Prevention of Protein Glycation by Natural Compounds

Sadowska-Bartosz, Izabela; Bartosz, Grzegorz

doi:10.3390/molecules20023309

Cited by 130 publications

(94 citation statements)

References 122 publications

(134 reference statements)

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…Once initiated, AGEs formation continues throughout the lifespan of proteins, and cannot be reversed by normalizing hyperglycemia [2,4].…”

mentioning

confidence: 99%

“…The disease accounts for 90% of diabetes cases worldwide and is characterized by defects in glucose metabolism [1]. Persistently high blood glucose concentration encountered in diabetes often initiates Maillard reaction which causes nonenzymatic glycation of proteins and yields a plethora of reactive compounds called advanced glycation end products (AGEs) [2].Modification of protein structure and function by AGEs is consistent with the progression of diabetic complications and correlates positively with the severity of conditions like retinopathy, neuropathy, and nephropathy [3]. Once initiated, AGEs formation continues throughout the lifespan of proteins, and cannot be reversed by normalizing hyperglycemia [2,4].…”

mentioning

confidence: 99%

“…Persistently high blood glucose concentration encountered in diabetes often initiates Maillard reaction which causes nonenzymatic glycation of proteins and yields a plethora of reactive compounds called advanced glycation end products (AGEs) [2].…”

mentioning

confidence: 99%

See 2 more Smart Citations

Vitamin D prevents glycation of proteins: an in vitro study

2016

View full text Add to dashboard Cite

Human serum albumin (HSA) is an important protein involved in the transport of hormones, fatty acids, drugs, and other macromolecules. Under hyperglycemic conditions, this molecule undergoes irreversible modification that affects its structure and function. In this study, we explored the effect of two forms of vitamin D, a nutraceutical, on glycation modification in HSA. The protein was incubated with a physiologically high concentration of glucose in the presence of vitamin D metabolites. After 21 days, samples were tested for secondary structural changes, side chain modification, and the presence of advanced glycation end products. Vitamin D metabolites could reduce glycation modification, albeit only to a small extent. Interaction studies reveal that Vitamin D interaction with HSA can prevent protein glycation.Keywords: calcitriol; glycation; protein Type 2 Diabetes is a global health issue growing at an unprecedented rate. The disease accounts for 90% of diabetes cases worldwide and is characterized by defects in glucose metabolism [1]. Persistently high blood glucose concentration encountered in diabetes often initiates Maillard reaction which causes nonenzymatic glycation of proteins and yields a plethora of reactive compounds called advanced glycation end products (AGEs) [2].Modification of protein structure and function by AGEs is consistent with the progression of diabetic complications and correlates positively with the severity of conditions like retinopathy, neuropathy, and nephropathy [3]. Once initiated, AGEs formation continues throughout the lifespan of proteins, and cannot be reversed by normalizing hyperglycemia [2,4].Human serum albumin (HSA) frequently undergoes Maillard reaction to from covalently cross-linked composites [3]. In normal adults, 6-10% of lysine chains are modified by nonenzymatic glycation, however, this number increases by 2-3 folds in individuals suffering from diabetes [5]. This may interfere with HSA function [5]. Since HSA is involved in the transportation of several moieties: nutrients, steroids, and a wide variety of drugs this can have detrimental physiological effects [6].Research suggests that vitamin D is involved in controlling AGE-associated damage in both diabetes and heart disorders [7]. Vitamin D is a fat-soluble micronutrient which is produced in the body by UV irradiation of a precursor steroid stored in the skin. The functionally active form of vitamin D, calcitriol, has a wide array of health implications [8]. Multiple studies have demonstrated its ability in limiting oxidative damage and regulating the status of a potent cellular antioxidant-reduced glutathione (GSH) [7]. Vitamin D deficiency is thought to be a risk factor for the development of diabetes; Low vitamin D status is associated with increased insulin resistance, glycated hemoglobin (HbA1c), and AGE formation [9][10][11]. Previous reports have correlated low circulating concentrations of vitamin D with increased risk of diabetic macrovascular and microvascular complications: mainly nephropathy a...

show abstract

“…Once initiated, AGEs formation continues throughout the lifespan of proteins, and cannot be reversed by normalizing hyperglycemia [2,4].…”

mentioning

confidence: 99%

mentioning

confidence: 99%

See 1 more Smart Citation

Vitamin D prevents glycation of proteins: an in vitro study

2016

View full text Add to dashboard Cite

show abstract

“…Some of the artificial and natural compounds have been used as antiglycating agent (Rahbar and Figarola, 2003). Antioxidants have been also shown to be effective partially in preventing the glycation mediated damage to biomolecules (Sadowska-Bartosz and Bartosz, 2015).…”

Section: Discussionmentioning

confidence: 99%

Reversal of glycoxidative damage of DNA and protein by antioxidants

Jha¹,

Momin²,

Kumar³

et al. 2018

View full text Add to dashboard Cite

Diabetes is a metabolic and endocrinological disorder. It is a manifestation of hyperglycemia and glucotoxicity for a long period of time. The high glucose concentra tion leads to secondary complications of diabetes like cataract, cardiovascular and, neurological disorders. The reactive carbonyl group of glucose reacts with amino groups of biomolecules like DNA and proteins leading to their structu ral altera tions. In the present study, effect of non-enzymatic glycation was checked on proteins and the structure of DNA. It was observed that there was an increase in the generation of early and advanced glycation products when BSA was incubated with methylglyoxal. There wa s a decrease in the amount of glycation products in the presence of most of the antioxidants except sodium acetate. The glycation system caused strand breakage and led to change in the conformation of pBR322 plasmid, from supercoiled to open circular. This structural damage of DNA increased in the presence of FeCl 3 , indicating the role of metal ions in the generation of free radicals. Antioxidants like sodium azide, eugenol and melatonin significantly reversed the DNA damage, induced by glycation system, as shown by agarose gel electrophoresis. Eugenol and mannitol were able to show significantly high percentage of DPPH inhibition and ABTS, as compared to sodium acetate and sodium azide. The amount of eugenol and mannitol used were able to show similar antioxidant capacity, as compared to 50 µg of vitamin C, a standard and potent antioxidant. It can be concluded from this study that generation of free radicals is the major rou te for glycation-induced DNA dama ge as shown by the reversal of damage in the presence of antioxidants. The study indicates the significance of natural antioxidants in the prevention of glycation related diseases.

show abstract

“…The rearrangement of Schiff base produces Amadori products that undergo rearrangements to form stable AGEs. This reaction is called Maillard reaction [5]. The formation of dicarbonyls such as 3-deoxyglucosone, methylglyoxal (MGO) and glyoxal occur in early glycation.…”

Section: Introductionmentioning

confidence: 99%

Inhibition of Advanced Glycation End-Product Formation by Quercetin and Catechin: An Alternative Therapy for Treating Diabetic Complications

Julius

Hopper

2017

Asian J Pharm Clin Res

View full text Add to dashboard Cite

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 formation and its inhibition by quercetin, and catechin, using the fluorescence of the AGE-BSA sample at excitation and emission wavelengths of 350 and 450 nm. Result:The ARIs, quercetin and catechin inhibited early glycation with an inhibitory concentration value of 15.58 mM and 35.01 mM, respectively. Conclusion:The suppression of AGEs formation by natural inhibitors of aldose reductase would provide an alternative approach to the control of diabetic complications.

show abstract

Prevention of Protein Glycation by Natural Compounds

Cited by 130 publications

References 122 publications

Vitamin D prevents glycation of proteins: an in vitro study

Vitamin D prevents glycation of proteins: an in vitro study

Reversal of glycoxidative damage of DNA and protein by antioxidants

Inhibition of Advanced Glycation End-Product Formation by Quercetin and Catechin: An Alternative Therapy for Treating Diabetic Complications

Contact Info

Product

Resources

About