Eriodictyol and naringenin inhibit the formation of AGEs: An in vitro and molecular interaction study

Liu, Jianli; Yang, Zhijun; Cheng, Ye; Wu, Qiong; Yin, He; Li, Qijiu; Cao, Xiangyu

doi:10.1002/jmr.2814

Cited by 22 publications

(8 citation statements)

References 35 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Almost every change of lysine in glycated BSA with fructose was attributed to formation of carboxymethylysine (CML) [9]. On the other hand, the effect on albumin exposed to MGO caused a greater increase in fluorescence intensity, which is in line with other results [67,68]. The irreversible changes generated by glycation of MGO in BSA are highly selective for arginine residues, with some modifications of lysine and amino-terminal groups [69,70].…”

Section: Plos Onesupporting

confidence: 64%

Fructose and methylglyoxal-induced glycation alters structural and functional properties of salivary proteins, albumin and lysozyme

et al. 2022

View full text Add to dashboard Cite

Glycation process refers to reactions between reduction sugars and amino acids that can lead to formation of advanced glycation end products (AGEs) which are related to changes in chemical and functional properties of biological structures that accumulate during aging and diseases. The aim of this study was to perform and analyze in vitro glycation by fructose and methylglyoxal (MGO) using salivary fluid, albumin, lysozyme, and salivary α-amylase (sAA). Glycation effect was analyzed by biochemical and spectroscopic methods. The results were obtained by fluorescence analysis, infrared spectroscopy (total attenuated reflection—Fourier transform, ATR-FTIR) followed by multivariate analysis of principal components (PCA), protein profile, immunodetection, enzymatic activity and oxidative damage to proteins. Fluorescence increased in all glycated samples, except in saliva with fructose. The ATR-FTIR spectra and PCA analysis showed structural changes related to the vibrational mode of glycation of albumin, lysozyme, and salivary proteins. Glycation increased the relative molecular mass (Mr) in protein profile of albumin and lysozyme. Saliva showed a decrease in band intensity when glycated. The analysis of sAA immunoblotting indicated a relative reduction in intensity of its correspondent Mr after sAA glycation; and a decrease in its enzymatic activity was observed. Carbonylation levels increased in all glycated samples, except for saliva with fructose. Thiol content decreased only for glycated lysozyme and saliva with MGO. Therefore, glycation of salivary fluid and sAA may have the potential to identify products derived by glycation process. This opens perspectives for further studies on the use of saliva, an easy and non-invasive collection fluid, to monitor glycated proteins in the aging process and evolution of diseases.

show abstract

Section: Plos Onesupporting

confidence: 64%

Fructose and methylglyoxal-induced glycation alters structural and functional properties of salivary proteins, albumin and lysozyme

et al. 2022

View full text Add to dashboard Cite

show abstract

“…This result indicated that MGO not only directly damage cells, but also indirectly induce cell damage by the formation of AGEs [66] . Previous spectroscopy experiments in our laboratory showed that MGO and BSA can quickly generate AGEs [19,25] . Overexpression of AGEs receptors was also found in leukocytes exposed to MGO [67] .…”

Section: Resultsmentioning

confidence: 97%

“…Moreover, the results of previous studies in our laboratory have proved that the reaction between MGO and bovine serum albumin (BSA) could quickly generate AGEs [19,25] . Both the analysis of the transcriptome of HEK293 cells and the expression profile of HEK293 in the human protein atlas database showed that they had the ability to express kidney development [26,27] .…”

Section: Introductionmentioning

confidence: 96%

Potential Mechanisms of Methylglyoxal‐Induced Human Embryonic Kidney Cells Damage: Regulation of Oxidative Stress, DNA Damage, and Apoptosis

Liú

Cheng

Tang

et al. 2022

Chemistry & Biodiversity

Self Cite

View full text Add to dashboard Cite

Methylglyoxal (MGO) is a reactive carbonyl species that can cause cellular damage and is closely related to kidney disease, especially diabetic nephropathy. The toxic effect of MGO (0.5, 1, and 2 mM) on human embryonic kidney (HEK293) cells and its underlying mechanisms were explored in this study. Cell viability, apoptosis and the signaling pathways were measured with MTT, fluorescent staining and western blot experiments, the results showed that MGO could induce oxidative stress and cell inflammation, the level of reactive oxygen species (ROS) increased, and p38MAPK, JNK and NF‐κB signaling pathways were activated. Meanwhile, MGO also induced DNA damage. The expression of DNA oxidative damage marker 8‐hydroxy‐2’‐deoxyguanosine (8‐OHdG) increased, the expression of double‐strand break marker γH2AX increased significantly, and ATM/Chk2/p53 DNA damage response signaling pathway was activated. Furthermore, the expression of the receptor for advanced glycation end products (RAGE) also increased. Finally, mitochondrial membrane potential (MMP) decreased, fluorescence intensity of Hoechst33258 increased, and the protein expression ratio of Bax/Bcl‐2 increased significantly after the treatment of MGO. These results demonstrated that MGO might induce HEK293 cells damage by regulating oxidative stress, inflammation, DNA damage, and cell apoptosis, which revealed the specific mechanisms of MGO‐induced damage to HEK293 cells.

show abstract

“…These interaction results indicate that several facilitated glycation sites of BSA were occupied, thereby blocking or suppressing the formation of AGEs. A previous investigation also reported that eriodictyol and naringenin interact with BSA by hydrogen bonds and hydrophobic interactions to inhibit AGE formation (Liu et al ., 2020).…”

Section: Resultsmentioning

confidence: 99%

Phytochemical bioaccessibility and in vitro antidiabetic effects of Chinese sumac (Rhus chinensis Mill.) fruits after a simulated digestion: insights into the mechanisms with molecular docking analysis

Liu

et al. 2021

Int J of Food Sci Tech

View full text Add to dashboard Cite

This work studied the effects of gastrointestinal digestion on the phytochemical bioaccessibility and in vitro anti-diabetic effects of different fractions from Chinese sumac fruits and delineated the underlying mechanisms by molecular docking. Results showed that gastric digestion significantly increased the phytochemical bioaccessibility and inhibitions for a-glucosidase, dipeptidyl peptidase-4 (DPP-IV) and advanced glycation end product (AGE) formation of the ethanol-extracted fraction, whereas intestinal digestion remarkably decreased these parameters (P < 0.05). For the free phenolic fraction, the parameters were remarkably reduced after gastric digestion but significantly increased after intestinal digestion (P < 0.05). Quercitrin and gvajaverin contributed the most to the a-glucosidase and DPP-IV inhibitions, and trigalloyl glucose and its isomer could be the primary bioactive substance responsible for AGE suppression. Quercitrin, the predominant phenolic compound, could effectively interact with crucial amino acid residues in a-glucosidase, DPP-IV and bovine serum albumin with hydrogen bonds and hydrophobic interactions to exert its inhibitions.

show abstract

Eriodictyol and naringenin inhibit the formation of AGEs: An in vitro and molecular interaction study

Cited by 22 publications

References 35 publications

Fructose and methylglyoxal-induced glycation alters structural and functional properties of salivary proteins, albumin and lysozyme

Fructose and methylglyoxal-induced glycation alters structural and functional properties of salivary proteins, albumin and lysozyme

Potential Mechanisms of Methylglyoxal‐Induced Human Embryonic Kidney Cells Damage: Regulation of Oxidative Stress, DNA Damage, and Apoptosis

Phytochemical bioaccessibility and in vitro antidiabetic effects of Chinese sumac (Rhus chinensis Mill.) fruits after a simulated digestion: insights into the mechanisms with molecular docking analysis

Contact Info

Product

Resources

About