Antioxidant balance and accumulation of advanced glycation end products after the consumption of standard diets including Maillard reaction products from silver carp peptides

2016 ◽  
Vol 7 (11) ◽  
pp. 4709-4719 ◽  
Author(s):  
Ye Yao ◽  
Kaining Han ◽  
Shiyuan Dong ◽  
Mingyong Zeng ◽  
Zunying Liu

The oxidative stress of diabetic mice fed on peptide MRPs with high AGE levels was aggravated, and the uptake of CML correlated with excretion but affected the accumulation in organs to a lesser extent.

2008 ◽  
Vol 28 (8) ◽  
pp. 1432-1438 ◽  
Author(s):  
Jun Su ◽  
Pamela A. Lucchesi ◽  
Romer A. Gonzalez-Villalobos ◽  
Desiree I. Palen ◽  
Bashir M. Rezk ◽  
...  

2021 ◽  
Author(s):  
Akio Nakamura ◽  
Ritsuko Kawahrada

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.


2010 ◽  
Vol 58 (20) ◽  
pp. 11119-11129 ◽  
Author(s):  
Deena Ramful ◽  
Evelyne Tarnus ◽  
Philippe Rondeau ◽  
Christine Robert Da Silva ◽  
Theeshan Bahorun ◽  
...  

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