, increasing in diabetes and associated vascular complications, renal failure, cirrhosis, Alzheimer's disease, arthritis, Parkinson's disease and aging. Proteins susceptible to methylglyoxal modification with related functional impairment are called the DCP (dicarbonyl proteome). The DCP includes albumin, haemoglobin, transcription factors, mitochondrial proteins, extracellular matrix proteins, lens crystallins and others. DCP component proteins are linked to mitochondrial dysfunction in diabetes and aging, oxidative stress, dyslipidaemia, cell detachment and anoikis and apoptosis. Methylglyoxal also modifies DNA where deoxyguanosine residues are modified to imidazopurinone MGdG {3-(2′-deoxyribosyl)-6,7-dihydro-6,7-dihydroxy-6/7-methylimidazo-[2,3-b]purine-9(8)one} isomers. MGdG was the major quantitative adduct detected in vivo. It was linked to frequency of DNA strand breaks and increased markedly during apoptosis induced by a cell-permeant glyoxalase I inhibitor. Glyoxalase I metabolizes >99% methylglyoxal and thereby protects the proteome and genome. Gene deletion of GLO1 is embryonically lethal and GLO1 silencing increases methylglyoxal concentration, MG-H1 and MGdG, premature aging and disease. Studies of methylglyoxal glycation have importance for human health, longevity and treatment of disease.
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Liu, Jing-Jing, Yong You, Shu-Qin Gao, Shuai Tang, Lei Chen, Ge-Bo Wen, and Ying-Wu Lin. "Identification of the Protein Glycation Sites in Human Myoglobin as Rapidly Induced by d-Ribose." Molecules 26, no. 19 (September 26, 2021): 5829. http://dx.doi.org/10.3390/molecules26195829.
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Protein glycation is an important protein post-translational modification and is one of the main pathogenesis of diabetic angiopathy. Other than glycated hemoglobin, the protein glycation of other globins such as myoglobin (Mb) is less studied. The protein glycation of human Mb with ribose has not been reported, and the glycation sites in the Mb remain unknown. This article reports that d-ribose undergoes rapid protein glycation of human myoglobin (HMb) at lysine residues (K34, K87, K56, and K147) on the protein surface, as identified by ultra-high performance liquid chromatography-mass spectrometry (UHPLC-MS) and electrospray ionization tandem mass spectrometry (ESI-MS/MS). Moreover, glycation by d-ribose at these sites slightly decreased the rate of the met heme (FeIII) in reaction with H2O2 to form a ferryl heme (FeIV=O). This study provides valuable insight into the protein glycation by d-ribose and provides a foundation for studying the structure and function of glycated heme proteins.
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Durge, Ankita, Isha Sharma, and Rashmi Santosh Tupe. "Glycation-Associated Diabetic Nephropathy and the Role of Long Noncoding RNAs." Biomedicines 10, no. 10 (October 19, 2022): 2623. http://dx.doi.org/10.3390/biomedicines10102623.
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The glycation of various biomolecules is the root cause of many pathological conditions associated with diabetic nephropathy and end-stage kidney disease. Glycation imbalances metabolism and increases renal cell injury. Numerous therapeutic measures have narrowed down the adverse effects of endogenous glycation, but efficient and potent measures are miles away. Recent advances in the identification and characterization of noncoding RNAs, especially the long noncoding RNAs (lncRNAs), have opened a mammon of new biology to explore the mitigations for glycation-associated diabetic nephropathy. Furthermore, tissue-specific distribution and condition-specific expression make lncRNA a promising key for second-generation therapeutic interventions. Though the techniques to identify and exemplify noncoding RNAs are rapidly evolving, the lncRNA study encounters multiple methodological constraints. This review will discuss lncRNAs and their possible involvement in glycation and advanced glycation end products (AGEs) signaling pathways. We further highlight the possible approaches for lncRNA-based therapeutics and their working mechanism for perturbing glycation and conclude our review with lncRNAs biology-related future opportunities.
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Tupe, Rashmi Santosh, and Vaishali Vilas Agte. "Role of zinc along with ascorbic acid and folic acid during long-term in vitro albumin glycation." British Journal of Nutrition 103, no. 3 (October 23, 2009): 370–77. http://dx.doi.org/10.1017/s0007114509991929.
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The present study aimed to investigate the role of Zn alone and in the presence of ascorbic acid (AA) and folic acid (FA) in albumin glycation. Glycation was performed by incubations of bovine serum albumin with glucose at 37°C along with Zn, AA or FA separately and Zn+AA or Zn+FA for 150 d. Glycation-mediated modifications were monitored as fluorescence of advanced glycation endproducts, carbonyl formation, β aggregation (thioflavin T and Congo red dyes), albumin-bound Zn, thiol groups and glycated aggregate's toxicity in HepG2 cells. Zn inhibited glycation and β aggregation, probably due to observed higher protein-bound Zn. It also protected protein thiols and increased cell survival. AA and FA enhanced glycation, which was lowered in Zn-co-incubated samples. FA increased albumin-bound Zn and showed maximum cell survival. Although these results warrant further in vivo investigation, the present data help in the understanding of the interplay of Zn with micronutrients in albumin glycation.
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Lin, Shih-Wei, Chi-Hao Wu, Ya-Chien Jao, You-Shan Tsai, Yen-Lien Chen, Chin-Chu Chen, Tony J. Fang, and Chi-Fai Chau. "Fermented Supernatants of Lactobacillus plantarum GKM3 and Bifidobacterium lactis GKK2 Protect against Protein Glycation and Inhibit Glycated Protein Ligation." Nutrients 15, no. 2 (January 5, 2023): 277. http://dx.doi.org/10.3390/nu15020277.
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With age, protein glycation in organisms increases continuously. Evidence from many studies shows that the accumulation of glycated protein is highly correlated with biological aging and the development of aging-related diseases, so developing a dietary agent to attenuate protein glycation is very meaningful. Previous studies have indicated that lactic acid bacteria-fermented products have diverse biological activities especially in anti-aging, so this study was aimed to investigate the inhibitory effect of the fermented supernatants of Lactobacillus plantarum GKM3 (GKM3) and Bifidobacterium lactis GKK2 (GKK2) on protein glycation. The results show that GKM3- and GKK2-fermented supernatants can significantly inhibit protein glycation by capturing a glycation agent (methylglyoxal) and/or protecting functional groups in protein against methylglyoxal-induced responses. GKM3- and GKK2-fermented supernatants can also significantly inhibit the binding of glycated proteins to the receptor for advanced glycation end products (RAGE). In conclusion, lactic acid bacteria fermentation products have the potential to attenuate biological aging by inhibiting protein glycation.
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De Caro, Liberato, Alberta Terzi, Luca Fusaro, Davide Altamura, Francesca Boccafoschi, Oliver Bunk, and Cinzia Giannini. "Time scale of glycation in collagen of bovine pericardium-derived bio-tissues." IUCrJ 8, no. 6 (October 28, 2021): 1024–34. http://dx.doi.org/10.1107/s2052252521010344.
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Glycosylation is the process of combining one or more glucose molecules (or other monosaccharides) with molecules of a different nature (which are therefore glycosylated). In biochemistry, glycosylation is catalyzed by several specific enzymes, and assumes considerable importance since it occurs mainly at the expense of proteins and phospholipids which are thus transformed into glycoproteins and glycolipids. Conversely, in diabetes and aging, glycation of proteins is a phenomenon of non-enzymatic nature and thus not easily controlled. Glycation of collagen distorts its structure, renders the extracellular matrix stiff and brittle and at the same time lowers the degradation susceptibility thereby preventing renewal. Based on models detailed in this paper and with parameters determined from experimental data, we describe the glycation of type 1 collagen in bovine pericardium derived bio-tissues, upon incubation in glucose and ribose. With arginine and lysine/hydroxylysine amino acids as the primary sites of glycation and assuming that the topological polar surface area of the sugar molecules determines the glycation rates, we modelled the glycation as a function of time and determined the glycation rate and thus the progression of glycation as well as the resulting volume increase.
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Vlassopoulos, Antonis, Michael E. J. Lean, and Emilie Combet. "Oxidative stress, protein glycation and nutrition – interactions relevant to health and disease throughout the lifecycle." Proceedings of the Nutrition Society 73, no. 3 (May 30, 2014): 430–38. http://dx.doi.org/10.1017/s0029665114000603.
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Protein glycation has been studied for over a century now and plays an important role in disease pathogenesis throughout the lifecycle. Strongly related to diabetic complications, glycation of Hb has become the gold standard method for diabetes diagnosis and monitoring. It is however attracting attention in normoglycaemia as well lately. Longitudinal studies increasingly suggest a positive relationship between glycation and the risk of chronic diseases in normoglycaemic individuals, but the mechanisms behind this association remain unclear. The interaction between glycation and oxidative stress may be particularly relevant in the normoglycaemic context, as suggested by recent epidemiological and in vitro evidence. In that context nutritional and lifestyle factors with an influence on redox status, such as smoking, fruit and vegetable and antioxidants consumption, may have the capacity to promote or inhibit glycation. However, experimental data from controlled trials are lacking the quality and rigour needed to reach firm conclusions. In the present review, we discuss the importance of glycation for health through the lifecycle and focus on the importance of oxidative stress as a driver for glycation. The importance of nutrition to modulate glycation is discussed, based on the evidence available and recommendations towards higher quality future research are made.
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Anne, B., St J. Dawnayand, and David J. Millar. "Glycation and Advanced Glycation End-Product Formation with Icodextrin and Dextrose." Peritoneal Dialysis International: Journal of the International Society for Peritoneal Dialysis 17, no. 1 (January 1997): 52–58. http://dx.doi.org/10.1177/089686089701700112.
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Objective To review protein glycation and advanced glycation end-product formation with particular reference to its occurrence in the peritoneum following exposure to peritoneal dialysis fluid. Data sources Articles identified through searches on MEDLINE and BIDS and references cited therein. Study selection Studies on the interaction of amino groups with glucose, maltose and glucose polymers. Studies containing evidence of peritoneal advanced glycation end-product formation. Data extraction Studies evaluated as to whether they are in vivo, ex vivo or in vitro under non-physiological or physiological conditions. Results Protein glycation is slower with maltose and glucose polymers than with equimolar glucose. Advanced glycation end-product formation occurs with all three sugars, but to a greater extent after standard heat sterilization of dialysis fluid and to a lesser extent in heat sterilized fluids containing icodextrin rather than glucose. Glucose degradation products significantly contribute to protein-linked advanced glycation end-productlike fluorescence. Histology and immunohistochemistry demonstrate diabetiform changes and advanced glycation end-products in the peritoneal membrane following exposure to glucose-containing peritoneal dialysis fluids. Their presence is likely to be detrimental to peritoneal function and may contribute to loss of ultrafiltration. Conclusions Advanced glycation end-product formation is lower but still significant with heat sterilized peritoneal dialysis fluid containing icodextrin than with glucose. More research is needed to investigate the interaction of glucose degradation products and glucose polymers with proteins and the possible consequences of advanced glycation end-product formation on peritoneal function.
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Sawabe, Akiyoshi, Atsuyuki Yamashita, Mei Fujimatsu, and Ryuji Takeda. "Development of Evaluation Methods for Anti-Glycation Activity and Functional Ingredients Contained in Coriander and Fennel Seeds." Processes 10, no. 5 (May 14, 2022): 982. http://dx.doi.org/10.3390/pr10050982.
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Spices are known to have various physiological functions. We focused on the anti-glycation effects of spices, researched anti-glycation active ingredients in coriander (Coriandrum sativum L.) and fennel (Foeniculum vulgare) seeds, and conducted experiments using human skin-derived fibroblast TIG-110 cells as a model of glycation. We isolated 11 compounds from two spice seeds and found several substances that showed anti-glycation activity. A new compound (5,5′-diallyl-2,2′-diglucopyranosyl-3,3′-dimethoxy diphenyl ether) was isolated from fennel seeds and showed high anti-glycation activity with an IC50 value of 0.08 mM, thereby indicating a high anti-glycosylation activity. In this study, we established a glyoxal (GO)-induced glycation test method for human skin cells, confirmed the anti-glycation effect of spice seeds using this glycation induction model, and found that the exposure of TIG-110 human skin-derived fibroblast cells to GO reduced cell viability. The most stable conditions for cell viability were found to be a GO concentration of 1.25 mM and a culture time of 48 h. We evaluated extracts and isolates of spice seeds using this model as a model test for glycation induction. We conducted qualitative and quantitative analyses of carboxymethyl lysine (CML), a type of AGE, to determine the relationship between cell viability and AGEs. The relationship between cell viability and the amount of CML was correlated. Establishing a glycation induction model test using skin cells makes it possible to quickly screen extracts of natural ingredients in the future. Moreover, the results of this model showed that extracts of two spice seeds and their isolates have high anti-glycation activity, and they are expected to be used as cosmetics, health foods, and pharmaceutical ingredients.