scholarly journals The Inhibitory Effect ofPrunella vulgarisL. on Aldose Reductase and Protein Glycation

2012 ◽  
Vol 2012 ◽  
pp. 1-7 ◽  
Author(s):  
Hong Mei Li ◽  
Jin Kyu Kim ◽  
Jai Man Jang ◽  
Sang Oh Kwon ◽  
Cheng Bi Cui ◽  
...  
Keyword(s):  
Aldose Reductase ◽  
Inhibitory Effect ◽  
Protein Glycation ◽  
Prunella Vulgaris ◽  
Inhibitory Effects ◽  
Advanced Glycation ◽  
High Concentration ◽  
Potent Inhibition ◽  
Glycation End Products

To evaluate the aldose reductase (AR) enzyme inhibitory ability ofPrunella vulgarisL. extract, six compounds were isolated and tested for their effects. The components were subjected toin vitrobioassays to investigate their inhibitory assays using rat lens aldose reductase (rAR) and human recombinant AR (rhAR). Among them, caffeic acid ethylene ester showed the potent inhibition, with the IC50values of rAR and rhAR at3.2±0.55 μM and12.58±0.32 μM, respectively. In the kinetic analyses using Lineweaver-Burk plots of 1/velocity and 1/concentration of substrate, this compound showed noncompetitive inhibition against rhAR. Furthermore, it inhibited galactitol formation in a rat lens incubated with a high concentration of galactose. Also it has antioxidative as well as advanced glycation end products (AGEs) inhibitory effects. As a result, this compound could be offered as a leading compound for further study as a new natural products drug for diabetic complications.

scholarly journals Inhibitory Activities ofStauntonia hexaphyllaLeaf Constituents on Rat Lens Aldose Reductase and Formation of Advanced Glycation End Products and Antioxidant

2017 ◽  
Vol 2017 ◽  
pp. 1-8 ◽  
Author(s):  
Seung Hwan Hwang ◽  
Shin Hwa Kwon ◽  
Set Byeol Kim ◽  
Soon Sung Lim
Keyword(s):  
Aldose Reductase ◽  
Advanced Glycation End Products ◽  
Inhibitory Activity ◽  
Solvent System ◽  
Inhibitory Effect ◽  
Advanced Glycation ◽  
Rat Lens Aldose Reductase ◽  
Glycation End Products ◽  
End Products ◽  
Etoac Fraction

Stauntonia hexaphylla(Thunb.) Decne. (Lardizabalaceae) leaves (SHL) have been used traditionally as analgesics, sedatives, diuretics, and so on, in China. To date, no data have been reported on the inhibitory effect of SHL and its constituents on rat lens aldose reductase (RLAR) and advanced glycation end products (AGEs). Therefore, the inhibitory effect of compounds isolated from SHL extract on RLAR and AGEs was investigated to evaluate potential treatments of diabetic complications. The ethyl acetate (EtOAC) fraction of SHL extract showed strong inhibitory activity on RLAR and AGEs; therefore, EtOAc fraction (3.0 g) was subjected to Sephadex LH-20 column chromatography, for further fractionation, with 100% MeOH solvent system to investigate its effect on RLAR and AGEs. Phytochemical investigation of SHL led to the isolation of seven compounds. Among the isolated compounds, chlorogenic acid, calceolarioside B, luteolin-3′-O-β-D-glucopyranoside, quercetin-3-O-β-D-glucopyranoside, and luteolin-7-O-β-D-glucopyranoside exhibited significant inhibitory activity against RLAR with IC50in the range of 7.34–23.99 μM. In addition, 3-(3,4-dihydroxyphenyl) propionic acid, neochlorogenic acid, and luteolin-3′-O-β-D-glucopyranoside exhibited the most potent inhibitory activity against formation of AGEs, with an IC50value of 115.07–184.06 μM, compared to the positive control aminoguanidine (820.44 μM). Based on these findings, SHL dietary supplements could be considered for the prevention and/or treatment of diabetes complication.

In vitro inhibition of protein glycation and advanced glycation end products formation by hydroethanolic extract and two fractions of Simaba trichilioides roots

2018 ◽  
Vol 34 (16) ◽  
pp. 2389-2393
Author(s):  
Bruno Pereira Motta ◽  
Anderson Kiyoshi Kaga ◽  
Juliana Oriel Oliveira ◽  
Maiara Destro Inacio ◽  
Cledson Ferreira da Silva ◽  
...  
Keyword(s):  
Advanced Glycation End Products ◽  
Protein Glycation ◽  
Advanced Glycation ◽  
Glycation End Products ◽  
End Products ◽  
In Vitro Inhibition ◽  
Hydroethanolic Extract

scholarly journals Resveratrol Prevents Dendritic Cell Maturation in Response to Advanced Glycation End Products

2013 ◽  
Vol 2013 ◽  
pp. 1-12 ◽  
Author(s):  
Brigitta Buttari ◽  
Elisabetta Profumo ◽  
Francesco Facchiano ◽  
Elif Inci Ozturk ◽  
Luca Segoni ◽  
...  
Keyword(s):  
Dendritic Cell ◽  
Advanced Glycation End Products ◽  
Map Kinases ◽  
Human Monocyte ◽  
Inhibitory Effect ◽  
The Body ◽  
Advanced Glycation ◽  
Glycation End Products ◽  
End Products

Advanced glycation end products (AGEs), generated through nonenzymatic glycosylation of proteins, lipids, and nucleic acids, accumulate in the body by age thus being considered as biomarkers of senescence. Senescence is characterized by a breakdown of immunological self-tolerance, resulting in increased reactivity to self-antigens. Previous findings suggest that AGE and its receptor RAGE may be involved in the pathogenesis of autoimmune reactions through dendritic cell (DC) activation. The aim of this study was to investigate whether resveratrol, a polyphenolic antioxidant compound with tolerogenic effects on DCs, was able to counteract the mechanisms triggered by AGE/RAGE interaction on DCs. By immunochemical and cytofluorimetric assays, we demonstrated thatin vitropretreatment of human monocyte-derived DCs with resveratrol prevents DC activation in response to glucose-treated albumin (AGE-albumin). We found that resveratrol exerts an inhibitory effect on DC surface maturation marker and RAGE up-regulation in response to AGE-albumin. It also inhibited proinflammatory cytokine expression, allostimulatory ability upregulation, mitogen-activated protein (MAP) kinases, and NF-κB activation in AGE-albumin-stimulated DCs. We suggest that resveratrol, by dismantling AGE/RAGE signaling on DCs may prevent or reduce increased reactivity to self-molecules in aging.

scholarly journals Inhibitory Effects of Hydroxysafflor Yellow A on the Formation of Advanced Glycation End Products in Vitro

2012 ◽  
Vol 35 (11) ◽  
pp. 2050-2053 ◽  
Author(s):  
Zhenzhen Ni ◽  
Zhengbing Zhuge ◽  
Wenlu Li ◽  
Huimin Xu ◽  
Zhongmiao Zhang ◽  
...  
Keyword(s):  
Advanced Glycation End Products ◽  
Inhibitory Effects ◽  
Hydroxysafflor Yellow A ◽  
Advanced Glycation ◽  
Glycation End Products ◽  
End Products

scholarly journals New Coumarinic Azo-Derivatives of Metoclopramide and Diphenhydramine: Synthesis and In Vitro Testing for Cholinesterase Inhibitory Effect and Protection Ability Against Chlorpyrifos

2020 ◽  
Vol 13 (1) ◽  
Author(s):  
Mahmood AAJ ◽  
Mustafa YS ◽  
Abdulstaar M
Keyword(s):  
Inhibitory Effect ◽  
Azo Compounds ◽  
Inhibitory Effects ◽  
High Concentration ◽  
Low Concentrations ◽  
Maximum Protection ◽  
Coumarin Compounds ◽  
New Compounds ◽  
Derivatives Of

Introduction: This study aims to synthesize new coumarin azo compounds of metoclopramide and diphenhydramine and to evaluate their in vitro cholinesterase inhibitory effects and protection abilities against chlorpyrifos. Methods: Two series of azo coumarin compounds were synthesized. Series I compound resulted from the diazotization of metoclopramide and then coupling with coumarin and 4-methyl coumarin to give compounds 1 and 2 respectively. Series II compound resulted from the diazotization of 7-aminocoumarin and 7-amino 4-methyl coumarin and then coupling with diphenhydramine to give compounds 3 and 4 respectively. The new compounds were tested for their in vitro cholinesterase inhibitory effect and protection ability against chlorpyrifos using the modified Elman electrometric method. Results: Metoclopramide derivatives with coumarin show selectivity protection for ChE against chlorpyriphos inhibitory effect as protect BChE and increase the inhibition of the AChE, or the opposite. Conclusion: Diphenhydramine derivatives with coumarin show more protective ability for both BChE and AChE as one of them shows the maximum protection for all concentration. However, the other derivative shows different manner as the low concentrations act as metoclopramide derivatives while the high concentration act as first diphenhydramine derivative (protect both AChE and BChE).

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