Journal articles: 'Advanced glycation endproducts (AGE)'

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Zhang, Xinchen, Shuting Hu, Feng Chen, and Mingfu Wang. "Treatment of proteins with dietary polyphenols lowers the formation of AGEs and AGE-induced toxicity." Food Funct. 5, no. 10 (2014): 2656–61. http://dx.doi.org/10.1039/c4fo00244j.

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Frank, Franziska, Veronika Bezold, Kaya Bork, Philip Rosenstock, Jonas Scheffler, and Rüdiger Horstkorte. "Advanced glycation endproducts and polysialylation affect the turnover of the neural cell adhesion molecule (NCAM) and the receptor for advanced glycation endproducts (RAGE)." Biological Chemistry 400, no. 2 (January 28, 2019): 219–26. http://dx.doi.org/10.1515/hsz-2018-0291.

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Abstract The balance between protein synthesis and degradation regulates the amount of expressed proteins. This protein turnover is usually quantified as the protein half-life time. Several studies suggest that protein degradation decreases with age and leads to increased deposits of damaged and non-functional proteins. Glycation is an age-dependent, non-enzymatic process leading to posttranslational modifications, so-called advanced glycation endproducts (AGE), which usually damage proteins and lead to protein aggregation. AGE are formed by the Maillard reaction, where carbonyls of carbohydrates or metabolites react with amino groups of proteins. In this study, we quantified the half-life time of two important receptors of the immunoglobulin superfamily, the neural cell adhesion molecule (NCAM) and the receptor for advanced glycation end products (RAGE) before and after glycation. We found, that in two rat PC12 cell lines glycation leads to increased turnover, meaning that glycated, AGE-modified proteins are degraded faster than non-glycated proteins. NCAM is the most prominent carrier of a unique enzymatic posttranslational modification, the polysialylation. Using two PC12 cell lines (a non-polysialylated and a polysialylated one), we could additionally demonstrate, that polysialylation of NCAM has an impact on its turnover and that it significantly increases its half-life time.

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Quintero, David G., Julia N. Winger, Rania Khashaba, and James L. Borke. "Advanced Glycation Endproducts and Rat Dental Implant Osseointegration." Journal of Oral Implantology 36, no. 2 (April 1, 2010): 97–103. http://dx.doi.org/10.1563/aaid-joi-d-09-00032.

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Abstract Advanced glycation endproducts (AGEs) are a diverse group of molecular adducts formed in environments high in reducing sugars that accumulate with aging and in diabetes. This study tests the hypothesis that AGEs inhibit the stabile osseointegration of dental implants through tissue interactions that interfere with bone turnover and compromise the biomechanical properties at the bone-implant interface. Maxillary first molars were extracted from 32 rats and allowed to heal for 4 weeks. Titanium implants (1 mm × 3 mm) were placed in the healed sockets of 2 groups of 16 rats consisting of 8 rats injected 3 times/wk for 1 month with AGE (prepared from glucose and lysine) and 8 rats injected with vehicle as a control. AGE injections continued for an additional 14 or 28 days before sacrifice. X-ray images, blood, and tissues were collected to examine bone/implant contact ratio, serum pyridinoline ([PYD] a collagen breakdown marker), osteocalcin ([OSC] a bone formation marker), and for immunohistochemistry with antibodies to AGE and the bone turnover-marker protein matrix metalloproteinase1. Compared with the AGE-treated groups, the controls showed significantly higher bone/implant contact at both 14- and 28-day time points. PYD (P < .05) and OSC (trend) levels from controls showed decreases at 28 days when compared with AGE-treated groups. Immunohistochemistry with AGE-specific and bone turnover marker antibodies showed stronger staining associated with the implant/tissue interface in AGE-treated rats. Our studies indicate an association between AGE and inhibition of bone turnover, suggesting that the formation of AGE in high glycemic conditions, such as diabetes, may contribute to a slower rate of osseointegration that negatively affects implant stability.

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Snelson, Matthew, Elisa Lucut, and Melinda T. Coughlan. "The Role of AGE-RAGE Signalling as a Modulator of Gut Permeability in Diabetes." International Journal of Molecular Sciences 23, no. 3 (February 3, 2022): 1766. http://dx.doi.org/10.3390/ijms23031766.

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There is increasing evidence for the role of intestinal permeability as a contributing factor in the pathogenesis of diabetes; however, the molecular mechanisms are poorly understood. Advanced glycation endproducts, of both exogenous and endogenous origin, have been shown to play a role in diabetes pathophysiology, in part by their ligation to the receptor for advanced glycation endproducts (RAGE), leading to a proinflammatory signalling cascade. RAGE signalling has been demonstrated to play a role in the development of intestinal inflammation and permeability in Crohn’s disease and ulcerative colitis. In this review, we explore the role of AGE-RAGE signalling and intestinal permeability and explore whether activation of RAGE on the intestinal epithelium may be a downstream event contributing to the pathogenesis of diabetes complications.

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Ohgami, Nobutaka, Ryoji Nagai, Mamoru Ikemoto, Hiroyuki Arai, Akira Miyazaki, Hideki Hakamata, Seikoh Horiuchi, and Hitoshi Nakayama. "CD36, serves as a receptor for advanced glycation endproducts (AGE)." Journal of Diabetes and its Complications 16, no. 1 (January 2002): 56–59. http://dx.doi.org/10.1016/s1056-8727(01)00208-2.

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van der Lugt, Timme, Antje R. Weseler, Misha F. Vrolijk, Antoon Opperhuizen, and Aalt Bast. "Dietary Advanced Glycation Endproducts Decrease Glucocorticoid Sensitivity In Vitro." Nutrients 12, no. 2 (February 10, 2020): 441. http://dx.doi.org/10.3390/nu12020441.

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Glucocorticoids are very effective anti-inflammatory drugs and widely used for inflammatory bowel disease (IBD) patients. However, approximately 20% of IBD patients do not respond to glucocorticoids and the reason for this is largely unknown. Dietary advanced glycation endproducts (AGEs) are formed via the Maillard reaction during the thermal processing of food products and can induce a pro-inflammatory reaction in human cells. To investigate whether this pro-inflammatory response could be mitigated by glucocorticoids, human macrophage-like cells were exposed to both LPS and AGEs to induce interleukin-8 (IL8) secretion. This pro-inflammatory response was then modulated by adding pharmacological compounds interfering in different steps of the anti-inflammatory mechanism of glucocorticoids: rapamycin, quercetin, and theophylline. Additionally, intracellular reactive oxygen species (ROS) were measured and the glucocorticoid receptor phosphorylation state was assessed. The results show that AGEs induced glucocorticoid resistance, which could be mitigated by quercetin and rapamycin. No change in the phosphorylation state of the glucocorticoid receptor was observed. Additionally, intracellular ROS formation was induced by AGEs, which was mitigated by quercetin. This suggests that AGE-induced ROS is an underlying mechanism to AGE-induced glucocorticoid resistance. This study shows for the first time the phenomenon of dietary AGE-induced glucocorticoid resistance due to the formation of ROS. Our findings indicate that food products with a high inflammatory potential can induce glucocorticoid resistance; these results may be of great importance to IBD patients suffering from glucocorticoid resistance.

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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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Brenner, Thorsten, Thomas H. Fleming, David Spranz, Peter Schemmer, Thomas Bruckner, Florian Uhle, Eike O. Martin, Markus A. Weigand, and Stefan Hofer. "Reactive Metabolites and AGE-RAGE-Mediated Inflammation in Patients following Liver Transplantation." Mediators of Inflammation 2013 (2013): 1–10. http://dx.doi.org/10.1155/2013/501430.

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Recent investigations have indicated that reactive metabolites and AGE-RAGE-mediated inflammation might play an important role in the pathogenesis of ischemia-reperfusion injury in liver transplantation. In this observational clinical study, 150 patients were enrolled following liver transplantation from deceased donors. The occurrence of short-term complications within 10 days of transplantation was documented. Blood samples were collected prior to transplantation, immediately after transplantation, and at consecutive time points, for a total of seven days after transplantation. Plasma levels of methylglyoxal were determined using HPLC, whereas plasma levels of L-arginine, asymmetric dimethylarginine, advanced glycation endproducts-carboxylmethyllysine, soluble receptor for advanced glycation endproducts, and total antioxidant capacity were measured by ELISA. Patients following liver transplantation were shown to suffer from increased RAGE-associated inflammation with an AGE load mainly dependent upon reactive carbonyl species-derived AGEs. In contrast, carboxylmethyllysine-derived AGEs were of a minor importance. As assessed by the ratio of L-arginine/asymmetric dimethylarginine, the bioavailability of nitric oxide was shown to be reduced in hepatic IRI, especially in those patients suffering from perfusion disorders following liver transplantation. For the early identification of patients at high risk of perfusion disorders, the implementation of asymmetric dimethylarginine measurements in routine diagnostics following liver transplantation from deceased donors should be taken into consideration.

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Schnaider Beeri, Michal, Helen Vlassara, Mary Sano, Jaime Uribarri, James Schmeidler, Sylvan Wallenstein, Weijing Cai, et al. "Serum Advanced Glycation Endproducts (AGE) Correlate With Cognition in the Very Elderly." Alzheimer Disease & Associated Disorders 20, Supplement 2 (July 2006): S100. http://dx.doi.org/10.1097/00002093-200607001-00016.

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Akasaka, Naruse, Sado, Uchiyama, Makino, Yamauchi, Ota, et al. "Involvement of Receptor for Advanced Glycation Endproducts in Hypertensive Disorders of Pregnancy." International Journal of Molecular Sciences 20, no. 21 (November 1, 2019): 5462. http://dx.doi.org/10.3390/ijms20215462.

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Preeclampsia/hypertensive disorders of pregnancy (PE/HDP) is a serious and potentially life-threatening disease. Recently, PE/HDP has been considered to cause adipose tissue inflammation, but the detailed mechanism remains unknown. We exposed human primary cultured adipocytes with serum from PE/HDP and healthy controls for 24 h, and analyzed mRNA expression of several adipokines, cytokines, and ligands of the receptor for advanced glycation endproducts (RAGE). We found that the mRNA levels of interleukin-6 (IL-6), C-C motif chemokine ligand 2 (CCL2), high mobility group box 1 (HMGB1), and RAGE were significantly increased by the addition of PE/HDP serum. Among RAGE ligands, advanced glycation endproducts (AGE) and HMGB1 increased mRNA levels of IL-6 and CCL2 in SW872 human adipocytes and mouse 3T3-L1 cells. The introduction of small interfering RNA for RAGE (siRAGE) into SW872 cells abolished the AGE- and HMGB1-induced up-regulation of IL-6 and CCL2. In addition, lipopolysaccharide (LPS), a ligand of RAGE, increased the expression of IL-6 and CCL2 and siRAGE attenuated the LPS-induced expression of IL-6 and CCL2. These results strongly suggest that the elevated AGE, HMGB1, and LPS in pregnant women up-regulate the expression of IL-6 and CCL2 via the RAGE system, leading to systemic inflammation such as PE/HDP.

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Park, Chan Hum, Takashi Tanaka, Hyun Young Kim, Jong Cheol Park, and Takako Yokozawa. "Protective Effects of Corni Fructus against Advanced Glycation Endproducts and Radical Scavenging." Evidence-Based Complementary and Alternative Medicine 2012 (2012): 1–7. http://dx.doi.org/10.1155/2012/418953.

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We investigated the inhibition of advanced glycation endproduct (AGE) activity using the fluorescence characteristics of fractions and compounds from Corni Fructus. Corni Fructus extract and its iridoid glycoside components showed low inhibitory activities as well as the AGE inhibitor aminoguanidine. However, a low molecular weight polyphenol, 7-O-galloyl-D-sedoheptulose, and an antioxidant, trolox, showed high inhibitory activities compared with aminoguanidine under reactive conditions. The AGE-inhibiting activity of polyphenolic fractions of Corni Fructus ranged from a level comparable to Corni Fructus extract to the higher level of 7-O-galloyl-D-sedoheptulose. As well as the results of AGE-inhibiting activity, Corni Fructus extract and iridoid components showed low or no 1,1-diphenyl-2-pycrylhydrazyl (DPPH) radical-scavenging activities, whereas 7-O-galloyl-D-sedoheptulose showed a level comparable to trolox. Polyphenolic fractions of Corni Fructus quenched DPPH radicals in a concentration-dependent manner. Some fractions exerted a higher DPPH radical-scavenging activity compared with trolox and 7-O-galloyl-D-sedoheptulose. The DPPH radical-scavenging activity was significantly correlated with the AGE-inhibiting activity. These results suggest that polyphenolic fractions of Corni Fructus inhibited AGE formation by antioxidant activity including free radical scavenging. The strong DPPH radical-scavenging and AGE-inhibiting fractions included ellagitannins and polymeric proanthocyanidins.

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van der Lugt, Timme, Antje Weseler, Wouter Gebbink, Misha Vrolijk, Antoon Opperhuizen, and Aalt Bast. "Dietary Advanced Glycation Endproducts Induce an Inflammatory Response in Human Macrophages in Vitro." Nutrients 10, no. 12 (December 2, 2018): 1868. http://dx.doi.org/10.3390/nu10121868.

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Advanced glycation endproducts (AGEs) can be found in protein- and sugar-rich food products processed at high temperatures, which make up a vast amount of the Western diet. The effect of AGE-rich food products on human health is not yet clear and controversy still exists due to possible contamination of samples with endotoxin and the use of endogenous formed AGEs. AGEs occur in food products, both as protein-bound and individual molecules. Which form exactly induces a pro-inflammatory effect is also unknown. In this study, we exposed human macrophage-like cells to dietary AGEs, both in a protein matrix and individual AGEs. It was ensured that all samples did not contain endotoxin concentrations > 0.06 EU/mL. The dietary AGEs induced TNF-alpha secretion of human macrophage-like cells. This effect was decreased by the addition of N(ε)-carboxymethyllysine (CML)-antibodies or a receptor for advanced glycation endproducts (RAGE) antagonist. None of the individual AGEs induce any TNF-alpha, indicating that AGEs should be bound to proteins to exert an inflammatory reaction. These findings show that dietary AGEs directly stimulate the inflammatory response of human innate immune cells and help us define the risk of regular consumption of AGE-rich food products on human health.

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Cepas, Vanesa, Massimo Collino, Juan C. Mayo, and Rosa M. Sainz. "Redox Signaling and Advanced Glycation Endproducts (AGEs) in Diet-Related Diseases." Antioxidants 9, no. 2 (February 6, 2020): 142. http://dx.doi.org/10.3390/antiox9020142.

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Diets are currently characterized by elevated sugar intake, mainly due to the increased consumption of processed sweetened foods and drinks during the last 40 years. Diet is the main source of advanced glycation endproducts (AGEs). These are toxic compounds formed during the Maillard reaction, which takes place both in vivo, in tissues and fluids under physiological conditions, favored by sugar intake, and ex vivo during food preparation such as baking, cooking, frying or storage. Protein glycation occurs slowly and continuously through life, driving AGE accumulation in tissues during aging. For this reason, AGEs have been proposed as a risk factor in the pathogenesis of diet-related diseases such as diabetes, insulin resistance, cardiovascular diseases, kidney injury, and age-related and neurodegenerative diseases. AGEs are associated with an increase in oxidative stress since they mediate the production of reactive oxygen species (ROS), increasing the intracellular levels of hydrogen peroxide (H2O2), superoxide (O2−), and nitric oxide (NO). The interaction of AGEs with the receptor for AGEs (RAGE) enhances oxidative stress through ROS production by NADPH oxidases inside the mitochondria. This affects mitochondrial function and ultimately influences cell metabolism under various pathological conditions. This short review will summarize all evidence that relates AGEs and ROS production, their relationship with diet-related diseases, as well as the latest research about the use of natural compounds with antioxidant properties to prevent the harmful effects of AGEs on health.

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Furst, Jessica R., Leonardo C. Bandeira, Wen-Wei Fan, Sanchita Agarwal, Kyle K. Nishiyama, Donald J. McMahon, Elzbieta Dworakowski, Hongfeng Jiang, Shonni J. Silverberg, and Mishaela R. Rubin. "Advanced Glycation Endproducts and Bone Material Strength in Type 2 Diabetes." Journal of Clinical Endocrinology & Metabolism 101, no. 6 (June 1, 2016): 2502–10. http://dx.doi.org/10.1210/jc.2016-1437.

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Abstract Context: Skeletal deterioration, leading to an increased risk of fracture, is a known complication of type 2 diabetes mellitus (T2D). Yet plausible mechanisms to account for skeletal fragility in T2D have not been clearly established. Objective: The objective of the study was to determine whether bone material properties, as measured by reference point indentation, and advanced glycation endproducts (AGEs), as determined by skin autofluorescence (SAF), are related in patients with T2D. Design: This was a cross-sectional study. Setting: The study was conducted at a tertiary medical center. Patients: Sixteen postmenopausal women with T2D and 19 matched controls participated in the study. Main Outcome Measures: Bone material strength index (BMSi) by in vivo reference point indentation, AGE accumulation by SAF, and circulating bone turnover markers were measured. Results: BMSi was reduced by 9.2% in T2D (P = .02) and was inversely associated with the duration of T2D (r = −0.68, P = .004). Increased SAF was associated with reduced BMSi (r = −0.65, P = .006) and lower bone formation marker procollagen type 1 amino-terminal propeptide (r = −0.63, P = .01) in T2D, whereas no associations were seen in controls. SAF accounted for 26% of the age-adjusted variance in BMSi in T2D (P = .03). Conclusions: Bone material properties are impaired in postmenopausal women with T2D as determined by reference point indentation. The results suggest a role for the accumulation of AGEs to account for inferior BMSi in T2D.

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Turk, Zdenka, Spomenka Ljubic, Niksa Turk, and Bojan Benko. "Serum antibodies to advanced glycation endproducts (AGE) and circulating AGE-immune complexes in NIDDM patients." Diabetes Research and Clinical Practice 50 (September 2000): 357. http://dx.doi.org/10.1016/s0168-8227(00)81217-6.

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Wang, Ruojiao, Mitsuhiro Kudo, Munehiro Yokoyama, and Goro Asano. "Roles of Advanced Glycation Endproducts (AGE) and Receptor for AGE on Vascular Smooth Muscle Cell Growth." Journal of Nippon Medical School 68, no. 6 (2001): 472–81. http://dx.doi.org/10.1272/jnms.68.472.

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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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Akhter, Firoz, Doris Chen, Asma Akhter, Shi Fang Yan, and Shirley ShiDu Yan. "Age-dependent accumulation of dicarbonyls and advanced glycation endproducts (AGEs) associates with mitochondrial stress." Free Radical Biology and Medicine 164 (February 2021): 429–38. http://dx.doi.org/10.1016/j.freeradbiomed.2020.12.021.

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Sano, Hiroyuki, Ryoji Nagai, Kenshi Matsumoto, and Seikoh Horiuchi. "Receptors for proteins modified by advanced glycation endproducts (AGE)—their functional role in atherosclerosis." Mechanisms of Ageing and Development 107, no. 3 (March 1999): 333–46. http://dx.doi.org/10.1016/s0047-6374(99)00011-1.

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Simm, A., J. Wagner, T. Gursinsky, N. Nass, I. Friedrich, R. Schinzel, E. Czeslik, R. E. Silber, and R. J. Scheubel. "Advanced glycation endproducts: A biomarker for age as an outcome predictor after cardiac surgery?" Experimental Gerontology 42, no. 7 (July 2007): 668–75. http://dx.doi.org/10.1016/j.exger.2007.03.006.

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Kani, Hatice K., Ebru K. Kocazorbaz, and Figen Zihnioglu. "Investigation and isolation of peptide based antiglycating agents from various sources." Turkish Journal of Biochemistry 44, no. 5 (October 25, 2019): 699–705. http://dx.doi.org/10.1515/tjb-2018-0294.

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Abstract Background In this work, peptide based antiglycation agents from various sources against the advanced glycation endproducts (AGE) formation was investigated. Materials and methods As a source of peptides with deglycating activity, Glycine max, Hordeum vulgare, Triticum aestivum, Avena sativa, Prunus dulcis ve Juglans regia were used. The metal chelating activity and antioxidant activity were determined by Cu(II) chelating activity and CUPRAC (Cupric Reducing Antioxidant Capacity) methods. Antidiabetic activity was evaluated through BSA-glucose model. Results Most of the extracts obtained have inhibitory activity against AGE formation. Among all plant peptide isolates soybean was found to be most efficient by means of antiglycating (IC50 1.33 μg/mL), antioxidant (28.2 ± 1.4 μmol AAE/mg) and metal chelation activity (55%). Conclusion As a result, this study can provide preliminary data to literature to support researches those focused on peptide based glycation inhibitors and discovery of potent AGE inhibitory peptides.

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de Arriba, Susana Garcia, Claudia Loske, Ina Meiners, Gerd Fleischer, Michael Lobisch, Klaus Wessel, Hans Tritschler, Reinhard Schinzel, and Gerald Münch. "Advanced Glycation Endproducts Induce Changes in Glucose Consumption, Lactate Production, and ATP Levels in SH-SY5Y Neuroblastoma Cells by a Redox-Sensitive Mechanism." Journal of Cerebral Blood Flow & Metabolism 23, no. 11 (November 2003): 1307–13. http://dx.doi.org/10.1097/01.wcb.0000090622.86921.0e.

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Advanced glycation endproducts (AGEs) accumulate on long-lived proteins, including β-amyloid plaques in Alzheimer's disease, and are suggested to contribute to neuronal dysfunction and cell death. We have investigated the effects of a model AGE upon glucose metabolism and energy production in a neuroblastoma cell line. AGEs decrease cellular ATP levels and increase glucose consumption and lactate production. All of the AGE-induced metabolic changes can be attenuated by antioxidants such as (R+)-α-lipoic acid and 17β-estradiol. These antioxidants may become useful drugs against (AGE-mediated) effects in neurodegeneration through their positive effects on cellular energy metabolism.

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Rabbani, Naila, Antonysunil Adaikalakoteswari, James R. Larkin, Sianna Panagiotopoulos, Richard J. MacIsaac, Dennis K. Yue, Gregory R. Fulcher, et al. "Analysis of Serum Advanced Glycation Endproducts Reveals Methylglyoxal-Derived Advanced Glycation MG-H1 Free Adduct Is a Risk Marker in Non-Diabetic and Diabetic Chronic Kidney Disease." International Journal of Molecular Sciences 24, no. 1 (December 21, 2022): 152. http://dx.doi.org/10.3390/ijms24010152.

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Accumulation of advanced glycation endproducts (AGEs) is linked to decline in renal function, particularly in patients with diabetes. Major forms of AGEs in serum are protein-bound AGEs and AGE free adducts. In this study, we assessed levels of AGEs in subjects with and without diabetes, with normal renal function and stages 2 to 4 chronic kidney disease (CKD), to identify which AGE has the greatest progressive change with decline in renal function and change in diabetes. We performed a cross-sectional study of patients with stages 2–4 CKD, with and without diabetes, and healthy controls (n = 135). Nine protein-bound and free adduct AGEs were quantified in serum. Most protein-bound AGEs increased moderately through stages 2–4 CKD whereas AGE free adducts increased markedly. Methylglyoxal-derived hydroimidazolone MG-H1 free adduct was the AGE most responsive to CKD status, increasing 8-fold and 30-fold in stage 4 CKD in patients without and with diabetes, respectively. MG-H1 Glomerular filtration flux was increased 5-fold in diabetes, likely reflecting increased methylglyoxal glycation status. We conclude that serum MG-H1 free adduct concentration was strongly related to stage of CKD and increased in diabetes status. Serum MG-H1 free adduct is a candidate AGE risk marker of non-diabetic and diabetic CKD.

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Smit, A., and H. Lutgers. "The Clinical Relevance of Advanced Glycation Endproducts (AGE) and Recent Developments in Pharmaceutics to Reduce AGE Accumulation." Current Medicinal Chemistry 11, no. 20 (October 1, 2004): 2767–84. http://dx.doi.org/10.2174/0929867043364342.

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Gugliucci, A., and M. Bendayan. "Reaction of advanced glycation endproducts with renal tissue from normal and streptozotocin-induced diabetic rats: an ultrastructural study using colloidal gold cytochemistry." Journal of Histochemistry & Cytochemistry 43, no. 6 (June 1995): 591–600. http://dx.doi.org/10.1177/43.6.7769229.

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Advanced glycation endproducts (AGEs) are believed to play important roles in the molecular basis of long-term diabetes complications. In the present study we have revealed direct reactivity of AGEs towards kidney tissue structures. Bovine serum albumin, modified by advanced glycation and tagged with colloidal gold (AGE-BSA-gold) was applied to renal tissue sections from normal and long-term diabetic rats by a post-embedding procedure at the electron microscopic level. The AGE-BSA probes were characterized by fluorometry, spectrophotometry, free amines analysis, measurement of early glycation products, electrophoresis, and isoelectrofocusing. When applied to renal tissue sections, AGE-BSA-gold exhibited strong labeling on nuclei. At the extracellular level, glomerular basement membranes and mesangial matrix were labeled. Probes having a higher content of AGEs yielded more intense labeling. Control experiments demonstrated the specificity of the labeling obtained. Quantitative evaluation indicated little variation in reactivity among tissues from rats of different ages. However, a significant increase in reactivity was established for tissues from streptozotocin-induced long-term diabetic rats. This study thus provides direct evidence that soluble AGEs bind to cell nuclei and to structures implicated in the development of diabetic glomerular nephropathy, demonstrating higher AGE reactivity in tissues from diabetic animals.

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Kunt, T., T. Forst, O. Harzer, G. Buchert, A. Pfützner, M. Löbig, A. Zschäbitz, E. Stofft, M. Engelbach, and J. Beyer. "The influence of advanced glycation endproducts (AGE) on the expression of human endothelial adhesion molecules." Experimental and Clinical Endocrinology & Diabetes 106, no. 03 (July 14, 2009): 183–88. http://dx.doi.org/10.1055/s-0029-1211974.

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Pereira, R., V. A. D. C. Hong, L. Bortolotto, R. D. S. Pinto, M. Passarelli, and A. Machado-Lima. "Dietary Advanced Glycation Endproducts (Age) Impaired The Endothelial Function In Healthy Eutrophic In Aging Process." Atherosclerosis 287 (August 2019): e266. http://dx.doi.org/10.1016/j.atherosclerosis.2019.06.823.

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Verbeke, Philippe, Martine Perichon, Caroline Borot–Laloi, Jean Schaeverbeke, and Hilaire Bakala. "Accumulation of Advanced Glycation Endproducts in the Rat Nephron: Link with Circulating AGEs During Aging." Journal of Histochemistry & Cytochemistry 45, no. 8 (August 1997): 1059–68. http://dx.doi.org/10.1177/002215549704500804.

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The accumulation of advanced glycosylation end products (AGEs) is believed to be a factor in the development of aging nephropathy. We have attempted to establish a link between the formation of AGEs and the onset of renal impairment with aging, indicated by albuminuria, using a fluorescence assay and immunohistochemical detection of AGEs in the renal extracellular matrix in rats. The fluorescence of collagenase-digested Type IV collagen from GBM increased with age, from 1.65 ± 0.05 AU/mM OHPro (3 months) and 1.58 ± 0.04 (10 months) to 2.16 ± 0.06 (26 months) ( p>0.001) and 2.53 ± 0.18 (30 months) ( p>0.001). In contrast, the extent of early glycation products significantly decreased from 5.35 ± 0.25 nmol HCHO/nmol OHPro at 3 months to 3.14 ± 0.19 at 10 months ( p>0.001), 3.42 ± 0.38 at 26 months, and 0.74 ± 0.08 at 30 months ( p>0.001). The urinary fluorescence of circulating AGE rose from 2.42 ± 0.15 AU/mg protein (3 months), 1.69 ± 0.07 (10 months), to 4.63 ± 0.35 (26 months) ( p>0.01) and 4.73 ± 0.72 (30 months), while the serum fluorescence increased from 0.39 ± 0.02 AU/mg protein at 3 months and 0.43 ± 0.02 at 10 months to 0.59 ± 0.04 at 26 months ( p>0.001) and 0.54 ± 0.03 at 30 months ( p>0.04). Polyclonal antibodies raised against AGE RNase showed faint areas of AGE immunoreactivity in mesangial areas in the nephrons of young rats. The immunolabeling of Bowman's capsule, the mesangial matrices, and the peripheral loops of glomerular and tubule basement membranes increased with rat age. The increase in circulating AGE peptides parallels the accumulation of AGEs in the nephron, and this parallels the pattern of extracellular matrix deposition, suggesting a close link between AGE accumulation and renal impairment in aging rats. (J Histochem Cytochem 45:1059–1068, 1997)

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Lohou, Sasaki, Boullier, Duplantier, and Sonnet. "Hydroxypyridinone-Diamine Hybrids as Potential Neuroprotective Agents in the PC12 Cell-Line Model of Alzheimer's Disease." Pharmaceuticals 12, no. 4 (October 27, 2019): 162. http://dx.doi.org/10.3390/ph12040162.

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There is an urgent need to propose effective treatments for Alzheimer’s disease (AD). Although the origin of the disease is poorly understood, several therapeutic options have been proposed. The new therapeutic approaches targeting biometal-mediated neurodegenerative pathways appear to be interesting ones. As a continuation of our preceding studies, two novel series of advanced glycation endproducts (AGE)/advanced lipid peroxidation endproducts (ALE) inhibitors have been developed as multifunctional scavengers. This extended work allowed us to highlight the new hydroxypyridinone-diamine hybrid IIa-3 bearing a C4 alkyl linker between the two pharmacophores. This derivative exhibited preserved potent capacities to trap reactive carbonyl species (vicinal diamine function) as well as reactive oxygen species and transition metals (hydroxypyridinone moiety) in comparison with previously described lead compound 1. In addition, its good predicted absorption, distribution, metabolism and excretion (ADME) properties were correlated with a better efficacy to inhibit in vitro methylglyoxal-induced apoptosis in neuronal-like PC12 cells. This new promising agent revealed improved druglikeness and ability to prevent biometal-mediated oxidative and carbonyl stress amplification involved in AD pathogenesis.

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Zen, Ke, Li-Min Li, Dan-Qing Liu, Ya-Lan Guo, Yuan Liu, and Chen-Yu Zhang. "Role of microRNA-214-targeting PTEN in advanced glycation endproducts-induced apoptosis delay of monocytes (89.35)." Journal of Immunology 184, no. 1_Supplement (April 1, 2010): 89.35. http://dx.doi.org/10.4049/jimmunol.184.supp.89.35.

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Abstract Advanced glycation endproduct(AGE) delays spontaneous apoptosis of human monocytes and contributes to the development of a local inflammatory response. The mechanism by which AGEs effect monocyte apoptosis, however, is unclear. Here we report that AGE-modified BSA and β2-microglobulin(β2m) can increase miR-214 expression in monocytes, which in turn, enhances cell survival by reducing the expression of phosphatase and tensin homolog(PTEN). Employing miRNA microarray, we obtains a genome-wide miRNA expression profiling of THP-1 cells treated with/without AGEs. Among 470 miRNAs screened, 6 miRNAs including miR-214 are upregulated while 5 miRNAs were down-regulated (fold-change>2) in AGE-treated cells. AGE-induced miRNA differential expression is validated by miRNA qRT-PCR. Significant upregulation of miR-214 is confirmed in normal human monocytes treated with AGEs and monocytes isolated from patients with chronic renal failure. Both AGE-treated monocytes and patient monocytes have a delayed apoptosis. Luciferase reporter assay shows that miR-214 targets PTEN mRNA 3’-untranslated region. Furthermore, PTEN expression is inversely correlated with miR-214 expression in monocytes and the forced expression of miR-214 leads to a delayed apoptosis of THP-1. In contrast, decrease of miR-214 expression via anti-miR-214 largely abolishes AGE-induced cell survival. In summary, our findings define a new regulation role of miR-214 on AGE-induced monocyte survival by impeding PTEN expression.

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Prevost, G., E. Boulanger, H. Bulckaen, C. Gaxatte, G. Beraud, G. Robitaille, V. Roquet, P. Fontaine, and F. Puisieux. "P2 L’aminoguanidine prévient le vieillissement vasculaire lié aux AGE (Advanced Glycation Endproducts) chez la souris diabétique." Diabetes & Metabolism 34 (March 2008): H43. http://dx.doi.org/10.1016/s1262-3636(08)72914-8.

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AHMED, Naila, Ognian K. ARGIROV, Harjit S. MINHAS, Carlos A. A. CORDEIRO, and Paul J. THORNALLEY. "Assay of advanced glycation endproducts (AGEs): surveying AGEs by chromatographic assay with derivatization by 6-aminoquinolyl-N-hydroxysuccinimidyl-carbamate and application to N∊-carboxymethyl-lysine- and N∊-(1-carboxyethyl)lysine-modified albumin." Biochemical Journal 364, no. 1 (May 8, 2002): 1–14. http://dx.doi.org/10.1042/bj3640001.

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Glycation of proteins leads to the formation of early glycation adducts (fructosamine derivatives) and advanced glycation endproducts (AGEs). Formation of AGEs has been linked to the development of cataract, diabetic complications, uraemia, Alzheimer's disease and other disorders. AGEs are a group of compounds of diverse molecular structure and biological function. To characterize AGE-modified proteins used in studies of structural and functional effects of glycation, an assay was developed that surveys the content of early and advanced glycation adducts in proteins. The assay procedure involved enzymic hydrolysis of protein substrate, derivatization of the hydrolysate with 6-aminoquinolyl-N-hydroxysuccinimidyl carbamate (AQC) and HPLC of the resulting adducts with fluorimetric detection. Structural isomers of methylglyoxal-derived hydroimidazolone, glyoxal-derived hydroimidazolone, 3-deoxyglucosone-derived hydroimidazolone and Nδ-(4-carboxy-4,6-dimethyl-5,6-dihydroxy-1,4,5,6-tetrahydropyrimidin-2-yl)-ornithine (THP) were determined for the first time. AGEs with intrinsic fluorescence (argpyrimidine, pentosidine) were assayed without derivatization. Limits of detection were 2–17pmol and levels of recovery were 50–99%, depending on the analyte. The AQC assay resolved structural and epimeric isomers of methylglyoxal-derived hydroimidazolones and THP. Hydroimidazolones, THP and argpyrimidine were AGEs of short-to-intermediate stability under physiological conditions, with half-lives of 1–2weeks. Their measurement provides further insight into the glycation process. The assay was applied to the characterization of human serum albumin minimally and highly modified by N∊-carboxymethyl-lysine and N∊-(1-carboxyethyl)-lysine.

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Yamagishi, Sho-ichi. "Role of Advanced Glycation Endproduct (AGE)-Receptor for Advanced Glycation Endproduct (RAGE) Axis in Cardiovascular Disease and Its Therapeutic Intervention." Circulation Journal 83, no. 9 (August 23, 2019): 1822–28. http://dx.doi.org/10.1253/circj.cj-19-0618.

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M Ames, J. "Dietary Maillard Reaction Products: Implications for Human Health and Disease." Czech Journal of Food Sciences 27, Special Issue 1 (June 24, 2009): S66—S69. http://dx.doi.org/10.17221/624-cjfs.

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When foods are heat processed, the sugars and lipids react with the proteins they contain via the Maillard and related reactions to form a wide range of products. As a result, the sensory, safety, nutritional and health-promoting attributes of the foods are affected. Reaction products include advanced glycation/lipoxidation endproducts (AGE/ALEs), acrylamide and heterocyclic amines (HAA), all of which may impact on human health and disease. Furthermore, some Maillard reaction products affect the growth of colonic bacteria and thermally-induced modification of dietary protein can affect allergenicity. This paper briefly reviews aspects of the Maillard reaction in food related to human health.

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Saraswat, Megha, P. Yadagiri Reddy, P. Muthenna, and G. Bhanuprakash Reddy. "Prevention of non-enzymic glycation of proteins by dietary agents: prospects for alleviating diabetic complications." British Journal of Nutrition 101, no. 11 (November 6, 2008): 1714–21. http://dx.doi.org/10.1017/s0007114508116270.

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The accumulation of advanced glycation endproducts (AGE) due to non-enzymic glycation of proteins has been implicated in several pathophysiologies associated with ageing and diabetes. The formation of AGE is accelerated in hyperglycaemic conditions, which alter the structure and function of long-lived proteins. Thus inhibition of the formation of AGE is believed to play a role in the prevention of diabetic complications. In the present study we evaluated the antiglycating effect of aqueous extracts of various plant-based foods. The effect of aqueous extracts of these agents in terms of their ability to prevent the accumulation of AGE due to fructose-mediatedin vitroglycation of eye lens soluble proteins was investigated. The degree of protein glycation in the absence and presence of dietary extracts was assessed by different complementary methods, i.e. non-tryptophan AGE fluorescence, AGE-induced cross-linking by SDS-PAGE and glyco-oxidative damage by carbonyl assay. Five out of the seventeen agents tested showed significant inhibitory potential againstin vitroprotein glycation in a dose-dependent manner. Prominent among them were ginger, cumin, cinnamon, black pepper and green tea, which inhibitedin vitroAGE formation to lens proteins 40–90 % at 1·0 mg/ml concentration. Assessing their potential to reduce the amount of glycated protein using boronate affinity chromatography and also their ability to prevent the formation of specific antigenic-AGE structures by immunodetection further substantiated the importance of ginger, cumin and cinnamon in reducing AGE burden. These findings indicate the potential of some dietary components to prevent and/or inhibit protein glycation. Thus these dietary agents may be able to be exploited for controlling AGE-mediated diabetic pathological conditionsin vivo.

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Maessen, Dionne E. M., Coen D. A. Stehouwer, and Casper G. Schalkwijk. "The role of methylglyoxal and the glyoxalase system in diabetes and other age-related diseases." Clinical Science 128, no. 12 (March 27, 2015): 839–61. http://dx.doi.org/10.1042/cs20140683.

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The formation and accumulation of advanced glycation endproducts (AGEs) are related to diabetes and other age-related diseases. Methylglyoxal (MGO), a highly reactive dicarbonyl compound, is the major precursor in the formation of AGEs. MGO is mainly formed as a byproduct of glycolysis. Under physiological circumstances, MGO is detoxified by the glyoxalase system into D-lactate, with glyoxalase I (GLO1) as the key enzyme in the anti-glycation defence. New insights indicate that increased levels of MGO and the major MGO-derived AGE, methylglyoxal-derived hydroimidazolone 1 (MG-H1), and dysfunctioning of the glyoxalase system are linked to several age-related health problems, such as diabetes, cardiovascular disease, cancer and disorders of the central nervous system. The present review summarizes the mechanisms through which MGO is formed, its detoxification by the glyoxalase system and its effect on biochemical pathways in relation to the development of age-related diseases. Although several scavengers of MGO have been developed over the years, therapies to treat MGO-associated complications are not yet available for application in clinical practice. Small bioactive inducers of GLO1 can potentially form the basis for new treatment strategies for age-related disorders in which MGO plays a pivotal role.

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Mastrocola, Raffaella, Manuela Aragno, Giuseppe Alloatti, Massimo Collino, Claudia Penna, and Pasquale Pagliaro. "Metaflammation: Tissue-Specific Alterations of the NLRP3 Inflammasome Platform in Metabolic Syndrome." Current Medicinal Chemistry 25, no. 11 (April 17, 2018): 1294–310. http://dx.doi.org/10.2174/0929867324666170407123522.

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In the last decades, the extension of life expectancy and the increased consumption of foods rich in saturated fats and added sugars have exposed the general population to emerging health problems. The prevalence of metabolic syndrome (MS), composed of a cluster of factors as obesity, dyslipidemia, hyperglycemia, and hypertension, is rapidly increasing in industrialized and developing countries leading to precocious onset of age-related diseases. Indeed, oxidative stress, accumulation of advanced glycation endproducts, and a chronic low-grade inflammation are common features of MS and physiological ageing. In particular, the entire set of MS factors contributes to the development of an inflammatory status named metaflammation, which has been associated with activation of early innate immune response through the assembling of the multiprotein complex inflammasome. The most investigated family of inflammasome platforms is the NOD-like receptor pyridine containing (NLRP) 3, which is activated by several exogenous and endogenous stimuli, leading to the sequential cleavage of caspase-1 and IL-1β, followed by secretion of active IL-1β. We here collect the most recent findings on NLRP3 activation in MS providing evidence of its central role in disease progression and organ dysfunction in target tissues of metaflammation, in particular in cardiovascular, hepatic and renal complications, with a focus on oxidative stress and advanced glycation endproducts. A wide overview of the most promising strategies for the modulation of NLRP3 activation and related metabolic repercussions is also provided, since the finding of specific pharmacological tools is an urgent requirement to reduce the social and economic burden of MS- and elderly-associated diseases.

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Inan-Eroglu, Elif, Aylin Ayaz, and Zehra Buyuktuncer. "Formation of advanced glycation endproducts in foods during cooking process and underlying mechanisms: a comprehensive review of experimental studies." Nutrition Research Reviews 33, no. 1 (November 8, 2019): 77–89. http://dx.doi.org/10.1017/s0954422419000209.

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AbstractAdvanced glycation endproducts (AGE) are a group of complex and heterogeneous molecules, sharing some common characteristics such as covalent cross-link formation among proteins, the effect of transforming the colour of food products into yellow-brown colours and fluorescence formation. AGE are linked to many diseases including diabetes, renal diseases, CVD, liver diseases, neuro-degenerative and eye disorders, female reproductive dysfunction, and even cancer. AGE are formed endogenously but are also provided from exogenous sources including diet and tobacco. Western diet, rich in processed and/or heat-treated foods, fat and sugar, increases the exposure to AGE. The foods that contain high levels of fat and protein are generally rich in terms of AGE, and are also prone to AGE formation during cooking compared with carbohydrate-rich foods such as vegetables, fruits, legumes and whole grains. The present article aimed to review the literature about the effects of different cooking methods and conditions on the AGE content of food and AGE formation mechanisms using a comprehensive approach.

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Sotomayor, Camilo G., António W. Gomes-Neto, Marco van Londen, Rijk O. B. Gans, Ilja M. Nolte, Stefan P. Berger, Gerjan J. Navis, et al. "Circulating Advanced Glycation Endproducts and Long-Term Risk of Cardiovascular Mortality in Kidney Transplant Recipients." Clinical Journal of the American Society of Nephrology 14, no. 10 (September 17, 2019): 1512–20. http://dx.doi.org/10.2215/cjn.00540119.

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Background and objectivesIn kidney transplant recipients, elevated circulating advanced glycation endproducts (AGEs) are the result of increased formation and decreased kidney clearance. AGEs trigger several intracellular mechanisms that ultimately yield excess cardiovascular disease. We hypothesized that, in stable kidney transplant recipients, circulating AGEs are associated with long-term risk of cardiovascular mortality, and that such a relationship is mediated by inflammatory, oxidative stress, and endothelial dysfunction biomarkers.Design, setting, participants, & measurementsProspective cohort study of stable kidney transplant recipients recruited between 2001 and 2003 in a university setting. We performed multivariable-adjusted Cox regression analyses to assess the association of AGEs (i.e., Nε-[Carboxymethyl]lysine (CML) and Nε-[Carboxyethyl]lysine (CEL), measured by tandem mass spectrometry) with cardiovascular mortality. Mediation analyses were performed according to Preacher and Hayes’s procedure.ResultsWe included 555 kidney transplant recipients (age 51±12 years, 56% men). During a median follow-up of 6.9 years, 122 kidney transplant recipients died (52% deaths were due to cardiovascular causes). CML and CEL concentrations were directly associated with cardiovascular mortality (respectively, hazard ratio, 1.55; 95% confidence interval, 1.24 to 1.95; P<0.001; and hazard ratio, 1.53; 95% confidence interval 1.18 to 1.98; P=0.002), independent of age, diabetes, smoking status, body mass index, eGFR and proteinuria. Further adjustments, including cardiovascular history, did not materially change these findings. In mediation analyses, free thiol groups and soluble vascular cell adhesion molecule-1 consistently explained approximately 35% of the association of CML and CEL with cardiovascular mortality.ConclusionsIn stable kidney transplant recipients, circulating levels of AGEs are independently associated with long-term risk of cardiovascular mortality.PodcastThis article contains a podcast at https://www.asn-online.org/media/podcast/CJASN/2019_09_17_CJN00540119.mp3

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Garay-Sevilla, M. E., M. S. Beeri, M. P. de la Maza, A. Rojas, S. Salazar-Villanea, and J. Uribarri. "The potential role of dietary advanced glycation endproducts in the development of chronic non-infectious diseases: a narrative review." Nutrition Research Reviews 33, no. 2 (April 2, 2020): 298–311. http://dx.doi.org/10.1017/s0954422420000104.

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AbstractIncreasing clinical and experimental evidence accumulated during the past few decades supports an important role for dietary advanced glycation endproducts (AGE) in the pathogenesis of many chronic non-infectious diseases, such as type 2 diabetes, CVD and others, that are reaching epidemic proportions in the Western world. Although AGE are compounds widely recognised as generated in excess in the body in diabetic patients, the potential importance of exogenous AGE, mostly of dietary origin, has been largely ignored in the general nutrition audience. In the present review we aim to describe dietary AGE, their mechanisms of formation and absorption into the body as well as their main mechanisms of action. We will present in detail current evidence of their potential role in the development of several chronic non-infectious clinical conditions, some general suggestions on how to restrict them in the diet and evidence regarding the potential benefits of lowering their consumption.

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Holik, Ann-Katrin, Verena Stöger, Kathrin Hölz, Mark M. Somoza, and Veronika Somoza. "Impact of free Nε-carboxymethyllysine, its precursor glyoxal and AGE-modified BSA on serotonin release from human parietal cells in culture." Food & Function 9, no. 7 (2018): 3906–15. http://dx.doi.org/10.1039/c8fo01045e.

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Lee, Hyun-Sun, and Jin-A. Yoon. "Inhibitory Activity of Advanced Glycation Endproducts (AGE) Formation of Edible Plants for Development of Anti-Wrinkle Ingredients." Journal of the Korean Society of Food Science and Nutrition 39, no. 2 (February 27, 2010): 186–92. http://dx.doi.org/10.3746/jkfn.2010.39.2.186.

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Bengmark, Stig, and Nóra Hajdú. "Endproducts and receptor of advanced glycation and lipoxidation (AGE, ALE, RAGE) and chronic diseases – a food perspective." Orvosi Hetilap 149, no. 17 (April 2008): 771–78. http://dx.doi.org/10.1556/oh.2008.28308.

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Background: Chronic diseases as well as complications to acute and chronic disease are repeatedly associated with accumulation in the body of glycated and lipoxidated proteins and peptides. These molecules are strongly associated with activation of a specific receptor called RAGE and a long-lasting exaggerated level of inflammation in the body. Methods: PubMed reports in excess of 5000 papers plus about 14000 articles about the related HbA1c, most of them published in the last five years. Most of available abstracts have been read and circa 800 full papers studied in detail. Results: RAGE, a member of the immunoglobulin superfamily of cell surface molecules and receptor for advanced glycation endproducts, functions as a master switch, induces sustained activation of NF-κB, suppresses a series of endogenous autoregulatory functions and converts long-lasting pro-inflammatory signals into sustained cellular dysfunction and disease. Its activation is associated with high levels of dysfunctioning proteins in body fluids and tissues, and strongly associated with a series of diseases from allergy and Alzheimer to rheumatoid arthritis and urogenital disorders. Heat-treatment, irradiation and ionisation of foods increase the content in foods of AGE/ALE. Conclusions: Some processed foods are much like tobacco smoking great contributors to accumulation of glycated and lipoxidated molecules in the tissues. Change of life style: avoidance of foods rich in deranged proteins and peptides and increased consumption of antioxidants, especially polyphenols counteracts such a development.

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Lin, Reigh-Yi, Ernane D. Reis, Anthony T. Dore, Min Lu, Newsha Ghodsi, John T. Fallon, Edward A. Fisher, and Helen Vlassara. "Lowering of dietary advanced glycation endproducts (AGE) reduces neointimal formation after arterial injury in genetically hypercholesterolemic mice." Atherosclerosis 163, no. 2 (August 2002): 303–11. http://dx.doi.org/10.1016/s0021-9150(02)00008-4.

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SCHEUBEL, R., S. KAHRSTEDT, H. WEBER, J. HOLTZ, I. FRIEDRICH, J. BORGERMANN, R. SILBER, and A. SIMM. "Depression of progenitor cell function by advanced glycation endproducts (AGEs): Potential relevance for impaired angiogenesis in advanced age and diabetes." Experimental Gerontology 41, no. 5 (May 2006): 540–48. http://dx.doi.org/10.1016/j.exger.2006.01.002.

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Migrino, Raymond Q., Hannah A. Davies, Seth Truran, Nina Karamanova, Daniel A. Franco, Thomas G. Beach, Geidy E. Serrano, Danh Truong, Mehdi Nikkhah, and Jillian Madine. "Amyloidogenic medin induces endothelial dysfunction and vascular inflammation through the receptor for advanced glycation endproducts." Cardiovascular Research 113, no. 11 (July 20, 2017): 1389–402. http://dx.doi.org/10.1093/cvr/cvx135.

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AbstractAimsMedin is a common amyloidogenic protein in humans that accumulates in arteries with advanced age and has been implicated in vascular degeneration. Medin’s effect on endothelial function remains unknown. The aims are to assess medin’s effects on human arteriole endothelial function and identify potential mechanisms underlying medin-induced vascular injury.Methods and resultsEx vivo human adipose and leptomeningeal arterioles were exposed (1 h) to medin (0.1, 1, or 5 µM) without or with FPS–ZM1 [100 µM, receptor for advanced glycation endproducts (RAGE)-specific inhibitor] and endothelium-dependent function (acetylcholine dilator response) and endothelium-independent function (dilator response to nitric oxide donor diethylenetriamine NONOate) were compared with baseline control. Human umbilical vein endothelial cells were exposed to medin without or with FPS–ZM1 and oxidative and nitrative stress, cell viability, and pro-inflammatory signaling measures were obtained. Medin caused impaired endothelial function (vs. baseline response: −45.2 ± 5.1 and −35.8 ± 7.9% in adipose and leptomeningeal arterioles, respectively, each P < 0.05). Dilator response to NONOate was not significantly changed. Medin decreased arteriole and endothelial cell nitric oxide production, increased superoxide production, reduced endothelial cell viability, proliferation, and migration. Medin increased gene and protein expression of interleukin-6 and interleukin-8 via activation of nuclear factor kappa-light-chain-enhancer of activated B cells (NFκB). Medin-induced endothelial dysfunction and oxidative stress were reversed by antioxidant polyethylene glycol superoxide dismutase and by RAGE inhibitor FPS-ZM1.ConclusionsMedin causes human microvascular endothelial dysfunction through oxidative and nitrative stress and promotes pro-inflammatory signaling in endothelial cells. These effects appear to be mediated via RAGE. The findings represent a potential novel mechanism of vascular injury.

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Turk, Zdenka, Spomenka Ljubic, Nikša Turk, and Bojan Benko. "Detection of autoantibodies against advanced glycation endproducts and AGE-immune complexes in serum of patients with diabetes mellitus." Clinica Chimica Acta 303, no. 1-2 (January 2001): 105–15. http://dx.doi.org/10.1016/s0009-8981(00)00389-2.

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Turk, Z., R. Mesić, and B. Benko. "Comparison of advanced glycation endproducts on haemoglobin (Hb-AGE) and haemoglobin A1c for the assessment of diabetic control." Clinica Chimica Acta 277, no. 2 (October 1998): 159–70. http://dx.doi.org/10.1016/s0009-8981(98)00128-4.

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Triginer, L., I. Carrión Barberà, L. Tío, T. C. Salman Monte, C. Pérez, L. Polino, A. Ribes, J. Llorente Onaindia, and J. Monfort. "AB1460 ACCUMULATED ADVANCED GLYCATION ENDPRODUCTS ARE SIGNIFICANTLY HIGHER IN PATIENTS WITH IMMUNE-MEDIATED INFLAMMATORY DISEASES THAN IN HEALTHY POPULATION." Annals of the Rheumatic Diseases 81, Suppl 1 (May 23, 2022): 1835.3–1836. http://dx.doi.org/10.1136/annrheumdis-2022-eular.4893.

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BackgroundAdvanced glycation endproducts (AGEs) are the result of non-enzymatic glycation of proteins, lipids or nucleic acids. In circumstances characterized by increased oxidative and carbonyl stress, such as chronic inflammation, AGEs can be formed more rapidly1, generating reactive oxygen species and activating inflammatory signaling cascades through their chief signaling receptor (commonly abbreviated as RAGE)2. This positive feedback of inflammation can play a role in the etiology of immune-mediated inflammatory diseases, more specifically in rheumatoid arthritis (RA), ankylosing spondylitis (AS) and systemic lupus erythematosus (SLE).ObjectivesTo investigate whether the accumulated concentrations of AGEs in patients with SLE, RA or AS are significantly higher than in healthy patients.MethodsOne hundred thirteen consecutive patients fulfilling ACR/EULAR criteria for RA, 60 patients fulfilling ASAS/OMERACT MRI criteria for AS, 97 patients fulfilling ACR/SLICC criteria for SLE and 527 sex-matched healthy controls were recruited.in cross-sectional study. Exclusion criteria were pregnancy, diabetes mellitus, corticosteroid treatment ≥ 20mg/day and malignant neoplasm. Accumulated AGEs were non-invasively measured by skin autofluorescence (Age Reader Mu Connect, Diagnostics Technologies B.V) and demographic and clinical data were collected. AGEs comparisons between patients and controls were performed by multiple linear regression analysis adjusted by confunders, previously described in literature (age, smoking habit and cardiovascular risk-factors). Age was centered at 55 years.ResultsTable 1 shows some descriptive characteristics of our cohorts. AGEs adjusted mean was significantly increased in SLE patients compared with matched controls (95% CI [2.27, 2.76] vs [1.66, 1.89], p<0.0001), RA patients and controls (95% CI [2.41, 2.61] vs [1.68, 1.88], p<0.0001) and AS patients and controls (95% CI [2.03, 2.6] vs [1.66, 1.93], p<0.0001). In all 3 models, AGEs were also significantly positive correlated with smoking habit measured by packs per year (p<0.001) and age (p<0.0001).Table 1.Descriptive characteristics of the cohortsSLERAASPatientsControlsPatientsControlsPatientsControlsN=96N=189N=113N=240N=60N=99AGEs2.57 (0.65)1.98 (0.45)2.59 (0.58)2.00 (0.42)2.26 (0.46)1.90 (0.46)Age51.0 [43.0;61.0]56.0 [52.0;62.0]58.0 [54.0;65.0]61.0 [56.0;66.0]47.5 [41.0;55.0]53.0 [49.0;57.0]SmokerNo76 (79.2%)133 (70.4%)86 (76.1%)196 (81.7%)42 (70.0%)58 (58.6%)Yes20 (20.8%)56 (29.6%)27 (23.9%)44 (18.3%)18 (30.0%)41 (41.4%)Packs/year0.00 [0.00;10.8]2.50 [0.00;18.8]2.50 [0.00;18.0]0.00 [0.00;12.6]0.00 [0.00;7.88]14.9 [2.00;30.6]HypertensionNo74 (77.1%)116 (61.4%)77 (68.1%)146 (60.8%)53 (88.3%)75 (75.8%)Yes22 (22.9%)73 (38.6%)36 (31.9%)94 (39.2%)7 (11.7%)24 (24.2%)ObesityNo80 (83.3%)128 (67.7%)86 (76.1%)163 (67.9%)51 (85.0%)81 (81.8%)Yes16 (16.7%)61 (32.3%)27 (23.9%)77 (32.1%)9 (15.0%)18 (18.2%)DyslipidemiaNo85 (88.5%)104 (55.0%)79 (69.9%)108 (45.0%)51 (85.0%)55 (55.6%)Yes11 (11.5%)85 (45.0%)34 (30.1%)132 (55.0%)9 (15.0%)44 (44.4%)Continuous normal: mean (SD); Continuous non-normal: median [IQR]; Categorical: absolute (relative frequency)ConclusionAccumulated AGEs in all 3 pathologies are significantly higher than in the healthy controls. The different means of AGEs in each of the diseases, being higher in SLE and lower in AS, may suggest a different participation of AGEs in the immune-mediated mechanisms of each pathology.References[1]K. de Leeuw, R. Graaff et al., Accumulation of advanced glycation endproducts in patients with systemic lupus erythematosus, Rheumatology, Volume 46, Issue 10, October 2007, Pg 1551–1556.[2]Yan S., Ramasamy R. & Schmidt A. Mechanisms of Disease: advanced glycation end-products and their receptor in inflammation and diabetes complications. Nat Rev Endocrinol4, 285–293 (2008).Disclosure of InterestsNone declared

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Nabi, Rabia, Sahir Sultan Alvi, Mohd Saeed, Saheem Ahmad, and Mohammad Salman Khan. "Glycation and HMG-CoA Reductase Inhibitors: Implication in Diabetes and Associated Complications." Current Diabetes Reviews 15, no. 3 (April 1, 2019): 213–23. http://dx.doi.org/10.2174/1573399814666180924113442.

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Abstract:

Introduction: Diabetes Mellitus (DM) acts as an absolute mediator of cardiovascular risk, prompting the prolonged occurrence, size and intricacy of atherosclerotic plaques via enhanced Advanced Glycation Endproducts (AGEs) formation. Moreover, hyperglycemia is associated with enhanced glyco-oxidized and oxidized Low-Density Lipoprotein (LDL) possessing greater atherogenicity and decreased the ability to regulate HMG-CoA reductase (HMG-R). Although aminoguanidine (AG) prevents the AGE-induced protein cross-linking due to its anti-glycation potential, it exerts several unusual pharmaco-toxicological effects thus restraining its desirable therapeutic effects. HMG-R inhibitors/statins exhibit a variety of beneficial impacts in addition to the cholesterol-lowering effects. Objective: Inhibition of AGEs interaction with receptor for AGEs (RAGE) and glyco-oxidized-LDL by HMG-R inhibitors could decrease LDL uptake by LDL-receptor (LDL-R), regulate cholesterol synthesis via HMG-R, decrease oxidative and inflammatory stress to improve the diabetes-associated complications. Conclusion: Current article appraises the pathological AGE-RAGE concerns in diabetes and its associated complications, mainly focusing on the phenomenon of both circulatory AGEs and those accumulating in tissues in diabetic nephropathy, diabetic neuropathy, and diabetic retinopathy, discussing the potential protective role of HMG-R inhibitors against diabetic complications.

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Journal articles on the topic 'Advanced glycation endproducts (AGE)'

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