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Journal articles on the topic 'Glycation inhibitors'

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Author: Grafiati
Published: 6 September 2023

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1

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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2

E-FARAN, MISS GULL, MUHAMMAD ANJUM ZIA, and NIGHAT ASLAM. "EFFECT OF CAPTOPRIL." Professional Medical Journal 19, no. 01 (January 3, 2012): 078–85. http://dx.doi.org/10.29309/tpmj/2012.19.01.1929.

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Objectives: (1) To investigate the inhibitory effect of Captopril on level of glycation (in vivo). (2) To study glycation inhibition invivo. Study design: Case study. Period: Sep. 2006 to March. 2008. One year seven months. Setting: Department of Biochemistry Universityof Agriculture, Faisalabad. Methods: Different parameters like fluorescence, total proteins, TBA (thiobarbituric acid) method, periodateborohydride assay were used to check the effect of inhibitor on glycation. Thirty two combinations were made and all these combinations wereplaced at 37̊C, at same time for five weeks. 3mL of blood sample was drawn after 1st, 3rd and 5th week of incubation to perform the experimentsfor glycation and glycation inhibition. Along with the same temperature (37̊C), different combinations of glucose and inhibitor were used.Results: Effective concentration of inhibitor helped to decrease the level of glycation. All concentrations of glucose (G , G and G ) showed 1 2 3glycation with protein. The inhibitor Captopril (all concentrations) showed variations in inhibition of glycation at one temperature (37̊C) withdifferent parameters (Fluorescence, TBA and Periodate) but the most effective concentration of inhibitors at each condition is I (1mM) but I (10 3 1mM) and I (5 mM) were also equally effective after I . Periodate borohydride Assay is more effective for glycation determination than 2 3thiobarbituric acid assay. Conclusions: Captopril can be used as glycation inhibitor in future. As it enhances the activity of transketolase, it canproduce 3DG compound which can block the AGEs. However, more experimentations should be done on animal or on large scale before itsapplication in diabetic patients.
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3

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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4

West, Brett J., Shixin Deng, Akemi Uwaya, Fumiyuki Isami, Yumi Abe, Sho-ichi Yamagishi, and C. Jarakae Jensen. "Iridoids are natural glycation inhibitors." Glycoconjugate Journal 33, no. 4 (June 15, 2016): 671–81. http://dx.doi.org/10.1007/s10719-016-9695-x.

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5

Hosseini, Asieh, and Mohammad Abdollahi. "Diabetic Neuropathy and Oxidative Stress: Therapeutic Perspectives." Oxidative Medicine and Cellular Longevity 2013 (2013): 1–15. http://dx.doi.org/10.1155/2013/168039.

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Diabetic neuropathy (DN) is a widespread disabling disorder comprising peripheral nerves' damage. DN develops on a background of hyperglycemia and an entangled metabolic imbalance, mainly oxidative stress. The majority of related pathways like polyol, advanced glycation end products, poly-ADP-ribose polymerase, hexosamine, and protein kinase c all originated from initial oxidative stress. To date, no absolute cure for DN has been defined; although some drugs are conventionally used, much more can be found if all pathophysiological links with oxidative stress would be taken into account. In this paper, although current therapies for DN have been reviewed, we have mainly focused on the links between DN and oxidative stress and therapies on the horizon, such as inhibitors of protein kinase C, aldose reductase, and advanced glycation. With reference to oxidative stress and the related pathways, the following new drugs are under study such as taurine, acetyl-L-carnitine, alpha lipoic acid, protein kinase C inhibitor (ruboxistaurin), aldose reductase inhibitors (fidarestat, epalrestat, ranirestat), advanced glycation end product inhibitors (benfotiamine, aspirin, aminoguanidine), the hexosamine pathway inhibitor (benfotiamine), inhibitor of poly ADP-ribose polymerase (nicotinamide), and angiotensin-converting enzyme inhibitor (trandolapril). The development of modern drugs to treat DN is a real challenge and needs intensive long-term comparative trials.
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6

Julius, Angeline, and Waheeta Hopper. "INHIBITION OF ADVANCED GLYCATION END-PRODUCT FORMATION BY QUERCETIN AND CATECHIN: AN ALTERNATIVE THERAPY FOR TREATING DIABETIC COMPLICATIONS." Asian Journal of Pharmaceutical and Clinical Research 10, no. 11 (November 1, 2017): 173. http://dx.doi.org/10.22159/ajpcr.2017.v10i11.19412.

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Objective: The objective of this research was to determine early advanced glycation end-product (AGE) inhibition by natural aldose reductase inhibitors (ARIs), quercetin and catechin.Methods: The assay mixture (4 ml) consisted of 2 ml of 50 mM phosphate-buffered saline (pH 7.4), 50 μg/μl bovine serum albumin (BSA), and 2 mM glucose with or without the inhibitor. The test samples were treated with three different concentrations (10 mM, 20 mM, and 40 mM) of quercetin and catechin. High-throughput screening-based assay was adapted to perform the BSA-glucose test to determine the induction of AGE formation and its inhibition by quercetin, and catechin, using the fluorescence of the AGE-BSA sample at excitation and emission wavelengths of 350 and 450 nm.Result: The ARIs, quercetin and catechin inhibited early glycation with an inhibitory concentration value of 15.58 mM and 35.01 mM, respectively.Conclusion: The suppression of AGEs formation by natural inhibitors of aldose reductase would provide an alternative approach to the control of diabetic complications.
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7

Pervez, Humayun, Nazia Khan, Jamshed Iqbal, Sumera Zaib, Muhammad Yaqub, Muhammad Nawaz Tahir, and Muhammad Moazzam Naseer. "Synthesis, crystal structure, molecular docking studies and bio-evaluation of some N4-benzyl-substituted isatin- 3-thiosemicarbazones as urease and glycation inhibitors." Heterocyclic Communications 24, no. 1 (February 23, 2018): 51–58. http://dx.doi.org/10.1515/hc-2017-0148.

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Abstract Fifteen N4-benzyl-substituted isatin-3-thiosemicarbazones 5a–o were synthesized and evaluated for their urease and glycation inhibitory potential. Lemna aequinocitalis growth and Artemia salina assays were also done to determine their phytotoxic and toxic effects. All compounds are potent inhibitors of the urease enzyme, displaying inhibition [half maximal inhibitory concentration (IC50)=1.08±0.12–11.23±0.19 μm] superior to that of the reference inhibitor thiourea (IC50=22.3±1.12 μm). Compounds 5c, 5d, 5h, 5j,k are potent antiglycating agents, showing glycation inhibitory activity better than that of the reference inhibitor rutin (IC50 values 209.87±0.37–231.70±6.71 vs. 294.5±1.5 μm). In the phytotoxicity assay, 11 thiosemicarbazones 5a–d, 5g, 5h, 5j–l, 5n,o are active, demonstrating 5–100% growth inhibition of L. aequinocitalis at the highest tested concentrations (1000 or 500 μg/mL). In the brine shrimp (A. salina) lethality bioassay, three derivatives 5b, 5j and 5o are active with median lethal dose (LD50) values of 3.63×10−5, 2.90×10−5 and 2.31×10−4 m, respectively.
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8

Starowicz, Małgorzata, and Henryk Zieliński. "Inhibition of Advanced Glycation End-Product Formation by High Antioxidant-Leveled Spices Commonly Used in European Cuisine." Antioxidants 8, no. 4 (April 15, 2019): 100. http://dx.doi.org/10.3390/antiox8040100.

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Spices and herbs, as good sources of polyphenols, could be strong inhibitors of advanced glycation end-product (AGE) formation. The aim of this research was to measure the ability of various spices to inhibit AGEs and to study the correlation of AGE inhibition with total phenolic (TP) content and antioxidant capacity. Fourteen spices commonly used in European cuisine were extracted with a 50% ethanol solution, and their water and total phenolic contents and antioxidant capacities were examined. Antioxidant capacity was evaluated using three methods: (1) Measurement of the radical scavenging ability of 2,2’-azino-bis-(3-ethylbenzothiazoline-6-sulphonic acid) (ABTS) and (2) 2,2-diphenyl-1-picrylhydrazyl (DPPH●); and (3) photochemiluminescence (PCL) assay. Antiglycation properties were studied in vivo using two model systems: Bovine serum albumin-glucose (BSA-glucose) and bovine serum albumin-methylglyoxal (BSA-MGO). The most potent glycation inhibitors, according to the BSA-MGO assay, were star anise (88%), cinnamon (85%), allspice (81%), and cloves (79%), whereas in the BSA-glucose measurement, oregano was noted to be a very effective inhibitor of the glycation process. The ability to inhibit glycation was highly correlated with TP values in the BSA-MGO and BSA-glucose assay (r = 0.84 and 0.76, respectively). Our research showed the high antiglycation ability of cinnamon, cloves, and allspice, and we suggest, for the first time, that anise could also be considered a good glycation inhibitor.
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9

Rahbar, Samuel, and James L. Figarola. "Novel inhibitors of advanced glycation endproducts." Archives of Biochemistry and Biophysics 419, no. 1 (November 2003): 63–79. http://dx.doi.org/10.1016/j.abb.2003.08.009.

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10

Rahbar, Samuel, Kiran Kumar Yernini, Stephen Scott, Noe Gonzales, and Iraj Lalezari. "Novel Inhibitors of Advanced Glycation Endproducts." Biochemical and Biophysical Research Communications 262, no. 3 (September 1999): 651–56. http://dx.doi.org/10.1006/bbrc.1999.1275.

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11

Rahbar, Samuel, Kiran Kumar Yernini, Stephen Scott, Noe Gonzales, and Iraj Lalezari. "Novel Inhibitors of Advanced Glycation Endproducts." Biochemical and Biophysical Research Communications 264, no. 3 (November 1999): 1008. http://dx.doi.org/10.1006/bbrc.1999.1531.

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12

Hwang, Seung, Hyun Kim, Guanglei Zuo, Zhiqiang Wang, Jae-Yong Lee, and Soon Lim. "Anti-glycation, Carbonyl Trapping and Anti-inflammatory Activities of Chrysin Derivatives." Molecules 23, no. 7 (July 17, 2018): 1752. http://dx.doi.org/10.3390/molecules23071752.

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The aim of this study was searching anti-glycation, carbonyl trapping and anti-inflammatory activities of chrysin derivatives. The inhibitory effect of chrysin on advanced glycation end-products (AGEs) was investigated by trapping methylglyoxal (MGO), and MGO-conjugated adducts of chrysin were analyzed using LC-MS/MS. The mono- or di-MGO-conjugated adducts of chrysin were present at 63.86 and 29.69% upon 48 h of incubation at a chrysin:MGO ratio of 1:10. The MGO adducted positions on chrysin were at carbon 6 or 6 & 8 in the A ring by classic aldol condensation. To provide applicable knowledge for developing chrysin derivatives as AGE inhibitors, we synthesized several O-alkyl or ester derivatives of chrysin and compared their AGE formation inhibitory, anti-inflammatory, and water solubility characteristics. The results showed that 5,7-di-O-acetylchrysin possessed higher AGE inhibitory and water solubility qualities than original chrysin, and retained the anti-inflammation activity. These results suggested that 5,7-di-O-acetylchrysin could be a potent functional food ingredient as an AGE inhibitor and anti-inflammatory agent, and promotes the development of the use of chrysin in functional foods.
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13

Morimitsu, Yasujiro, Kazunari Yoshida, Sachiko Esaki, and Akira Hirota. "Protein Glycation Inhibitors from Thyme (Thymus vulgaris)." Bioscience, Biotechnology, and Biochemistry 59, no. 11 (January 1995): 2018–21. http://dx.doi.org/10.1271/bbb.59.2018.

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14

Ramkissoon, J. S., Fawzi M. Mahomoodally, Nessar Ahmed, and Hussein A. Subratty. "Natural inhibitors of advanced glycation end‐products." Nutrition & Food Science 42, no. 6 (October 26, 2012): 397–404. http://dx.doi.org/10.1108/00346651211277645.

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15

Rahbar, Samuel. "Novel inhibitors of glycation and AGE formation." Cell Biochemistry and Biophysics 48, no. 2-3 (April 25, 2007): 147–57. http://dx.doi.org/10.1007/s12013-007-0021-x.

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16

Perera, HKI, and HASK Ranasinghe. "A simple method to detect plant based inhibitors of glycation induced protein cross-linking." Asian Journal of Medical Sciences 6, no. 1 (July 24, 2014): 28–33. http://dx.doi.org/10.3126/ajms.v6i1.10181.

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Background: Glycation induced cross-linking of proteins are associated with chronic diabetic complications. Inhibition of protein glycation is one of the therapeutic approaches to prevent the progression of diabetic complications. Objective: Objective of this study was to establish a simple method to identify medicinal plants which can inhibit glycation induced protein cross-linking. Methods: Lysozyme was incubated at 37°C up to 4 weeks with different concentrations of glucose, fructose and ribose in sodium phosphate buffer (pH 7.4). Appropriate controls and blanks were carried out. Aminoguanidine (AG) was used as the standard inhibitor. Water extracts of Bryophyllum pinnatum leaves, Coriandrum sativum seed and Murraya koenigi leaves were used as potential inhibitors. Aliquots were removed from the incubation mixtures at intervals and analyzed for the presence of AGE induced protein cross-links, using SDS-PAGE. Appearance and the intensity of high molecular weight products were compared. Results: Extent of cross-linking was dependent on the sugar concentration. Cross-linking was slowest in the presence of glucose and fastest in the presence of ribose. AG inhibited glycation induced protein cross-linking in the presence of all three sugars. B. pinnatum leaves, C. sativum seeds and M. koenigi leaves inhibited protein cross-linking in the presence of sugar. This inhibition was greater than that of AG. Conclusions: We have established a simple SDS-PAGE method to identify medicinal plants which inhibit glycation induced protein cross-linking. We also demonstrated the effectiveness of B. pinnatum leaves, C. sativum seed and M. koenigi leaves in inhibiting glycation induced protein cross-linking in vitro. DOI: http://dx.doi.org/10.3126/ajms.v6i1.10181 Asian Journal of Medical Sciences Vol.6(1) 2015 28-33
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17

Zheng, Wenge, Huijuan Li, Yuyo Go, Xi Hui (Felicia) Chan, Qing Huang, and Jianxin Wu. "Research Advances on the Damage Mechanism of Skin Glycation and Related Inhibitors." Nutrients 14, no. 21 (November 1, 2022): 4588. http://dx.doi.org/10.3390/nu14214588.

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Our skin is an organ with the largest contact area between the human body and the external environment. Skin aging is affected directly by both endogenous factors and exogenous factors (e.g., UV exposure). Skin saccharification, a non-enzymatic reaction between proteins, e.g., dermal collagen and naturally occurring reducing sugars, is one of the basic root causes of endogenous skin aging. During the reaction, a series of complicated glycation products produced at different reaction stages and pathways are usually collectively referred to as advanced glycation end products (AGEs). AGEs cause cellular dysfunction through the modification of intracellular molecules and accumulate in tissues with aging. AGEs are also associated with a variety of age-related diseases, such as diabetes, cardiovascular disease, renal failure (uremia), and Alzheimer’s disease. AGEs accumulate in the skin with age and are amplified through exogenous factors, e.g., ultraviolet radiation, resulting in wrinkles, loss of elasticity, dull yellowing, and other skin problems. This article focuses on the damage mechanism of glucose and its glycation products on the skin by summarizing the biochemical characteristics, compositions, as well as processes of the production and elimination of AGEs. One of the important parts of this article would be to summarize the current AGEs inhibitors to gain insight into the anti-glycation mechanism of the skin and the development of promising natural products with anti-glycation effects.
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Olías, Raquel, Carmen Becerra-Rodríguez, Jorge R. Soliz-Rueda, F. Javier Moreno, Cristina Delgado-Andrade, and Alfonso Clemente. "Glycation affects differently the main soybean Bowman–Birk isoinhibitors, IBB1 and IBBD2, altering their antiproliferative properties against HT29 colon cancer cells." Food & Function 10, no. 9 (2019): 6193–202. http://dx.doi.org/10.1039/c9fo01421g.

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19

Price, David L., Patricia M. Rhett, Suzanne R. Thorpe, and John W. Baynes. "Chelating Activity of Advanced Glycation End-product Inhibitors." Journal of Biological Chemistry 276, no. 52 (October 24, 2001): 48967–72. http://dx.doi.org/10.1074/jbc.m108196200.

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20

Poornima, B., D. Anand Kumar, Bandi Siva, A. Venkanna, P. R. Rao Vadaparthi, K. Kumar, Ashok K. Tiwari, and K. Suresh Babu. "Advanced glycation end-products inhibitors isolated fromSchisandra grandiflora." Natural Product Research 30, no. 4 (March 27, 2015): 493–96. http://dx.doi.org/10.1080/14786419.2015.1024117.

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21

Rahbar, Samuel, Kiran Kumar Yerneni, Stephen Scott, Noe Gonzales, and Iraj Lalezari. "Novel Inhibitors of Advanced Glycation Endproducts (Part II)." Molecular Cell Biology Research Communications 3, no. 6 (June 2000): 360–66. http://dx.doi.org/10.1006/mcbr.2000.0239.

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22

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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23

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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Rabbani, Naila, and Paul J. Thornalley. "Emerging Glycation-Based Therapeutics—Glyoxalase 1 Inducers and Glyoxalase 1 Inhibitors." International Journal of Molecular Sciences 23, no. 5 (February 23, 2022): 2453. http://dx.doi.org/10.3390/ijms23052453.

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The abnormal accumulation of methylglyoxal (MG) leading to increased glycation of protein and DNA has emerged as an important metabolic stress, dicarbonyl stress, linked to aging, and disease. Increased MG glycation produces inactivation and misfolding of proteins, cell dysfunction, activation of the unfolded protein response, and related low-grade inflammation. Glycation of DNA and the spliceosome contribute to an antiproliferative and apoptotic response of high, cytotoxic levels of MG. Glyoxalase 1 (Glo1) of the glyoxalase system has a major role in the metabolism of MG. Small molecule inducers of Glo1, Glo1 inducers, have been developed to alleviate dicarbonyl stress as a prospective treatment for the prevention and early-stage reversal of type 2 diabetes and prevention of vascular complications of diabetes. The first clinical trial with the Glo1 inducer, trans-resveratrol and hesperetin combination (tRES-HESP)—a randomized, double-blind, placebo-controlled crossover phase 2A study for correction of insulin resistance in overweight and obese subjects, was completed successfully. tRES-HESP corrected insulin resistance, improved dysglycemia, and low-grade inflammation. Cell permeable Glo1 inhibitor prodrugs have been developed to induce severe dicarbonyl stress as a prospective treatment for cancer—particularly for high Glo1 expressing-related multidrug-resistant tumors. The prototype Glo1 inhibitor is prodrug S-p-bromobenzylglutathione cyclopentyl diester (BBGD). It has antitumor activity in vitro and in tumor-bearing mice in vivo. In the National Cancer Institute human tumor cell line screen, BBGD was most active against the glioblastoma SNB-19 cell line. Recently, potent antitumor activity was found in glioblastoma multiforme tumor-bearing mice. High Glo1 expression is a negative survival factor in chemotherapy of breast cancer where adjunct therapy with a Glo1 inhibitor may improve treatment outcomes. BBGD has not yet been evaluated clinically. Glycation by MG now appears to be a pathogenic process that may be pharmacologically manipulated for therapeutic outcomes of potentially important clinical impact.
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Velichkova, Stefaniya, Kenn Foubert, and Luc Pieters. "Natural Products as a Source of Inspiration for Novel Inhibitors of Advanced Glycation Endproducts (AGEs) Formation." Planta Medica 87, no. 10/11 (August 2021): 780–801. http://dx.doi.org/10.1055/a-1527-7611.

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AbstractProtein glycation, a post-translational modification found in biological systems, is often associated with a core defect in glucose metabolism. In particular, advanced glycation endproducts are complex heterogeneous sugar-derived protein modifications implicated in the progression of pathological conditions such as atherosclerosis, diabetic complications, skin diseases, rheumatism, hypertension, and neurodegenerative diseases. Undoubtedly, there is the need to expand the knowledge about antiglycation agents that can offer a therapeutic approach in preventing and treating health issues of high social and economic importance. Although various compounds have been under consideration, little data from clinical trials are available, and there is a lack of approved and registered antiglycation agents. Next to the search for novel synthetic advanced glycation endproduct inhibitors, more and more the efforts of scientists are focusing on researching antiglycation compounds from natural origin. The main purpose of this review is to provide a thorough overview of the state of scientific knowledge in the field of natural products from plant origin (e.g., extracts and pure compounds) as inhibitors of advanced glycation endproduct formation in the period between 1990 and 2019. Moreover, the objectives of the summary also include basic chemistry of AGEs formation and classification, pathophysiological significance of AGEs, mechanisms for inhibiting AGEs formation, and examples of several synthetic anti-AGEs drugs.
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Menzel, Ernst Johannes, and Roland Reihsner. "Comparison of the Effect of Different Inhibitors on the Non-Enzymatic Glycation of Rat Tail Tendons and Bovine Serum Albumin." Annals of Clinical Biochemistry: International Journal of Laboratory Medicine 33, no. 3 (May 1996): 241–48. http://dx.doi.org/10.1177/000456329603300311.

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The biomechanical and biochemical properties of collagen are changed by non-enzymatic glycation culminating in increased cross-linking. We have previously shown that dibasic amino acids such as L-arginine inhibit in vitro the non-enzymatic glycation of soluble proteins and insoluble connective tissue macromolecules. In the present in vitro study we obtained evidence that the nucleophilic hydrazine derivative aminoguanidine and the non-steroidal antirheumatic drug ibuprofen inhibit the formation of fluorescent advanced glycation end products (AGEs) to a comparable extent, while arginine is ineffective as a consequence of its tendency to form AGEs itself. Periodic replacement of glycated arginine in the rat tail tendon system, however, engendered an inhibition of fluorescence similar to that obtained by the other inhibitors. Long-term glycation of rat tail tendons caused a significant increase in Young's modulus, which could also be inhibited by periodically renewed arginine. In contrast to ibuprofen, aminoguanidine and arginine-lysine inhibited the marked increase in maximum contraction force of long-term glycated rat tail tendons. As opposed to other inhibitors, aminoguanidine also reduced the thermal contraction force of native tendons, shifted the maximum contraction temperature to markedly lower values and solubilized a significant part of the rat tail tendon collagen. These findings indicate that the in vitro alterations of rat tail tendon collagen induced by non-enzymatic glycation can be prevented by arginine, arginine-lysine and aminoguanidine. However, collagen structure is seriously affected by aminoguanidine.
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Matsuura, Nobuyasu, Tadashi Aradate, Chihiro Kurosaka, Makoto Ubukata, Shiho Kittaka, Yuri Nakaminami, Kanae Gamo, Hiroyuki Kojima, and Mitsuharu Ohara. "Potent Protein Glycation Inhibition of Plantagoside inPlantago majorSeeds." BioMed Research International 2014 (2014): 1–5. http://dx.doi.org/10.1155/2014/208539.

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Plantagoside (5,7,4′,5′-tetrahydroxyflavanone-3′-O-glucoside) and its aglycone (5,7,3′,4′,5′-pentahydroxyflavanone), isolated from a 50% ethanol extract ofPlantago majorseeds (Plantaginaceae), were established to be potent inhibitors of the Maillard reaction. These compounds also inhibited the formation of advanced glycation end products in proteins in physiological conditions and inhibited protein cross-linking glycation. These results indicate thatP. majorseeds have potential therapeutic applications in the prevention of diabetic complications.
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Frau, Juan, and Daniel Glossman-Mitnik. "Chemical Reactivity Theory Study of Advanced Glycation Endproduct Inhibitors." Molecules 22, no. 2 (February 2, 2017): 226. http://dx.doi.org/10.3390/molecules22020226.

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Chompoo, Jamnian, Atul Upadhyay, Wataru Kishimoto, Tadahiro Makise, and Shinkichi Tawata. "Advanced glycation end products inhibitors from Alpinia zerumbet rhizomes." Food Chemistry 129, no. 3 (December 2011): 709–15. http://dx.doi.org/10.1016/j.foodchem.2011.04.034.

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Khalifah, Raja G., John W. Baynes, and Billy G. Hudson. "Amadorins: Novel Post-Amadori Inhibitors of Advanced Glycation Reactions." Biochemical and Biophysical Research Communications 257, no. 2 (April 1999): 251–58. http://dx.doi.org/10.1006/bbrc.1999.0371.

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31

Abdel-Wahab, Y. H. A., F. P. M. O'Harte, C. R. Barnett, and P. R. Flatt. "Characterization of insulin glycation in insulin-secreting cells maintained in tissue culture." Journal of Endocrinology 152, no. 1 (January 1997): 59–67. http://dx.doi.org/10.1677/joe.0.1520059.

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Abstract Characteristics of cellular insulin glycation were examined in the pancreatic B-cell line, BRIN-BD11. The extent of insulin glycation increased stepwise during 72 h of culture at 5·6–33·3 mmol/l glucose, attaining levels up to 27%. Glycation of insulin at 33·3 mmol/l glucose was rapid, reaching maximal values within 2 h, and not readily reversible during 2 to 24 h of subsequent exposure to 5·6 mmol/l glucose. Glycated insulin was readily secreted by BRIN-BD11 cells upon active stimulation with glucose and other secretagogues. Cellular insulin glycation was decreased by 66–80% by inhibitors of protein glycation, vitamin C, aminoguanidine or acetylsalicylic acid. Modulation of insulin-secretory activity of BRIN-BD11 cells by co-culture at high glucose with diazoxide, l-alanine or glibenclamide indicated that long-term stimulation of secretion was associated with a decrease in the extent of insulin glycation. Glycation of insulin in vitro was substantially less extensive than in BRIN-BD11 cells, although glucose-6-phosphate and glyceraldehyde-3-phosphate were 1·4- to 2·0-fold more reactive than glucose per se. These observations indicate that insulin is readily glycated and secreted from insulin-secreting cells under hyperglycaemic conditions in culture. Journal of Endocrinology (1997) 152, 59–67
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Faruqui, Tabrez, Mohd Sajid Khan, Yusuf Akhter, Salman Khan, Zeeshan Rafi, Mohd Saeed, Ihn Han, Eun-Ha Choi, and Dharmendra Kumar Yadav. "RAGE Inhibitors for Targeted Therapy of Cancer: A Comprehensive Review." International Journal of Molecular Sciences 24, no. 1 (December 23, 2022): 266. http://dx.doi.org/10.3390/ijms24010266.

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The receptor for advanced glycation end products (RAGE) is a member of the immunoglobulin family that is overexpressed in several cancers. RAGE is highly expressed in the lung, and its expression increases proportionally at the site of inflammation. This receptor can bind a variety of ligands, including advanced glycation end products, high mobility group box 1, S100 proteins, adhesion molecules, complement components, advanced lipoxidation end products, lipopolysaccharides, and other molecules that mediate cellular responses related to acute and chronic inflammation. RAGE serves as an important node for the initiation and stimulation of cell stress and growth signaling mechanisms that promote carcinogenesis, tumor propagation, and metastatic potential. In this review, we discuss different aspects of RAGE and its prominent ligands implicated in cancer pathogenesis and describe current findings that provide insights into the significant role played by RAGE in cancer. Cancer development can be hindered by inhibiting the interaction of RAGE with its ligands, and this could provide an effective strategy for cancer treatment.
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Reddy, V. Prakash, Puspa Aryal, and Pallavi Soni. "RAGE Inhibitors in Neurodegenerative Diseases." Biomedicines 11, no. 4 (April 9, 2023): 1131. http://dx.doi.org/10.3390/biomedicines11041131.

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Nonenzymatic reactions of reducing sugars with primary amino groups of amino acids, proteins, and nucleic acids, followed by oxidative degradations would lead to the formation of advanced glycation endproducts (AGEs). The AGEs exert multifactorial effects on cell damage leading to the onset of neurological disorders. The interaction of AGEs with the receptors for advanced glycation endproducts (RAGE) contribute to the activation of intracellular signaling and the expression of the pro-inflammatory transcription factors and various inflammatory cytokines. This inflammatory signaling cascade is associated with various neurological diseases, including Alzheimer’s disease (AD), secondary effects of traumatic brain injury (TBI), amyotrophic lateral sclerosis (ALS), and diabetic neuropathy, and other AGE-related diseases, including diabetes and atherosclerosis. Furthermore, the imbalance of gut microbiota and intestinal inflammation are also associated with endothelial dysfunction, disrupted blood–brain barrier (BBB) and thereby the onset and progression of AD and other neurological diseases. AGEs and RAGE play an important role in altering the gut microbiota composition and thereby increase the gut permeability and affect the modulation of the immune-related cytokines. The inhibition of the AGE–RAGE interactions, through small molecule-based therapeutics, prevents the inflammatory cascade of events associated with AGE–RAGE interactions, and thereby attenuates the disease progression. Some of the RAGE antagonists, such as Azeliragon, are currently in clinical development for treating neurological diseases, including AD, although currently there have been no FDA-approved therapeutics based on the RAGE antagonists. This review outlines the AGE–RAGE interactions as a leading cause of the onset of neurological diseases and the current efforts on developing therapeutics for neurological diseases based on the RAGE antagonists.
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Perez Gutierrez, Rosa Martha. "Inhibition of Advanced Glycation End-Product Formation byOriganum majoranaL.In Vitroand in Streptozotocin-Induced Diabetic Rats." Evidence-Based Complementary and Alternative Medicine 2012 (2012): 1–8. http://dx.doi.org/10.1155/2012/598638.

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The development of AGE inhibitors is considered to have therapeutic potential in patients with diabetes diseases. The aim of the present study was investigate the effect of methanolic extract of the leaves ofOriganum majorana(OM) used as spice in many countries on AGEs formation.In vitrostudies indicated a significant inhibitory effects on the formation of AGEs. Their antiglycation activities were not only brought about by their antioxidant activities but also related to their trapping abilities of reactive carbonyl species such as methylglyoxal, an intermediate reactive carbonyl of AGE formation. The results demonstrate that OM have significant effects onin vitroAGE formation, and the glycation inhibitory activity was more effectively than those obtained using as standard antiglycation agent aminoguanidine. OM is a potent agent for protecting LDL against oxidation and glycation. Treatment of streptozotocin-diabetic mice with OM and glibenclamide for 28 days had beneficial effects on renal metabolic abnormalities including glucose level and AGEs formation. Diabetic mice showed increase in tail tendon collagen, glycated collagen linked fluorescence and reduction in pepsin digestion. Treatment with OM improved these parameters when compared to diabetic control and glibenclamide.
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Reddy, V. Prakash, Puspa Aryal, and Emmanuel K. Darkwah. "Advanced Glycation End Products in Health and Disease." Microorganisms 10, no. 9 (September 15, 2022): 1848. http://dx.doi.org/10.3390/microorganisms10091848.

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Advanced glycation end products (AGEs), formed through the nonenzymatic reaction of reducing sugars with the side-chain amino groups of lysine or arginine of proteins, followed by further glycoxidation reactions under oxidative stress conditions, are involved in the onset and exacerbation of a variety of diseases, including diabetes, atherosclerosis, and Alzheimer’s disease (AD) as well as in the secondary stages of traumatic brain injury (TBI). AGEs, in the form of intra- and interprotein crosslinks, deactivate various enzymes, exacerbating disease progression. The interactions of AGEs with the receptors for the AGEs (RAGE) also result in further downstream inflammatory cascade events. The overexpression of RAGE and the AGE-RAGE interactions are especially involved in cases of Alzheimer’s disease and other neurodegenerative diseases, including TBI and amyotrophic lateral sclerosis (ALS). Maillard reactions are also observed in the gut bacterial species. The protein aggregates found in the bacterial species resemble those of AD and Parkinson’s disease (PD), and AGE inhibitors increase the life span of the bacteria. Dietary AGEs alter the gut microbiota composition and elevate plasma glycosylation, thereby leading to systemic proinflammatory effects and endothelial dysfunction. There is emerging interest in developing AGE inhibitor and AGE breaker compounds to treat AGE-mediated pathologies, including diabetes and neurodegenerative diseases. Gut-microbiota-derived enzymes may also function as AGE-breaker biocatalysts. Thus, AGEs have a prominent role in the pathogenesis of various diseases, and the AGE inhibitor and AGE breaker approach may lead to novel therapeutic candidates.
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Papagiouvannis, Georgios, Panagiotis Theodosis-Nobelos, and Eleni Rekka. "Nipecotic Acid Derivatives as Potent Agents against Neurodegeneration: A Preliminary Study." Molecules 27, no. 20 (October 17, 2022): 6984. http://dx.doi.org/10.3390/molecules27206984.

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Alzheimer’s Disease (AD) is a common neurodegenerative disorder characterized by memory loss and cognitive impairment. Its pathology has not been fully clarified and therefore highly effective treatments have not been obtained yet. Almost all the current treatment options aim to alleviate only the symptoms and not to eliminate the disease itself. Acetylcholinesterase inhibitors are the main therapeutic agents against AD, whereas oxidative stress and inflammation have been found to be of great significance for the development and progression of neurodegeneration. In this work, ethyl nipecotate (ethyl-piperidine-3-carboxylate), a heterocyclic carboxylic acid derivative, which acts as a GABA reuptake inhibitor and has been used in research for diseases involving GABAergic neurotransmission dysfunction, was amidated with various carboxylic acids bearing antioxidant and/or anti-inflammatory properties (e.g., ferulic acid, sinapic acid, butylated hydroxycinnamic acid). Most of our compounds have significant antioxidant potency as lipid peroxidation inhibitors (IC50 as low as 20 μΜ), as oxidative protein glycation inhibitors (inhibition up to 57%), and act as DPPH reducing agents. Moreover, our compounds are moderate LOX inhibitors (up to 33% at 100 μΜ) and could reduce rat paw edema induced by carrageenan by up to 61%. Finally, some of them possessed inhibitory activity against acetylcholinesterase (IC50 as low as to 47 μΜ). Our results indicate that our compounds could have the potentiality for further optimization as multi-targeting agents directed against AD.
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37

S. Rahbar, Bentham Science Publisher, and Bentham Science Publisher J.L. Figarola. "Inhibitors and Breakers of Advanced Glycation Endproducts (AGEs): A Review." Current Medicinal Chemistry-Immunology, Endocrine & Metabolic Agents 2, no. 2 (June 1, 2002): 135–61. http://dx.doi.org/10.2174/1568013023358889.

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38

Fouotsa, Hugues, Alain Meli Lannang, Celine Djama Mbazoa, Saima Rasheed, Bishnu P. Marasini, Zulfiqar Ali, Krishna Prasad Devkota, et al. "Xanthones inhibitors of α-glucosidase and glycation from Garcinia nobilis." Phytochemistry Letters 5, no. 2 (June 2012): 236–39. http://dx.doi.org/10.1016/j.phytol.2012.01.002.

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39

Lee, Yeon Sil, Young-Hee Kang, Ju-Young Jung, Sanghyun Lee, Kazuo Ohuchi, Kuk Hyun Shin, Il-Jun Kang, Jung Han Yoon Park, Hyun-Kyung Shin, and Soon Sung Lim. "Protein Glycation Inhibitors from the Fruiting Body of Phellinus linteus." Biological & Pharmaceutical Bulletin 31, no. 10 (2008): 1968–72. http://dx.doi.org/10.1248/bpb.31.1968.

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40

Rahbar, Samuel, Rama Natarajan, KiranKumar Yerneni, Stephen Scott, Noe Gonzales, and Jerry L. Nadler. "Evidence that pioglitazone, metformin and pentoxifylline are inhibitors of glycation." Clinica Chimica Acta 301, no. 1-2 (November 2000): 65–77. http://dx.doi.org/10.1016/s0009-8981(00)00327-2.

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41

Sadowska-Bartosz, Izabela, and Grzegorz Bartosz. "Effect of glycation inhibitors on aging and age-related diseases." Mechanisms of Ageing and Development 160 (December 2016): 1–18. http://dx.doi.org/10.1016/j.mad.2016.09.006.

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42

Lehman, Trang D., and Beryl J. Ortwerth. "Inhibitors of advanced glycation end product-associated protein cross-linking." Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease 1535, no. 2 (February 2001): 110–19. http://dx.doi.org/10.1016/s0925-4439(00)00087-9.

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43

Pashikanti, Srinath, David R. de Alba, Gilbert A. Boissonneault, and Daniel Cervantes-Laurean. "Rutin metabolites: Novel inhibitors of nonoxidative advanced glycation end products." Free Radical Biology and Medicine 48, no. 5 (March 2010): 656–63. http://dx.doi.org/10.1016/j.freeradbiomed.2009.11.019.

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44

Anago, Eugénie, Guilphados Djogbede, Ezéchiel Mahougnon Salomon Fiogbe, Gaétan Augustin Julien Segbo, and Dèwanou Casimir Akpovi. "Rôle de la glycation des protéines dans les complications et la thérapie du diabète: revue bibliographique." International Journal of Biological and Chemical Sciences 16, no. 6 (March 12, 2023): 2930–44. http://dx.doi.org/10.4314/ijbcs.v16i6.37.

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La fixation d’un ose, fréquemment le glucose, sur les protéines est une réaction biochimique courante entraînant la formation des produits avancés de la glycation (en anglais Advanced Glycation Endproducts, AGEs). L’hyperglycémie permanente observée pendant le diabète, provoque une élévation du taux de glycation des protéines, avec pour conséquence une altération de leurs fonctions. Plusieurs auteurs ont montré le lien entre l’accumulation des AGEs dans différents organes et les complications microvasculaires et macrovasculaires observées lors du diabète. D’autres travaux ont montré que ces complications diabétiques et plusieurs autres maladies métaboliques découlent d’une série de processus délétères initiée par les AGEs. Il s’agit de l’inflammation par le biais des récepteurs, les modifications conformationnelles des macromolécules aboutissant à des accumulations d’agrégats et à une réponse immunitaire médiée par l’immunogénicité des AGEs. Les principales approches thérapeutiques pour le traitement du diabète impliquent l’administration d'insuline, l'inhibition des enzymes de digestion des polysaccharides (alpha-amylase et alpha-glucosidase) et les inhibiteurs de la glycation. Plusieurs travaux ont prouvé qu’un nombre important de plantes, herbes aromatiques et épices possèdent des propriétés antiglycatives très intéressantes et pourront être envisagées pour élargir la gamme des molécules thérapeutiques. The binding of a monosaccharide, frequently glucose, to proteins is a common biochemical reaction leading to the formation of advanced glycation end products (AGEs). The permanent hyperglycaemia observed during diabetes induces an increase in the glycation rate of proteins, with the consequent alteration of their functions. Several authors have demonstrated the link between the accumulation of AGEs in different organs and the microvascular and macrovascular complications observed in diabetes. Other work has shown that these diabetic complications and several other metabolic diseases stem from a series of deleterious processes initiated by AGEs. This is inflammation through receptors, conformational changes of macromolecules leading to accumulations of aggregates and an immune response mediated by the immunogenicity of AGEs. The main therapeutic approaches for the treatment of diabetes involve insulin administration, inhibition of polysaccharide digestion enzymes (alpha-amylase and alpha-glucosidase) and glycation inhibitors. Several works have proven that a large number of plants, aromatic herbs and spices have very interesting antiglycative properties and could be considered to expand the range of therapeutic molecules.
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Patil, Rahul S., Ashwini D. Jagdale, Megha L. Nalawade, Laxman N. Bavkar, and Akalpita U. Arvindekar. "GLYCATION INHIBITORS AND PROBIOTICS CAN AMELIORATE THE CHANGES CAUSED BY HIGH FRUCTOSE FEED." International Journal of Pharmacy and Pharmaceutical Sciences 10, no. 7 (July 1, 2018): 28. http://dx.doi.org/10.22159/ijpps.2018v10i7.26870.

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Objective: To evaluate the use of protein glycation inhibitors and probiotics to ameliorate secondary complications in diabetes and to improve gut microbiota respectively in high fructose fed Wistar rat.Methods: The study was conducted on male Wistar rats for 7 d. Blood glucose levels in oral glucose tolerance test (OGTT) were measured using glucometer, serum parameters were analyzed using commercial kits, antioxidant status was evaluated by measuring superoxide dismutase (SOD) and catalase (CAT) levels, total reactive oxygen species were estimated using a fluorescent 2’, 7’-dichlorofluorescin diacetate (DCF-DA) dye, and tissue fluorescence of liver, kidney and intestine were measured using a spectrofluorimeter.Results: OGTT pattern shows significant increase in blood glucose of fructose fed rats i.e. 154 mg/dl while, in aminoguanidine (AMG) treated and gut microbiota modulated animals it is 137 and 119 mg/dl resp. after 30 min on glucose administration. Marked reduction was found in SOD 6.37 and 11.25 mg/dl and catalase 186 and 65.5 mg/dl in liver and kidney of fructose fed animals when compared to fructose+AMG and fructose+EUGI. There is 5-6 fold significant increase in general and specific tissue fluorescence of liver and kidney, and 2.2 fold increase in liver reactive oxygen species was observed in fructose fed group as compare to control animals. Significantly higher glycation was found in intestine of fructose fed animals (general fluorescence 2.1 and specific fluorescence 3.1 AU/mg), more than that of diabetic control rats (general fluorescence 0.9 and specific fluorescence 1.6 AU/mg), represented an evidence for adverse impact of excess fructose on healthy gut.Conclusion: The use of protein glycation inhibitor and use of pre and probiotics significantly improved the serum parameters and would prevent progression to secondary complications.
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Haldipur, Ashrita C., and Nagarajan Srividya. "Multi-Mechanistic In Vitro Evaluation of Antihyperglycemic, Antioxidant and Antiglycation Activities of Three Phenolic-Rich Indian Red Rice Genotypes and In Silico Evaluation of Their Phenolic Metabolites." Foods 10, no. 11 (November 16, 2021): 2818. http://dx.doi.org/10.3390/foods10112818.

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The study evaluated the antidiabetic potential of three traditional Indian red rice genotypes/RR (Kattuyanam/KA, Chennangi/CH & Karungkuruvai/KU) using a combination of in vitro, metabolomics (Quadrupole-Time of Flight-Liquid chromatography-Mass spectrometry/Q-TOF-LC-MS/MS), and in silico techniques. In terms of antihyperglycemic potential, KA exhibited the highest inhibitory activity against α-amylase; CH against α-glucosidase; and KU against DPPIV and PTP1B enzymes. KA exhibited the highest antioxidant activity (DPPH, FRAP, and ABTS) and greater inhibition of protein glycation compared to other RR indicating its potential to mitigate diabetic complications. The metabolomic analysis confirmed the presence of 99 phenolics in the sample extracts (KU-71, KA-70, CH-68). Molecular docking studies revealed seven metabolites to be good inhibitors of the four target enzymes and activators of insulin receptor substrate/IRS. The antihyperglycemic and oxidation-glycation reduction composite index revealed KA to have the highest overall antidiabetic potential. Hence, the RR could be utilized in functional foods with a multi-barrelled strategy for diabetes prevention/management.
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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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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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48

Nurkolis, Fahrul, Keren Esther Kristina Mantik, Mury Kuswari, Fachruddin Perdana, Nelly Mayulu, Melvin Junior Tanner, Ariela Primalova, et al. "Sea Grape (Ceulerpa racemosa) Cereal with Addition of Tempe as an Anti-Aging Functional Food: In Vitro Study." Current Developments in Nutrition 5, Supplement_2 (June 2021): 41. http://dx.doi.org/10.1093/cdn/nzab033_041.

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Abstract Objectives This study aims to determine in vitro the effect of collagen size on anti-aging activity in the form of anti-glycation, tyrosinase inhibitors and antioxidant activity in order to obtain the optimum anti-aging collagen isolation technique from sea grape cereal with the addition of tempe. Methods Sample preparation by making cereals consisting of sea grape and tempe flour into powder using a Freeze Dryer (Lyovapor ™ L-200). Collagen isolation was carried out by varying the concentration of NaOH, which are 0.10 M; 0.20 M; and 0.30 M with a ratio of 1:10 (w/v) for 48 hours, followed by immersion using 1 M acetic acid with a ratio of 1:10 (w/v) for 24 hours. Collagen obtained from the best immersion treatment with NaOH solution is dissolved in distilled water with a ratio of 1 : 2 (v/v) and the size is changed with the help of a magnetic stirrer at a speed of 1000 rpm with a time variation of 5 and 10 hours. The results were then tested for particle size using a Particle Size Analyzer (PSA) and then tested for antioxidant activity using the DPPH (2,2-diphenyl-1-picrylhydrazyl) method, anti-glycation, and tyrosinase inhibitors. Selection of the best results is based on antioxidant, anti-glycation, and anti-tyrosinase activities. The data obtained from three replications were analyzed using ANOVA at a 95% confidence interval. Results Collagen isolated with 0.10 M NaOH was the collagen with the largest particle size, yield and anti-glycation respectively 2.45 µm, 11.65%, 62.76% and had the infrared spectrum that best matched the standard collagen. Furthermore, this collagen is stirred at a speed of 1000 rpm for 5 and 10 hours for size reduction. Collagen with 5 hours stirring has a smaller particle size (1482 nm) compared to 10 hours stirring (1568 nm). Collagen with a size of 1482 nm showed the best activity, namely antioxidant activity against (DPPH) of 24.70% and tyrosinase inhibitor of 26.77%. There was a significant difference (P < 0.05) in the DPPH inhibition test and the tyrosinase inhibition of L-DOPA substrates. Conclusions Based on the anti-glycation, anti-tyrosinase and antioxidant activity of collagen by immersing 0.10 M NaOH and stirring for 5 hours, it has the best anti-aging properties. This is useful for tests in determining variations of cereal formulations that will be used as functional food products rich in anti-aging collagen. Funding Sources Personal funding from author
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49

Vasarri, Marzia, Emanuela Barletta, Santina Vinci, Matteo Ramazzotti, Andrea Francesconi, Francesco Manetti, and Donatella Degl’Innocenti. "Annona cherimola Miller Fruit as a Promising Candidate against Diabetic Complications: An In Vitro Study and Preliminary Clinical Results." Foods 9, no. 10 (September 24, 2020): 1350. http://dx.doi.org/10.3390/foods9101350.

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Diabetes is a chronic metabolic disease with a strong social impact worldwide. Under chronic hyperglycemia, protein glycation strongly contributes to diabetes-related complications onset. Anti-glycation agents and inhibitors of α-glucosidase are often therapeutically used to control postprandial glycemia in order to prevent development of long-term diabetic complications. Given drug resistance and adverse effects of conventional antidiabetic therapies, the discovery of new effective and non-toxic naturally occurring compounds is needed to prevent and/or to manage life-threatening diabetic complications. Annona cherimola Miller fruit has been used in Mexican traditional medicine as natural remedy against diabetes. In this work, the in vitro anti-glycation and anti-α-glucosidase roles of Annona cherimola Miller pulp extract (CE) were investigated. Moreover, healthy and diabetic subjects were enrolled in a cross-over design intervention study aimed at investigating the effects of pulp intake on postprandial glycemia. This work shows that CE was able to inhibit albumin glycation in vitro and to inhibit α-glucosidase enzyme. Furthermore, the pulp intake did not contribute to an increase in postprandial glycemia, making it a suitable source of health-promoting phytonutrients and a potential functional food in diabetics and pre-diabetics diet.
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Saify, Zafar, Nighat Sultana, Nousheen Mushtaq, and Nazia Hasan. "(1H-Pyrrolo [2,3-B] Pyridine) 7-Azaindole as Cholinesterase/ Glycation Inhibitors." International Journal of Biochemistry Research & Review 4, no. 6 (January 10, 2014): 624–43. http://dx.doi.org/10.9734/ijbcrr/2014/9721.

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