scholarly journals Potent Protein Glycation Inhibition of Plantagoside inPlantago majorSeeds

2014 ◽  
Vol 2014 ◽  
pp. 1-5 ◽  
Author(s):  
Nobuyasu Matsuura ◽  
Tadashi Aradate ◽  
Chihiro Kurosaka ◽  
Makoto Ubukata ◽  
Shiho Kittaka ◽  
...  
Keyword(s):  
Maillard Reaction ◽  
Advanced Glycation End Products ◽  
Ethanol Extract ◽  
Protein Glycation ◽  
Cross Linking ◽  
Plantago Major ◽  
Advanced Glycation ◽  
Physiological Conditions ◽  
Glycation End Products ◽  
End Products

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.

scholarly journals Advanced Glycation End Products and Oxidative Stress in a Hyperglycaemic Environment

2021 ◽  
Author(s):  
Akio Nakamura ◽  
Ritsuko Kawahrada
Keyword(s):  
Oxidative Stress ◽  
Reactive Oxygen Species ◽  
Advanced Glycation End Products ◽  
Reactive Oxygen ◽  
Protein Glycation ◽  
Oxygen Species ◽  
Advanced Glycation ◽  
Glycation End Products ◽  
End Products ◽  
And Oxidative Stress

Protein glycation is the random, nonenzymatic reaction of sugar and protein induced by diabetes and ageing; this process is quite different from glycosylation mediated by the enzymatic reactions catalysed by glycosyltransferases. Schiff bases form advanced glycation end products (AGEs) via intermediates, such as Amadori compounds. Although these AGEs form various molecular species, only a few of their structures have been determined. AGEs bind to different AGE receptors on the cell membrane and transmit signals to the cell. Signal transduction via the receptor of AGEs produces reactive oxygen species in cells, and oxidative stress is responsible for the onset of diabetic complications. This chapter introduces the molecular mechanisms of disease onset due to oxidative stress, including reactive oxygen species, caused by AGEs generated by protein glycation in a hyperglycaemic environment.

scholarly journals Development of a novel Maillard reaction-based time–temperature indicator for monitoring the fluorescent AGE content in reheated foods

RSC Advances ◽  
2020 ◽  
Vol 10 (18) ◽  
pp. 10402-10410 ◽  
Author(s):  
Bei Hu ◽  
Lin Li ◽  
Yi Hu ◽  
Di Zhao ◽  
Yuting Li ◽  
...  
Keyword(s):  
Chronic Diseases ◽  
Maillard Reaction ◽  
Advanced Glycation End Products ◽  
Advanced Glycation ◽  
Glycation End Products ◽  
End Products

Dietary advanced glycation end products (AGEs) are formed via the Maillard reaction in foods, especially in reheated foods, and can cause chronic diseases.

Identification of advanced glycation end products of the Maillard reaction in Pick's disease

1996 ◽  
Vol 219 (2) ◽  
pp. 95-98 ◽  
Author(s):  
Takemi Kimura ◽  
Kazuyoshi Ikeda ◽  
Junichi Takamatsu ◽  
Toshio Miyata ◽  
Gen Sobue ◽  
...  
Keyword(s):  
Maillard Reaction ◽  
Advanced Glycation End Products ◽  
Pick's Disease ◽  
Pick’S Disease ◽  
Advanced Glycation ◽  
Glycation End Products ◽  
End Products

scholarly journals How Does Pyridoxamine Inhibit the Formation of Advanced Glycation End Products? The Role of Its Primary Antioxidant Activity

Antioxidants ◽  
2019 ◽  
Vol 8 (9) ◽  
pp. 344 ◽  
Author(s):  
Rafael Ramis ◽  
Joaquín Ortega-Castro ◽  
Carmen Caballero ◽  
Rodrigo Casasnovas ◽  
Antonia Cerrillo ◽  
...  
Keyword(s):  
Antioxidant Activity ◽  
Advanced Glycation End Products ◽  
Rate Constants ◽  
Protein Glycation ◽  
Diffusion Limit ◽  
Advanced Glycation ◽  
Hydrogen Atoms ◽  
Glycation End Products ◽  
End Products ◽  
Primary Antioxidant

Pyridoxamine, one of the natural forms of vitamin B6, is known to be an effective inhibitor of the formation of advanced glycation end products (AGEs), which are closely related to various human diseases. Pyridoxamine forms stable complexes with metal ions that catalyze the oxidative reactions taking place in the advanced stages of the protein glycation cascade. It also reacts with reactive carbonyl compounds generated as byproducts of protein glycation, thereby preventing further protein damage. We applied Density Functional Theory to study the primary antioxidant activity of pyridoxamine towards three oxygen-centered radicals (•OOH, •OOCH3 and •OCH3) to find out whether this activity may also play a crucial role in the context of protein glycation inhibition. Our results show that, at physiological pH, pyridoxamine can trap the •OCH3 radical, in both aqueous and lipidic media, with rate constants in the diffusion limit (>1.0 × 108 M - 1 s - 1 ). The quickest pathways involve the transfer of the hydrogen atoms from the protonated pyridine nitrogen, the protonated amino group or the phenolic group. Its reactivity towards •OOH and •OOCH3 is smaller, but pyridoxamine can still scavenge them with moderate rate constants in aqueous media. Since reactive oxygen species are also involved in the formation of AGEs, these results highlight that the antioxidant capacity of pyridoxamine is also relevant to explain its inhibitory role on the glycation process.

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