The morbidity and mortality associated with diabetes is the result of the myriad complications related to the disease One of the most explored hypotheses to explain the onset of complications is a hyperglycemia-induced increase in oxidative stress Reactive oxygen species (ROS) are produced by oxidative phosphorylation, nicotinamide adenine dinucleotide phosphate oxidase (NADPH), xanthine oxidase, the uncoupling of lipoxygenases, cytochrome P450 monooxygenases, and glucose autoxidation Once formed, ROS deplete antioxidant defenses, rendering the affected cells and tissues more susceptible to oxidative damage Lipid, DNA, and protein are the cellular targets for oxidation, leading to changes in cellular structure and function Recent evidence suggests ROS are also important as second messengers in the regulation of intracellular signaling pathways and, ultimately, gene expression This review explores the production of ROS and the propagation and consequences of oxidative stress in diabetes

The role of oxidative stress in diabetic complications.

Maillard reactions lead to changes in food color, organoleptic properties, protein functionality, and protein digestibility Numerous different strategies for controlling Maillard reactions in foods have been attempted during the past decades In this paper, recent advances in strategies for controlling the Maillard reaction and subsequent downstream reaction products in food systems are critically reviewed The underlying mechanisms at play are presented, strengths and weaknesses of each strategy are discussed, and reasonable reaction mechanisms are proposed to reinforce the evaluations The review includes strategies involving addition of functional ingredients, such as plant polyphenols and vitamins, as well as enzymes The resulting trapping or modification of Maillard targets, reactive intermediates, and advanced glycation endproducts (AGEs) are presented with their potential unwanted side effects Finally, recent advances in processing for control of Maillard reactions are discussed

http://pubs.acs.org/doi/pdf/10.1021/acs.jafc.7b00882

Control of Maillard Reactions in Foods: Strategies and Chemical Mechanisms

http://morelife.org/references/full_papers/14568010.pdf

Novel inhibitors of advanced glycation endproducts

The formation and accumulation of methylglyoxal (MGO), a highly reactive dicarbonyl compound, has been implicated in the pathogenesis of type 2 diabetes, vascular complications of diabetes, and sev...

https://journals.physiology.org/doi/pdf/10.1152/physrev.00001.2019

Methylglyoxal, a highly reactive dicarbonyl compound, in diabetes, its vascular complications and other age-related diseases

The formation and accumulation of advanced glycation endproducts (AGEs) are related to diabetes and other age-related diseases. Methylglyoxal (MGO), a highly reactive dicarbonyl compound, is the major precursor in the formation of AGEs. MGO is mainly formed as a byproduct of glycolysis. Under physiological circumstances, MGO is detoxified by the glyoxalase system into D-lactate, with glyoxalase I (GLO1) as the key enzyme in the anti-glycation defence. New insights indicate that increased levels of MGO and the major MGO-derived AGE, methylglyoxal-derived hydroimidazolone 1 (MG-H1), and dysfunctioning of the glyoxalase system are linked to several age-related health problems, such as diabetes, cardiovascular disease, cancer and disorders of the central nervous system. The present review summarizes the mechanisms through which MGO is formed, its detoxification by the glyoxalase system and its effect on biochemical pathways in relation to the development of age-related diseases. Although several scavengers of MGO have been developed over the years, therapies to treat MGO-associated complications are not yet available for application in clinical practice. Small bioactive inducers of GLO1 can potentially form the basis for new treatment strategies for age-related disorders in which MGO plays a pivotal role.

The role of methylglyoxal and the glyoxalase system in diabetes and other age-related diseases.

http://www.morelife.org/references/full_papers/12051689.pdf

Effect of pyridoxamine on chemical modification of proteins by carbonyls in diabetic rats: characterization of a major product from the reaction of pyridoxamine and methylglyoxal

Anirudh Mally

Papers

Effect of pyridoxamine on chemical modification of proteins by carbonyls in diabetic rats: characterization of a major product from the reaction of pyridoxamine and methylglyoxal