Inhibition of advanced glycation endproduct formation by foodstuffs

Abstract

The Maillard reaction, which is generally termed nonenzymatic browning or glycation, has been implicated in accelerated aging and diabetic complications in vivo. Although the molecular basis of glycation-induced pathogenesis is not well understood, the following have been noted: (1) protein glycation leads to the formation and accumulation of toxic advanced glycation endproducts (AGEs); (2) AGEs can permanently alter the structure and function of body proteins; and (3) the interaction between AGE-modified proteins and AGE-specific receptors (RAGEs) on the cell surface induces the overproduction of reactive oxygen species (ROSs) and inflammatory mediators, which leads to cellular disorders in biological systems. To date, studies that have examined the contribution of protein glycation to disease-states have primarily focused on the deleterious effects and related mechanisms of these glycotoxins. However, it remains unknown whether phytochemicals exert protective effects against glycotoxin-induced damage. Thus, the development and investigation of AGE inhibitors, especially the natural anti-AGE agents without adverse effects, may provide a therapeutic approach for delaying and preventing premature aging and diabetic complications. In this review, we provide an outline of anti-glycation properties of foodstuffs and/or their active components, and discuss their mechanisms of action.

Komatsuna Seed Extracts Protection Against Amyloid β(1-42)-Induced Neuronal Cell Death

“…**p<0.01 compared with the controls. [23] shows that the Schiff base is oxidized in the first stage of glycation and it easily produces free radicals. These reactions increase the misfolding of the proteins such as Aβ in AD.…”

Aqueous extract of some indigenous medicinal plants inhibits glycation at multiple stages and protects erythrocytes from oxidative damage–an in vitro study

“…Inhibition of protein glycation is a complex process and glycation inhibitors may act by various mechanisms at different steps that can delay or prevent the glycation process, such as: i) at an early stage scavenging hydroxyl radicals and superoxide radicals and reducing the generation of reactive carbonyl or dicarbonyl groups, 2) during the glycation process, blocking the carbonyl or dicarbonyl groups in reducing sugars, Schiff bases or Amadori products, 3) metal ion chelation to inhibit AGE formation, 4) inhibiting the formation of latestage Amadori products, 5) breaking the crosslinking structures in the formed AGEs and 6) AGEs receptor (RAGE) blocking (Wu et al 2011). Based on this background, to completely elucidate the effect of 4 plant extracts at concentrations of physiological relevance on albumin glycation, its structural modifications and cellular effects; a series of experiments were performed in the present study.…”

Tailoring recombinant protein quality by rational media design

“…It was shown that betain inhibits glycation in vivo since it counteracted the elevation of reactive intermediate methylglyoxal and AGE levels in fructose-fed rat heart 146 . In a review of AGE inhibitors by foodstuffs, a great number of substances was identified including carnosine (a dipeptide: β-alanyl-L-histidine), curcumin (a diarylheptanoid), flavonoids, phenolic acids, and vitamins 147 . Hence, it is worthwhile to evaluate the applicability of these inhibitors in the frame of recombinant protein production from both a scientific and economic standpoint.…”