Protein Glycation

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Sirichai Adisakwattana - One of the best experts on this subject based on the ideXlab platform.

  • RESEARCH ARTICLE Protective Effects of Ferulic Acid on High Glucose-Induced Protein Glycation, Lipid Peroxidation, and Membrane Ion Pump
    2016
    Co-Authors: Activity In Human Erythrocytes, Weerachat Sompong, Henrique Cheng, Sirichai Adisakwattana
    Abstract:

    Ferulic acid (FA) is the ubiquitous phytochemical phenolic derivative of cinnamic acid. Ex-perimental studies in diabetic models demonstrate that FA possesses multiple mechanisms of action associated with anti-hyperglycemic activity. The mechanism by which FA prevents diabetes-associated vascular damages remains unknown. The aim of study was to investi-gate the protective effects of FA on Protein Glycation, lipid peroxidation, membrane ion pump activity, and phosphatidylserine exposure in high glucose-exposed human erythro-cytes. Our results demonstrated that FA (10-100 μM) significantly reduced the levels of gly-cated hemoglobin (HbA1c) whereas 0.1-100 μM concentrations inhibited lipid peroxidation in erythrocytes exposed to 45 mM glucose. This was associated with increased glucose consumption. High glucose treatment also caused a significant reduction in Na+/K+-ATPase activity in the erythrocyte plasma membrane which could be reversed by FA. Furthermore, we found that FA (0.1-100 μM) prevented high glucose-induced phosphatidylserine expo-sure. These findings provide insights into a novel mechanism of FA for the prevention of vascular dysfunction associated with diabetes

  • cyanidin 3 rutinoside attenuates methylglyoxal induced Protein Glycation and dna damage via carbonyl trapping ability and scavenging reactive oxygen species
    BMC Complementary and Alternative Medicine, 2016
    Co-Authors: Thavaree Thilavech, Sathaporn Ngamukote, Damien P Belobrajdic, Mahinda Y Abeywardena, Sirichai Adisakwattana
    Abstract:

    Advanced Glycation end-products (AGEs) play a significant role in the development and progression of vascular complication in diabetes. Anthocyanin has been recently reported to possess antiglycating activity. This study aimed to determine whether a naturally occurring anthocyanin, cyanidin-3-rutinoside (C3R) inhibits methylglyoxal (MG) induced Protein Glycation and oxidative Protein and DNA damage. C3R (0.125–1 mM) was incubated with bovine serum albumin and MG (1 mM) for 2 weeks. The formation of fluorescent AGEs was measured by using spectrofluorometer and thiol group content were used to detect Protein oxidative damage. Gel electrophoresis was used to determine whether C3R (0.125–1 mM) reduced DNA strand breakage in a Glycation model comprising lysine, MG and/or Cu2+. The generation of superoxide anions and hydroxyl radicals were detected by the cytochrome c reduction assay and the thiobarbituric acid reactive substances assay. MG-trapping capacity was assessed by high performance liquid chromatography (HPLC). C3R (0.25–1 mM) reduced the formation of fluorescent AGEs and depleted Protein thiol groups in bovine serum albumin mediated by MG. At 1 mM C3R inhibited oxidative DNA damage in the Glycation model (p < 0.05) and at 0.5–1 mM prevented Cu2+ induced DNA strand breakage in the presence of lysine and MG. The findings showed that C3R reduced the formation of superoxide anion and hydroxyl radicals during the Glycation reaction of MG with lysine. C3R directly trapped MG in a concentration and time dependent manner (both p < 0.001). These findings suggest that C3R protects against MG-induced Protein Glycation and oxidative damage to Protein and DNA by scavenging free radicals and trapping MG.

  • protective effects of ferulic acid on high glucose induced Protein Glycation lipid peroxidation and membrane ion pump activity in human erythrocytes
    PLOS ONE, 2015
    Co-Authors: Weerachat Sompong, Henrique Cheng, Sirichai Adisakwattana
    Abstract:

    Ferulic acid (FA) is the ubiquitous phytochemical phenolic derivative of cinnamic acid. Experimental studies in diabetic models demonstrate that FA possesses multiple mechanisms of action associated with anti-hyperglycemic activity. The mechanism by which FA prevents diabetes-associated vascular damages remains unknown. The aim of study was to investigate the protective effects of FA on Protein Glycation, lipid peroxidation, membrane ion pump activity, and phosphatidylserine exposure in high glucose-exposed human erythrocytes. Our results demonstrated that FA (10-100 μM) significantly reduced the levels of glycated hemoglobin (HbA1c) whereas 0.1-100 μM concentrations inhibited lipid peroxidation in erythrocytes exposed to 45 mM glucose. This was associated with increased glucose consumption. High glucose treatment also caused a significant reduction in Na+/K+-ATPase activity in the erythrocyte plasma membrane which could be reversed by FA. Furthermore, we found that FA (0.1-100 μM) prevented high glucose-induced phosphatidylserine exposure. These findings provide insights into a novel mechanism of FA for the prevention of vascular dysfunction associated with diabetes.

  • Protein Glycation inhibitory activity and antioxidant capacity of clove extract
    Journal of Food Science and Technology, 2015
    Co-Authors: Tanyawan Suantawee, Krittaporn Wesarachanon, Kanokphat Anantsuphasak, Tanuch Daenphetploy, Sroshin Thien-ngern, Thavaree Thilavech, Porntip Pasukamonset, Sathaporn Ngamukote, Sirichai Adisakwattana
    Abstract:

    Syzygium aromaticum (L.) (clove) is one of the most widely cultivated spices in many tropical countries. The aim of this study was to determine the phytochemical content, the antioxidant properties and the antiGlycation properties of aqueous extract of clove against fructose-mediated Protein Glycation and oxidation. The result showed that the content of total phenolics and flavonoids in clove extract was 239.58 ± 0.70 mg gallic acid equivalents/g dried extract and 65.67 ± 0.01 mg catechin equivalents/g dried extract, respectively. In addition, clove exhibited antioxidant properties including DPPH radical scavenging activity (IC_50 = 0.29 ± 0.01 mg/ml), Trolox equivalent antioxidant capacity (4.69 ± 0.03 μmol Trolox equivalents/mg dried extract), ferric reducing antioxidant power (20.55 ± 0.11 μmol ascorbic acid equivalents/mg dried extract), Oxygen radical absorbance capacity (31.12 ± 0.21 μmol Trolox equivalents/mg dried extract), hydroxyl radical scavenging activity (0.15 ± 0.04 mg Trolox equivalents/mg dried extract), and superoxide radical scavenging activity (18.82 ± 0.50 mg Trolox equivalents/mg dried extract). The aqueous extract of clove (0.25–1.00 mg/ml) significantly inhibited the formation of fluorescent advanced Glycation end products (AGEs) and non-fluorescent AGEs (N^ɛ-(carboxymethyl) lysine (CML)) in glycated BSA during 4 weeks of incubation. The extract also markedly prevented oxidation-induced Protein damage by decreasing Protein carbonyl formation and protecting against the loss of Protein thiol group. These results clearly demonstrated that a polyphenol enriched clove extract, owing to its antioxidant, was capable to inhibit the formation of AGEs and Protein Glycation. The findings might lead to the possibility of using the clove extract for targeting diabetic complications.

  • mesona chinensis benth extract prevents age formation and Protein oxidation against fructose induced Protein Glycation in vitro
    BMC Complementary and Alternative Medicine, 2014
    Co-Authors: Sirichai Adisakwattana, Thavaree Thilavech, Charoonsri Chusak
    Abstract:

    Mesona chinensis Benth (Chinese Mesona), an economically significant agricultural plant, is the most widely consumed as an herbal beverage in Southeast Asia and China. The objective of this study was to evaluate the inhibitory activity of Mesona chinensis (MC) extract on the formation of advanced Glycation end products (AGEs) and Protein oxidation in an in vitro model of fructose-mediated Protein Glycation. The content of total polyphenolic compounds was measured by using Folin–Ciocalteu assay. AntiGlycation activity was determined using the formation of AGE fluorescence intensity, Nϵ-(carboxymethyl)lysine (CML), the level of fructosamine, and the formation of amyloid cross β-structure. The Protein oxidation was examined using the level of Protein carbonyl content and thiol group. Our results revealed that the content of total polyphenolic compound in MC extract was 212.4 ± 5.6 mg gallic acid equivalents/g dried extract. MC extract (0.25-1.00 mg/mL) significantly inhibited the formation of fluorescence AGEs in fructose-glycated bovine serum albumin (BSA) during 4 weeks of study. Furthermore, MC extract also decreased the level of Nϵ-CML, fructosamine, and amyloid cross β-structure in fructose-glycated BSA. While the total thiol group was elevated and the Protein carbonyl content was decreased in BSA incubated with fructose and MC extract. The extract of MC inhibits fructose-mediated Protein Glycation and Protein oxidation. This edible plant could be a natural rich source of antiGlycation agent for preventing AGE-mediated diabetic complication.

Paul J. Thornalley - One of the best experts on this subject based on the ideXlab platform.

  • Highlights and hotspots of Protein Glycation in end-stage renal disease.
    Seminars in dialysis, 2009
    Co-Authors: Paul J. Thornalley, Naila Rabbani
    Abstract:

    Analysis of tissues, plasma, urine, other body fluids, and dialysate for Glycation adducts has revealed the presence of two major forms: Glycation adduct residues of Proteins and related glycated amino acids—called Glycation free adducts. The major effect on Protein Glycation in uremia is loss of clearance of Glycation free adducts and their marked increase in plasma. Changes in Glycation adduct residue content of plasma Protein in uremia is, in contrast, relatively modest. There is now doubt as to whether the concept of interaction of advanced Glycation endproduct (AGE)-modified Proteins with putative AGE receptors can be sustained in vivo. A residual important feature of the receptor for AGEs may be decrease in expression of glyoxalase 1 of the antiGlycation defence by S100A12 Protein leaving the vasculature vulnerable to dicarbonyl stress and related AGE formation. The dicarbonyl proteome, Proteins susceptible to dicarbonyl Glycation at functional sites, is the likely mediator of Glycation damage in uremia. Glycation of type IV collagen with shedding of endothelial cells and Glycation of apolipoProtein B100 with increased atherogenicity of low density lipoProtein are two examples which may link Protein Glycation to increased risk of cardiovascular disease in end-stage renal disease.

  • degradation products of Proteins damaged by Glycation oxidation and nitration in clinical type 1 diabetes
    Diabetologia, 2005
    Co-Authors: Naila Ahmed, Roya Babaeijadidi, Scott K Howell, Paul J Beisswenger, Paul J. Thornalley
    Abstract:

    Aims/hypothesis: Hyperglycaemia in diabetes is associated with increased Glycation, oxidative stress and nitrosative stress. Proteins modified consequently contain Glycation, oxidation and nitration adduct residues, and un- dergo cellular proteolysis with release of corresponding free adducts. These free adducts leak into blood plasma for eventual renal excretion. The aim of this study was to perform a comprehensive quantitative analysis of Protein Glycation, oxidation and nitration adduct residues in plasma Protein and haemoglobin as well as of free adducts in plasma and urine to quantify increased Protein damage and flux of proteolytic degradation products in diabetes. Methods: Type 1 diabetic patients (n=21) and normal healthy control subjects (n=12) were studied. Venous blood samples, with heparin anticoagulant, and 24-h urine samples were taken. Samples were analysed for Protein Glycation, oxidation and nitration adducts by a quantitative com- prehensive screening method using liquid chromatogra- phy with triple quadrupole mass spectrometric detection. Results: In type 1 diabetic patients, the concentrations of Protein Glycation, oxidation and nitration adduct residues increased up to three-fold in plasma Protein and up to one-fold in haemoglobin, except for decreases in pento- sidine and 3-nitrotyrosine residues in haemoglobin when compared with normal control subjects. In contrast, the concentrations of Protein Glycation and oxidation free adducts increased up to ten-fold in blood plasma, and urinary excretion increased up to 15-fold in diabetic patients. Conclusions/interpretation: We conclude that there are profound increases in proteolytic products of glycated and oxidised Proteins in diabetic patients, con- currentwithmuchlowerincreases inProteinGlycationand oxidation adduct residues. Keywords Glycation . HbA1c . 3-Nitrotyrosine . Oxidative stress . Type 1 diabetes Abbreviations CEL: N"� carboxyethyllysine . CML: N"� carboxymethyllysine . 3-DG: 3-deoxyglucosone . 3DG-H: 3-deoxyglucosone-derivedhydroimidazolone,N � - (5-hydro-5-(2,3,4-trihydroxybutyl)-4-imidazolon-2-yl) ornithine and related structural isomers . DOLD: 3- deoxyglucosone-derived lysine dimer . FL: fructosyl- lysine . FPG: mean fasting plasma glucose concentration .

  • profound mishandling of Protein Glycation degradation products in uremia and dialysis
    Journal of The American Society of Nephrology, 2005
    Co-Authors: Stamatina Agalou, Roya Babaeijadidi, Naila Ahmed, Anne Dawnay, Paul J. Thornalley
    Abstract:

    The aim of this study was to define the severe deficits of Protein Glycation adduct clearance in chronic renal failure and elimination in peritoneal dialysis (PD) and hemodialysis (HD) therapy using a liquid chromatography-triple quadrupole mass spectrometric detection method. Physiologic proteolysis of Proteins damaged by Glycation, oxidation, and nitration forms Protein Glycation, oxidation, and nitration free adducts that are released into plasma for urinary excretion. Inefficient elimination of these free adducts in uremia may lead to their accumulation. Patients with mild uremic chronic renal failure had plasma Glycation free adduct concentrations increased up to five-fold associated with a decline in renal clearance. In patients with ESRD, plasma Glycation free adducts were increased up to 18-fold on PD and up to 40-fold on HD. Glycation free adduct concentrations in peritoneal dialysate increased over 2- to 12-h dwell time, exceeding the plasma levels markedly. Plasma Glycation free adducts equilibrated rapidly with dialysate of HD patients, with both plasma and dialysate concentrations decreasing during a 4-h dialysis session. It is concluded that there are severe deficits of Protein Glycation free adduct clearance in chronic renal failure and in ESRD on PD and HD therapy.

  • Protein Glycation oxidation and nitration adduct residues and free adducts of cerebrospinal fluid in alzheimer s disease and link to cognitive impairment
    Journal of Neurochemistry, 2005
    Co-Authors: Naila Ahmed, Paul J. Thornalley, Usman Ahmed, Klaus Hager, Gerd Fleischer, Gerald Munch
    Abstract:

    Increased damage to Proteins by Glycation, oxidation and nitration has been implicated in neuronal cell death leading to Alzheimer's disease (AD). Protein Glycation, oxidation and nitration adducts are consequently formed. Quantitative screening of these adducts in CSF may provide a biochemical indicator for the diagnosis of AD. To assess this, we measured 11 Glycation adducts, three oxidation adducts and a nitration adduct, determining both Protein adduct residues and free adducts, in CSF samples of age-matched normal healthy subjects (n = 18) and subjects with Alzheimer's disease (n = 32). In CSF Protein, the concentrations of 3-nitrotyrosine, Nɛ-carboxymethyl-lysine, 3-deoxyglucosone-derived hydroimidazolone and N-formylkynurenine residues were increased in subjects with Alzheimer's disease. In CSF ultrafiltrate, the concentrations of 3-nitrotyrosine, methylglyoxal-derived hydroimidazolone and glyoxal-derived hydroimidazolone free adducts were also increased. The Mini-Mental State Examination (MMSE) score correlated negatively with 3-nitrotyrosine residue concentration (p < 0.05), and the negative correlation with fructosyl-lysine residues just failed to reach significance (p = 0.052). Multiple linear regression gave a regression model of the MMSE score on 3-nitrotyrosine, fructosyl-lysine and Nɛ-carboxyethyl-lysine residues with p-values of 0.021, 0.031 and 0.052, respectively. These findings indicate that Protein Glycation, oxidation and nitration adduct residues and free adducts were increased in the CSF of subjects with Alzheimer's disease. A combination of nitration and Glycation adduct estimates of CSF may provide an indicator for the diagnosis of Alzheimer's disease.

  • increased formation of methylglyoxal and Protein Glycation oxidation and nitrosation in triosephosphate isomerase deficiency
    Biochimica et Biophysica Acta, 2003
    Co-Authors: Naila Ahmed, Sinan Battah, Nikolaos Karachalias, Roya Babaeijadidi, Margit Horanyi, Klara Baroti, Susan R Hollan, Paul J. Thornalley
    Abstract:

    Triosephosphate isomerase deficiency is associated with the accumulation of dihydroxyacetonephosphate (DHAP) to abnormally high levels, congenital haemolytic anaemia and a clinical syndrome of progressive neuromuscular degeneration leading to infant mortality. DHAP degrades spontaneously to methylglyoxal (MG)--a potent precursor of advanced Glycation endproducts (AGEs). MG is detoxified to D-lactate intracellularly by the glyoxalase system. We investigated the changes in MG metabolism and markers of Protein Glycation, oxidation and nitrosation in a Hungarian family with two germline identical brothers, compound heterozygotes for triosephosphate isomerase deficiency, one with clinical manifestations of chronic neurodegeneration and the other neurologically intact. The concentration of MG and activity of glyoxalase I in red blood cells (RBCs) were increased, and the concentrations of D-lactate in blood plasma and D-lactate urinary excretion were also increased markedly in the propositus. There were concomitant increases in MG-derived AGEs and the oxidative marker dityrosine in hemoglobin. Smaller and nonsignificant increases were found in the neurologically unaffected brother and parents. There was a marked increase (15-fold) in urinary excretion of the nitrosative stress marker 3-nitrotyrosine in the propositus. The increased derangement of MG metabolism and associated Glycation, oxidative and nitrosative stress in the propositus may be linked to neurodegenerative process in triosephosphate isomerase deficiency.

Weerachat Sompong - One of the best experts on this subject based on the ideXlab platform.

  • RESEARCH ARTICLE Protective Effects of Ferulic Acid on High Glucose-Induced Protein Glycation, Lipid Peroxidation, and Membrane Ion Pump
    2016
    Co-Authors: Activity In Human Erythrocytes, Weerachat Sompong, Henrique Cheng, Sirichai Adisakwattana
    Abstract:

    Ferulic acid (FA) is the ubiquitous phytochemical phenolic derivative of cinnamic acid. Ex-perimental studies in diabetic models demonstrate that FA possesses multiple mechanisms of action associated with anti-hyperglycemic activity. The mechanism by which FA prevents diabetes-associated vascular damages remains unknown. The aim of study was to investi-gate the protective effects of FA on Protein Glycation, lipid peroxidation, membrane ion pump activity, and phosphatidylserine exposure in high glucose-exposed human erythro-cytes. Our results demonstrated that FA (10-100 μM) significantly reduced the levels of gly-cated hemoglobin (HbA1c) whereas 0.1-100 μM concentrations inhibited lipid peroxidation in erythrocytes exposed to 45 mM glucose. This was associated with increased glucose consumption. High glucose treatment also caused a significant reduction in Na+/K+-ATPase activity in the erythrocyte plasma membrane which could be reversed by FA. Furthermore, we found that FA (0.1-100 μM) prevented high glucose-induced phosphatidylserine expo-sure. These findings provide insights into a novel mechanism of FA for the prevention of vascular dysfunction associated with diabetes

  • protective effects of ferulic acid on high glucose induced Protein Glycation lipid peroxidation and membrane ion pump activity in human erythrocytes
    PLOS ONE, 2015
    Co-Authors: Weerachat Sompong, Henrique Cheng, Sirichai Adisakwattana
    Abstract:

    Ferulic acid (FA) is the ubiquitous phytochemical phenolic derivative of cinnamic acid. Experimental studies in diabetic models demonstrate that FA possesses multiple mechanisms of action associated with anti-hyperglycemic activity. The mechanism by which FA prevents diabetes-associated vascular damages remains unknown. The aim of study was to investigate the protective effects of FA on Protein Glycation, lipid peroxidation, membrane ion pump activity, and phosphatidylserine exposure in high glucose-exposed human erythrocytes. Our results demonstrated that FA (10-100 μM) significantly reduced the levels of glycated hemoglobin (HbA1c) whereas 0.1-100 μM concentrations inhibited lipid peroxidation in erythrocytes exposed to 45 mM glucose. This was associated with increased glucose consumption. High glucose treatment also caused a significant reduction in Na+/K+-ATPase activity in the erythrocyte plasma membrane which could be reversed by FA. Furthermore, we found that FA (0.1-100 μM) prevented high glucose-induced phosphatidylserine exposure. These findings provide insights into a novel mechanism of FA for the prevention of vascular dysfunction associated with diabetes.

  • a comparative study of ferulic acid on different monosaccharide mediated Protein Glycation and oxidative damage in bovine serum albumin
    Molecules, 2013
    Co-Authors: Weerachat Sompong, Henrique Cheng, Aramsri Meeprom, Sirichai Adisakwattana
    Abstract:

    Three dietary monosaccharides, (glucose, fructose, and ribose), have different rates of Protein Glycation that accelerates the production of advanced Glycation end-products (AGEs). The present work was conducted to investigate the effect of ferulic acid (FA) on the three monosaccharide-mediated Protein Glycations and oxidation of BSA. Comparing the percentage reduction, FA (1-5 mM) reduced the level of fluorescence AGEs (F-AGEs) and N(e)-(carboxymethyl) lysine (N(e)-CML) in glucose-glycated BSA (F-AGEs = 12.61%-36.49%; N(e)-CML = 33.61%-66.51%), fructose-glycated BSA (F-AGEs = 25.28%-56.42%; N(e)-CML = 40.21%-62.91%), and ribose-glycated BSA (F-AGEs = 25.63%-51.18%; N(e)-CML = 26.64%-64.08%). In addition, the percentages of FA reduction of fructosamine (Frc) and amyloid cross β-structure (Amy) were Frc = 20.45%-43.81%; Amy = 17.84%-34.54% in glucose-glycated BSA, Frc = 25.17%-36.92%; Amy = 27.25%-39.51% in fructose-glycated BSA, and Frc = 17.34%-29.71%; Amy = 8.26%-59.92% in ribose-glycated BSA. FA also induced a reduction in Protein carbonyl content (PC) and loss of Protein thiol groups (TO) in glucose-glycated BSA (PC = 37.78%-56.03%; TO = 6.75%-13.41%), fructose-glycated BSA (PC = 36.72%-52.74%; TO = 6.18%-20.08%), and ribose-glycated BSA (PC = 25.58%-33.46%; TO = 20.50%-39.07%). Interestingly, the decrease in fluorescence AGEs by FA correlated with the level of N(e)-CML, fructosamine, amyloid cross β-structure, and Protein carbonyl content. Therefore, FA could potentially be used to inhibit Protein Glycation and oxidative damage caused by monosaccharides, suggesting that it might prevent AGEs-mediated pathologies during diabetic complications.

  • isoferulic acid a new anti Glycation agent inhibits fructose and glucose mediated Protein Glycation in vitro
    Molecules, 2013
    Co-Authors: Aramsri Meeprom, Weerachat Sompong, Catherine B Chan, Sirichai Adisakwattana
    Abstract:

    The inhibitory activity of isoferulic acid (IFA) on fructose- and glucose-mediated Protein Glycation and oxidation of bovine serum albumin (BSA) was investigated. Our data showed that IFA (1.25–5 mM) inhibited the formation of fluorescent advanced Glycation end products (AGEs) and non-fluorescent AGE [Ne-(carboxymethyl) lysine: CML], as well as the level of fructosamine. IFA also prevented Protein oxidation of BSA indicated by decreasing Protein carbonyl formation and Protein thiol modification. Furthermore, IFA suppressed the formation of β-cross amyloid structures of BSA. Therefore, IFA might be a new promising anti-Glycation agent for the prevention of diabetic complications via inhibition of AGEs formation and oxidation-dependent Protein damage.

  • cinnamic acid and its derivatives inhibit fructose mediated Protein Glycation
    International Journal of Molecular Sciences, 2012
    Co-Authors: Sirichai Adisakwattana, Weerachat Sompong, Sathaporn Ngamukote, Aramsri Meeprom, Sirintorn Yibchokanun
    Abstract:

    Cinnamic acid and its derivatives have shown a variety of pharmacologic properties. However, little is known about the antiGlycation properties of cinnamic acid and its derivatives. The present study sought to characterize the Protein Glycation inhibitory activity of cinnamic acid and its derivatives in a bovine serum albumin (BSA)/fructose system. The results demonstrated that cinnamic acid and its derivatives significantly inhibited the formation of advanced Glycation end products (AGEs) by approximately 11.96-63.36% at a concentration of 1 mM. The strongest inhibitory activity against the formation of AGEs was shown by cinnamic acid. Furthermore, cinnamic acid and its derivatives reduced the level of fructosamine, the formation of N(ɛ)-(carboxymethyl) lysine (CML), and the level of amyloid cross β-structure. Cinnamic acid and its derivatives also prevented oxidative Protein damages, including effects on Protein carbonyl formation and thiol oxidation of BSA. Our findings may lead to the possibility of using cinnamic acid and its derivatives for preventing AGE-mediated diabetic complications.

Aazdine Lamouri - One of the best experts on this subject based on the ideXlab platform.

  • parkinsonism associated Protein dj 1 park7 is a major Protein deglycase that repairs methylglyoxal and glyoxal glycated cysteine arginine and lysine residues
    Journal of Biological Chemistry, 2015
    Co-Authors: Gilbert Richarme, Mouadh Mihoub, Julien Dairou, Thibaut Leger, Aazdine Lamouri
    Abstract:

    Glycation is an inevitable nonenzymatic covalent reaction between Proteins and endogenous reducing sugars or dicarbonyls (methylglyoxal, glyoxal) that results in Protein inactivation. DJ-1 was reported to be a multifunctional oxidative stress response Protein with poorly defined function. Here, we show that human DJ-1 is a Protein deglycase that repairs methylglyoxal- and glyoxal-glycated amino acids and Proteins by acting on early Glycation intermediates and releases repaired Proteins and lactate or glycolate, respectively. DJ-1 deglycates cysteines, arginines, and lysines (the three major glycated amino acids) of serum albumin, glyceraldehyde-3-phosphate dehydrogenase, aldolase, and aspartate aminotransferase and thus reactivates these Proteins. DJ-1 prevented Protein Glycation in an Escherichia coli mutant deficient in the DJ-1 homolog YajL and restored cell viability in glucose-containing media. These results suggest that DJ-1-associated Parkinsonism results from excessive Protein Glycation and establishes DJ-1 as a major anti-Glycation and anti-aging Protein.

Hiroyuki Nakazawa - One of the best experts on this subject based on the ideXlab platform.

  • antioxidative and anti Glycation activity of garcinol from garcinia indica fruit rind
    Journal of Agricultural and Food Chemistry, 2000
    Co-Authors: Fumio Yamaguchi, Toshiaki Ariga, Yoshihiro Yoshimura, Hiroyuki Nakazawa
    Abstract:

    Garcinol, a polyisoprenylated benzophenone derivative, was purified from Garcinia indica fruit rind, and its antioxidative activity, chelating activity, free radical scavenging activity, and anti-Glycation activity were studied. Garcinol exhibited moderate antioxidative activity in the micellar linoleic acid peroxidation system and also exhibited chelating activity at almost the same level as citrate. It also showed nearly 3 times greater DPPH (1, 1-diphenyl-2-picrylhydrazyl) free radical scavenging activity than DL-alpha-tocopherol by weight in aqueous ethanol solution. In a phenazine methosulfate/NADH-nitroblue tetrazolium system, garcinol exhibited superoxide anion scavenging activity and suppressed Protein Glycation in a bovine serum albumin/fructose system. Thus, garcinol might be beneficial as a potent antioxidant and a Glycation inhibitor under specified conditions.

  • antioxidative and anti Glycation activity of garcinol from garcinia indica fruit rind
    Journal of Agricultural and Food Chemistry, 2000
    Co-Authors: Fumio Yamaguchi, Toshiaki Ariga, Yoshihiro Yoshimura, Hiroyuki Nakazawa
    Abstract:

    Garcinol, a polyisoprenylated benzophenone derivative, was purified from Garcinia indica fruit rind, and its antioxidative activity, chelating activity, free radical scavenging activity, and anti-Glycation activity were studied. Garcinol exhibited moderate antioxidative activity in the micellar linoleic acid peroxidation system and also exhibited chelating activity at almost the same level as citrate. It also showed nearly 3 times greater DPPH (1,1-diphenyl-2-picrylhydrazyl) free radical scavenging activity than dl-α-tocopherol by weight in aqueous ethanol solution. In a phenazine methosulfate/NADH−nitroblue tetrazolium system, garcinol exhibited superoxide anion scavenging activity and suppressed Protein Glycation in a bovine serum albumin/fructose system. Thus, garcinol might be beneficial as a potent antioxidant and a Glycation inhibitor under specified conditions. Keywords: Garcinia indica; garcinol; antioxidant; Glycation

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