scholarly journals Health Promoting Effect of Phyllanthus emblica and Azadiractha indica against Advanced Glycation End Products Formation

2021 ◽  
Vol 11 (19) ◽  
pp. 8819
Author(s):  
Mohammed A. Alsahli ◽  
Shehwaz Anwar ◽  
Faisal M. Alzahrani ◽  
Ahmad Almatroudi ◽  
Hani Alfheeaid ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Advanced Glycation End Products ◽  
Structural Changes ◽  
Therapeutic Potential ◽  
Health Problems ◽  
Phyllanthus Emblica ◽  
Advanced Glycation ◽  
Glycation End Products ◽  
End Products

Oxidative stress is linked with inflammation, diabetic complications, and advanced glycation end products formation. Intake of flavonoid-rich foods has been reported to have a beneficial effect on human health. The aim of this study was to verify the therapeutic potential of Phyllanthusemblica and Azadiractha indica against glycation and other oxidative stress-induced complications such as inflammation using in vitro study. Ethanol extracts of Phyllanthus emblica fruit pulp and dried leaf of Azadiractha indica were prepared to investigate in vitro anti-inflammatory and anti-glycating potentials. In a DPPH assay, the EC50 value of extract of P. emblica and A. indica was found to be 1532.36 ± 0.17 and 1380.61 ± 0.27 µg/mL, respectively. The FRAP value of P. emblica and A. indica extract was 86.6 and 32.12 µg ascorbic acid/100 mg dry weight of the extract. The maximum percentage of H2O2 scavenging activity was 71.30% and 67.38%, respectively. Extracts of P. emblica and A. indica showed maximum inhibition of heat-induced BSA denaturation by 62.42% and 53.00%, heat-induced denaturation of egg albumin, by 50.84%% and 44.31%, and heat-induced hemolysis by 54.44% and 50.21%. Both extracts (600 µg/mL) significantly reduced the browning, structural changes, aggregation, and AGEs formation. Our biophysical studies confirmed the AGEs formation was inhibiting the potential of extracts. Thus, our findings confirm that these extracts are a rich source of antioxidants and may be utilized to prevent the oxidative stress-induced destruction of biomolecules, glycation, and in the therapy of a variety of health problems, including inflammation. Further, a combination of extracts of P. emblica and A. indica may be extremely useful in preventing and treating health problems.

Advanced glycation end products and the kidney

2005 ◽  
Vol 289 (4) ◽  
pp. F645-F659 ◽  
Author(s):  
Jürgen M. Bohlender ◽  
Sybille Franke ◽  
Günter Stein ◽  
Gunter Wolf
Keyword(s):  
Advanced Glycation End Products ◽  
Structural Changes ◽  
Therapeutic Potential ◽  
Interstitial Fibrosis ◽  
Basement Membranes ◽  
Renal Diseases ◽  
Advanced Glycation ◽  
Tubular Atrophy ◽  
Glycation End Products ◽  
End Products

Advanced glycation end products (AGEs) are a heterogeneous group of protein and lipids to which sugar residues are covalently bound. AGE formation is increased in situations with hyperglycemia (e.g., diabetes mellitus) and is also stimulated by oxidative stress, for example in uremia. It appears that activation of the renin-angiotensin system may contribute to AGE formation through various mechanisms. Although AGEs could nonspecifically bind to basement membranes and modify their properties, they also induce specific cellular responses including the release of profibrogenic and proinflammatory cytokines by interacting with the receptor for AGE (RAGE). However, additional receptors could bind AGEs, adding to the complexity of this system. The kidney is both: culprit and target of AGEs. A decrease in renal function increases circulating AGE concentrations by reduced clearance as well as increased formation. On the other hand, AGEs are involved in the structural changes of progressive nephropathies such as glomerulosclerosis, interstitial fibrosis, and tubular atrophy. These effects are most prominent in diabetic nephropathy, but they also contribute to renal pathophysiology in other nondiabetic renal diseases. Interference with AGE formation has therapeutic potential for preventing the progression of chronic renal diseases, as shown from data of animal experiments and, more recently, the first clinical trials.

scholarly journals Effect of dicarbonyl-induced browning on alpha-crystallin chaperone-like activity: physiological significance and caveats of in vitro aggregation assays

2004 ◽  
Vol 379 (2) ◽  
pp. 273-282 ◽  
Author(s):  
M. Satish KUMAR ◽  
P. Yadagiri REDDY ◽  
P. Anil KUMAR ◽  
Ira SUROLIA ◽  
G. Bhanuprakash REDDY
Keyword(s):  
Advanced Glycation End Products ◽  
Molecular Chaperone ◽  
Structural Changes ◽  
Surface Hydrophobicity ◽  
Enzyme Inactivation ◽  
Advanced Glycation ◽  
Glycation End Products ◽  
End Products ◽  
Enzymic Browning

α-Crystallin is a member of the small heat-shock protein family and functions like a molecular chaperone, and may thus help in maintaining the transparency of the eye lens by protecting the lens proteins from various stress conditions. Non-enzymic glycation of long-lived proteins has been implicated in several age- and diabetes-related complications, including cataract. Dicarbonyl compounds such as methylglyoxal and glyoxal have been identified as the predominant source for the formation of advanced glycation end-products in various tissues including the lens. We have investigated the effect of non-enzymic browning of α-crystallin by reactive dicarbonyls on its molecular chaperone-like function. Non-enzymic browning of bovine α-crystallin in vitro caused, along with altered secondary and tertiary structures, cross-linking and high-molecular-mass aggregation. Notwithstanding these structural changes, methylglyoxal- and glyoxal-modified α-crystallin showed enhanced anti-aggregation activity in various in vitro aggregation assays. Paradoxically, increased chaperone-like activity of modified α-crystallin was not associated with increased surface hydrophobicity and rather showed less 8-anilinonaphthalene-l-sulphonic acid binding. In contrast, the chaperone-like function of modified α-crystallin was found to be reduced in assays that monitor the prevention of enzyme inactivation by UV-B and heat. Moreover, incubation of bovine lens with methylglyoxal in organ culture resulted in cataract formation with accumulation of advanced glycation end-products and recovery of α-crystallin in high proportions in the insoluble fraction. Furthermore, soluble α-crystallin from methylglyoxal-treated lenses showed decreased chaperone-like activity. Thus, in addition to describing the effects of methylglyoxal and glyoxal on structure and chaperone-like activity, our studies also bring out an important caveat of aggregation assays in the context of the chaperone function of α-crystallin.

scholarly journals Protective Effects of Kaempferitrin on Advanced Glycation End Products Induce Mesangial Cell Apoptosis and Oxidative Stress

2018 ◽  
Vol 19 (11) ◽  
pp. 3334 ◽  
Author(s):  
Wenxian Jiang ◽  
Rongshen Wang ◽  
Di Liu ◽  
Min Zuo ◽  
Chunzhen Zhao ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Membrane Potential ◽  
Mitochondrial Membrane Potential ◽  
Advanced Glycation End Products ◽  
Mitochondrial Membrane ◽  
Glomerular Mesangial Cells ◽  
Advanced Glycation ◽  
Glycation End Products ◽  
End Products

Advanced glycation end products (AGEs) and the receptor for AGEs (RAGE) both play important roles in diabetic nephropathy (DN). Previous studies have identified glomerular mesangial cells (GMCs) injury as a key early risk factor in the development of DN. Kaempferitrin (KM) is a potent antioxidant with hypoglycemic action. Although KM is known to protect against AGE-induced damage in GMCs, the effects and the mechanisms by which they occur are poorly understood. In this study, cultured rat GMCs were exposed to AGE-induced oxidative stress (OS) to model DN in vitro. Reactive oxygen species (ROS) was analyzed by 2′,7′-dichlorofluorescin diacetate (DCFH-DA). Superoxide dismutase (SOD) and malondialdehyde (MDA) were studied using commercial kits. Mitochondrial membrane potential (Δψm) was measured by rhodamine 123. Hoechst 33258 and annexin V and propidium iodide (PI) double staining were performed to observe the apoptosis states in GMCs, whereas apoptosis and protective mechanism in AGE-induced GMCs were investigated by Western blot. The data revealed that KM effectively increased SOD activity, decreased MDA levels, suppressed ROS generation, and protected against OS in AGE-induced GMCs. Treatment with KM also inhibited the expression of collagen IV and transforming growth factor-β1 (TGF-β1), improved mitochondrial membrane potential recovery, and suppressed the mitochondrial/cytochrome c-mediated apoptosis pathway through the expression of anti-apoptotic factors in GMCs in vitro. These findings suggest that KM may be a new potential agent in the treatment of DN in future.

Sulforaphane inhibits formation of advanced glycation end products in vitro

2014 ◽  
Vol 1 (e1) ◽  
pp. 001-001 ◽  
Author(s):  
Kei Fukami ◽  
Takanori Matsui ◽  
Sho-ichi Yamagishi
Keyword(s):  
Advanced Glycation End Products ◽  
Advanced Glycation ◽  
Glycation End Products ◽  
End Products
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