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Journal articles on the topic 'Glycation inhibitors'

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 (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 com

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2

E-FARAN, MISS GULL, MUHAMMAD ANJUM ZIA, and NIGHAT ASLAM. "EFFECT OF CAPTOPRIL." Professional Medical Journal 19, no. 01 (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 bl

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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 (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

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4

West, Brett J., Shixin Deng, Akemi Uwaya, et al. "Iridoids are natural glycation inhibitors." Glycoconjugate Journal 33, no. 4 (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 thi

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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 (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

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7

Pervez, Humayun, Nazia Khan, Jamshed Iqbal, et al. "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 (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 bet

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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 (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 ab

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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 (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 (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 (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 (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 knowle

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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 (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 (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 (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 (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. Aminoguani

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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 (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 c

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18

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 (2001): 48967–72. http://dx.doi.org/10.1074/jbc.m108196200.

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20

Poornima, B., D. Anand Kumar, Bandi Siva, et al. "Advanced glycation end-products inhibitors isolated fromSchisandra grandiflora." Natural Product Research 30, no. 4 (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 (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 (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

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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 (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 obtai

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24

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 (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 induc

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25

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 (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

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26

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 (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 inef

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27

Matsuura, Nobuyasu, Tadashi Aradate, Chihiro Kurosaka, et al. "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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28

Frau, Juan, and Daniel Glossman-Mitnik. "Chemical Reactivity Theory Study of Advanced Glycation Endproduct Inhibitors." Molecules 22, no. 2 (2017): 226. http://dx.doi.org/10.3390/molecules22020226.

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29

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 (2011): 709–15. http://dx.doi.org/10.1016/j.foodchem.2011.04.034.

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30

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 (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 (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 inhib

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32

Faruqui, Tabrez, Mohd Sajid Khan, Yusuf Akhter, et al. "RAGE Inhibitors for Targeted Therapy of Cancer: A Comprehensive Review." International Journal of Molecular Sciences 24, no. 1 (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 importa

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Reddy, V. Prakash, Puspa Aryal, and Pallavi Soni. "RAGE Inhibitors in Neurodegenerative Diseases." Biomedicines 11, no. 4 (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

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34

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 format

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35

Reddy, V. Prakash, Puspa Aryal, and Emmanuel K. Darkwah. "Advanced Glycation End Products in Health and Disease." Microorganisms 10, no. 9 (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 t

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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 (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

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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 (2002): 135–61. http://dx.doi.org/10.2174/1568013023358889.

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38

Fouotsa, Hugues, Alain Meli Lannang, Celine Djama Mbazoa та ін. "Xanthones inhibitors of α-glucosidase and glycation from Garcinia nobilis". Phytochemistry Letters 5, № 2 (2012): 236–39. http://dx.doi.org/10.1016/j.phytol.2012.01.002.

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Lee, Yeon Sil, Young-Hee Kang, Ju-Young Jung, et al. "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 (2000): 65–77. http://dx.doi.org/10.1016/s0009-8981(00)00327-2.

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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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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 (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 (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 (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 co

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45

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 (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

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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 (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 t

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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 (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-toxicolog

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Nurkolis, Fahrul, Keren Esther Kristina Mantik, Mury Kuswari, 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 (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, fol

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Vasarri, Marzia, Emanuela Barletta, Santina Vinci, et al. "Annona cherimola Miller Fruit as a Promising Candidate against Diabetic Complications: An In Vitro Study and Preliminary Clinical Results." Foods 9, no. 10 (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 comp

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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 (2014): 624–43. http://dx.doi.org/10.9734/ijbcrr/2014/9721.

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