Food Seasoning Spices Mixture Improves Glucose Metabolism and Lipid Profile in Fructose-Fed Hyperinsulinemic Rats
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Fructose feeding has been shown to induce insulin resistance in rats, associated with hyperinsulinemia, hyperglycemia, and hypertriglyceridemia. We have investigated the effect of administering food seasoning spices mixture (SM) on glucose, insulin, and lipids in circulation and carbohydrate enzymes in the erythrocytes of high fructose-fed rats. Additionally, we also measured the protein glycation status by assaying the levels of glycated hemoglobin, fructosamine, and plasma protein glycation. Male Wistar rats received a daily diet containing either 60% fructose or 60% starch (control). The rats were administered SM at three different doses (10, 30, or 50 mg/day per rat) orally 15 days later. At the end of the 45-day experimental period, fructose-fed rats showed significantly higher levels of plasma glucose and insulin, dyslipidemia, and alterations in enzyme activities. Treatment with SM significantly reduced plasma glucose and insulin levels and brought about a favorable lipid profile. In these rats, the activities of enzymes of glucose metabolism were normal. These effects were observed at all three doses of SM. High homeostasis model assessment (HOMA) values indicated insulin resistance in fructose-fed rats, while the HOMA values in SM-treated fructose-fed rats were comparable to those of control rats. We conclude that administration of SM improves glucose metabolism and plasma lipid profile in fructose-fed rats, possibly through improved insulin-sensitizing actions of the active constituents.Keywords:
Hyperinsulinemia
Carbohydrate Metabolism
Fructosamine
Dyslipidemia
Glycated hemoglobin
Diabetes mellitus (DM) commonly occurs in dogs, and the laboratorial confirmation is carried out by glycemia test. The diagnosis and monitoring in humans is made by glycated hemoglobin and fructosamine concentrations. The objective of this study was to diagnose DM in 19 dogs, by evaluating seric glucose, glycated hemoglobin and fructosamine concentrations. Six dogs with DM and treated with insulin were assisted during a twelve-month period, by means of the same blood analysis, until the death (three dogs) or glycemic control (three dogs). Glucose, glycated hemoglobin and fructosamine increased in all dogs with DM, and dogs that did not survive presented higher glycated hemoglobin and seric glucose values than those that survived at the last evaluation. The results showed the importance of evaluating glycated hemoglobin and fructosamine in dogs with DM
Fructosamine
Glycated hemoglobin
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To determine whether there were variations in vivo and in vitro in the glycation process among patients with diabetes mellitus and to assess the characteristics of patients with high and low glycation, if this was observed.Patients (n = 185) attending a Diabetes Day Care Centre or Notre-Dame Hospital in Montreal participated in the in vivo study. Patients found to have high and low glycation were asked to allow the use of their serum for the in vitro part of the study.Capillary blood glucose levels were determined by nursing staff 4 times a day over 7.3 (standard deviation [SD]5.3) consecutive days with commercially available glucose oxydase reagent strips and meters. The ratio of the fructosamine concentration to the protein concentration (the F/P ratio) and the glycated hemoglobin were also determined at the same time as the capillary blood glucose level. Glycation was defined as the mean capillary blood glucose/F/P ratio. Patients with high and low glycation (higher or lower than [SD], of the mean) were compared. For the in vitro study, incorporation of carbon-14 glucose in serum proteins incubated with a 30-mmol/L glucose concentration was studied in some of the patients with low and high glycation.The mean capillary blood glucose/F/P ratio was a mean of 2.30 (SD 0.29) g/mL. Of the 185 subjects 31 had high glycation (1.46 [SD 0.19] g/mL) and 27 had low glycation (2.97 [SD 0.035] g/mL, p < 0.001). There was no significant difference in age, sex, diabetic treatment and glycated hemoglobin levels between the 2 groups. However, patients with low glycation had a greater body mass index (29.4 [SD 5.7] kg/m2 v. 26.4 [SD 4.3] kg/m2, p < 0.05). In vitro, incorporation of 14C glucose in serum proteins incubated with a 30mmol/L glucose concentration was higher in the 9 patients with high glycation than in that of the 7 with low glycation (0.031% [SD 0.03%] per gram of proteins v. 0.028% [SD 0.03%] per gram of proteins, p < 0.02).Glycation may vary among patients with diabetes mellitus who have similar capillary blood glucose concentrations. Glycation appears to be lower in patients with a greater body mass index. Furthermore, alternation in the glycation process itself may explain, in addition to the mean blood glucose level, the difference in fructosamine levels.
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Summary A rare sugar, D-allose (All), exhibits antioxidant activity, and its application in the fields of medicine and food chemistry can be expected. Glycation of proteins has been thought to evoke an oxidative stress state in vivo, but the detailed process involved is unclear. We estimated the reactivity of All during the glycation of human serum albumin (HSA), which was carried out in the presence of All, D-glucose (Glc), D-fructose (Frc) and D-psicose (Psi). The glycation conditions were at pH 7.4 and pH 9.0, 37℃ for 7 days and 50℃ for 48 hours, respectively. The amount of glycation was measured using a glycated albumin kit (Lucica GA-L), fructosamine assay, MALDI-TOF MS, etc,. All reactivities were 1.93-2.38-fold, 1.83-2.40-fold, and 1.63-2.78-fold higher than Glc in glycated albumin, fructosamine, and molecular mass, respectively. Molecular mass increases were larger at pH 9.0 than at pH 7.4. Our results also revealed that alkaline conditions promoted glycation.
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Serum Albumin
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Fructose-mediated protein glycation (fructation) has been linked to an increase in diabetic and cardiovascular complications due to over consumption of high-fructose containing diets in recent times. The objective of the present study is to evaluate the protective effect of (R)-α-lipoic acid (ALA) against fructose-induced myoglobin fructation and the formation of advanced glycation end products (AGEs) in vitro. The anti-glycation activity of ALA was determined using the formation of AGEs fluorescence intensity, iron released from the heme moiety of myoglobin and the level of fructosamine. The fructation-induced myoglobin oxidation was examined using the level of protein carbonyl content and thiol group estimation. The results showed that co-incubation of myoglobin (1 mg/mL), fructose (1 M) and ALA (1, 2 and 4 mM) significantly inhibited the formation of AGEs during the 30 day study period. ALA markedly decreased the levels of fructosamine, which is directly associated with the reduction of AGEs formation. Furthermore, ALA significantly reduced free iron release from myoglobin which is attributed to the protection of myoglobin from fructose-induced glycation. The results also demonstrated a significant protective effect of ALA on myoglobin oxidative damages, as seen from decreased protein carbonyl content and increased protein thiols. These findings provide new insights into the anti-glycation properties of ALA and emphasize that ALA supplementation is beneficial in the prevention of AGEs-mediated diabetic and cardiovascular complications.
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Fructosamine
Bovine serum albumin
L-Glucose
Serum Albumin
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Hyperglycemia plays an important role in the pathogenesis of diabetic complications, as it increases protein glycation, as well as the progressive accumulation of advanced glycation end products (AGEs), which are complex structures that produce fluorescence. The glycation reaction raises the levels of protein carbonyl, N ε-(carboxymethyl)lysine (CML), and fructosamine and decreases the level of thiol groups.In the present study, the antiglycation activity was determined by fluorescence intensity using the bovine serum albumin (BSA)/glucose, CML method, and the level of fructosamine. The oxidation of proteins was determined by the carbonyl protein content and thiol groups.The results show that the hexane extract of Acca sellowiana (FOH) at different concentrations (0.30-5 mg/ml) significantly inhibited the formation of AGEs in the BSA/glucose model during the 4 weeks of the study. FOH reduced the levels of fructosamine and CML. Our results showed a significant effect of FOH in the prevention of oxidative damage of proteins, as well as an effect on the oxidation of thiol groups and carbonyl proteins.The present study indicates that FOH is effective in inhibiting the glycation of proteins in vitro, so it can prevent or ameliorate the chronic conditions of diabetes associated with the formation of AGEs.
Fructosamine
Advanced glycation end-product
Bovine serum albumin
Pathogenesis
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Hyperinsulinemia
Fructolysis
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High-carbohydrate containing diets have become a precursor to glucose-mediated protein glycation which has been linked to an increase in diabetic and cardiovascular complications. The aim of the present study was to evaluate the protective effect of (R)-α-lipoic acid (ALA) against glucose-induced myoglobin glycation and the formation of advanced glycation end products (AGEs) in vitro. Methods: The effect of ALA on myoglobin glycation was determined via the formation of AGEs fluorescence intensity, iron released from the heme moiety of myoglobin and the level of fructosamine. The extent of glycation-induced myoglobin oxidation was measured via the levels of protein carbonyl and thiol. Results: The results showed that the co-incubation of ALA (1, 2 and 4 mM) with myoglobin (1 mg/mL) and glucose (1 M) significantly decreased the levels of fructosamine, which is directly associated with the decrease in the formation of AGEs. Furthermore, ALA significantly reduced the release of free iron from myoglobin which is attributed to the protection of myoglobin from glucose-induced glycation. The results also demonstrated a significant protective effect of ALA on myoglobin from oxidative damage, as seen from the decreased protein carbonyls and increased protein thiols. Conclusion: The anti-glycation properties of ALA suggest that ALA supplementation may be beneficial in the prevention of AGEs-mediated diabetic and cardiovascular complications.
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Advanced glycation end-product
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Background: Chronic hyperglycemia in diabetes causes a non‐enzymatic glycation between reducing sugars and amino groups of proteins, resulting in production of advanced glycation end products (AGEs). It has been known that AGEs play a pivotal role in the pathogenesis of both microvascular and macrovascular complications of diabetic patients. Moringa Oleifera is one of the well‐known Thai medicinal plants that have been shown to have the favorable effects in the treatment and prevention of diabetes through various mechanisms . However, the antiglycation activity of Moringa oleifera leaf extract has not been investigated. Objective: The purpose of this study was to determine the inhibitory effect of Moringa oleifera leaf extract (MOE) on fructose‐induced protein glycation. Methods: The various concentrations of MOE were incubated with bovine serum albumin (BSA) and 0.5M fructose at 37ºC for 7, 14, 21 and 28 days. Fluorescence AGEs formation, fructosamine and β‐amyloid structure level were measured. Results: MOE (0.5‐2.00 mg/ml) showed a dose‐dependent decrease in fluorescence AGEs formation. Moreover, MOE significantly reduced fructosamine and β‐amyloid structure level when compared to the negative control. Discussion and Conclusion: MOE may reduce diabetic complications through inhibiting the AGEs formation, decreasing fructosamine level and also preventing protein aggregation (β‐amyloid structure). Additionally, this research may also provide beneficial effects of MOE on reducing the risk of advanced glycation endproduct associated diseases. Grant Funding Source : Supported by Thailand Research Fund
Fructosamine
Moringa
Advanced glycation end-product
Bovine serum albumin
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Dogs have been proposed as a translational model and used for studying aging, diabetes, and diabetes-related complications in humans. However, no studies have ever compared the glycation of plasma proteins between dogs and humans under similar experimental conditions. Thus, the aim of this study was to fill this gap by comparing the plasma protein glycation patterns of dogs and humans in an ex-vivo system. Canine and human plasma samples were incubated with glucose at concentrations comparable to those observed in diabetic patients. The final glucose plasma concentration resulted in similar glucose:albumin ratios in both species. Glycated proteins were evaluated by measuring the content of fructosamine, protein carbonyls, and the formation of advanced glycation end-products (AGEs). The concentrations of fructosamine and protein carbonyls in canine and human plasma increased in a glucose concentration-dependent manner (P < 0.0001). Of note, the relative increment of fructosamine and protein carbonyl content and AGE formation was always higher in human than in dog plasma. Our results reveal that the plasma glycation processes in dogs and humans are not similar. These novel findings could contribute to improve our understating about canine and human diabetes as well as other condition associated in the glycation of proteins.
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