Total Sulfhydryl Research Articles

Zingerone neuroprotective effects in a rat model of manic-like behavior induced by ketamine

Bipolar disorder (BD), before known as manic depression, is a chronic illness and a mood disorder characterized by manic and depressive periods. Drugs used to treat bipolar disorder can cause side effects if used chronically. Therefore, new therapeutic approaches are needed for treatment of BD. Given that inflammatory parameters and oxidative markers increase in BD and on the other hand there are a lot of evidences that zingerone (ZGR) has antioxidant and anti-inflammatory effects, the aim of this study was to investigate the neuroprotective effects of ZGR as one of the active phytochemicals existing in ginger in a model of manic-like behavior (MLB) induced by ketamine (KET) in rats. Thirty-six rats were randomly divided into six groups, including three groups of healthy rats: control, lithium chloride (LiCl) (45 mg/kg, p.o.) and ZGR (50 mg/kg, p.o.), and three groups of MLB rats (received 25 mg/kg KET, i.p. from day 8 to day 15): control, lithium (45 mg/kg, p.o.) and ZGR (50 mg/kg, p.o.). Pre-treatment with ZGR (50 mg/kg) once daily or LiCl (45 mg/kg) twice a day for 14 days prevented all KET-induced changes except total sulfhydryl content (total SH), which was not significant. The data of this study showed that 25 mg/kg KET increased the number of crossings in the open-field test and induced oxidative and inflammatory damage in the rat hippocampus (HPC) and prefrontal cortex (PFC). KET increased thiobarbituric acid reactive substances (TBARS), nitric oxide (NO), and tumor necrosis factor-alpha (TNF-α) levels; and decreased the activity of catalase (CAT) and superoxide dismutase (SOD) enzymes as well as the amount total SH in the HPC and PFC. These findings suggest that oxidative stress (OS) and inflammation may play an important role in BD, and ZGR as an anti-inflammatory and antioxidant agent might be able to reduce the oxidative and inflammatory damage related to the manic phase of this disorder.

Production of freeze-dried beef powder for complementary food: Effect of temperature control in retaining protein digestibility

This study investigated the effect of temperature control during freeze-drying of beef on the in vitro protein digestibility. Frozen (at − 50 °C for 2 days)-then-aged (at 4 °C for 26 days) beef was freeze-dried at 25 °C (FD1) and 2 °C (FD2) to obtain freeze-dried beef powder. Tryptophan fluorescence intensity and total free sulfhydryl groups of beef myofibrillar proteins decreased (P < 0.05) and increased (P < 0.05) after freeze-drying, respectively. In the myosin fraction of FD2, α-helix increased and β-sheet decreased (P < 0.05) compared to raw beef. In contrast, the actin fraction of FD1 showed a decrease in α-helix and increase in β-sheet (P < 0.05) compared to raw beef. The contents of α-amino group and proteins digested to<3 kDa in the in vitro digesta of beef were retained in FD2 while the α-amino group of FD1 decreased (P < 0.05). Therefore, freeze-drying at 2 °C can efficiently retain in vitro protein digestibility of beef.

Ionic strength-mediated protein and flavor studies on thermally processed hairtail pieces.

This study aimed to investigate the impact of different ionic strengths on the texture, protein, and flavor of thermally processed hairtail pieces. Incorporating salt ions into the heat treatment process had a positive impact on the quality of the cooked hairtail pieces. The pieces treated with 2M NaCl showed superior texture and sensory scores. The ionic strength had a significant positive correlation with the chewiness and cohesion of cooked hairtail (p<0.01). Furthermore, the myofibrillar protein content and total sulfhydryl content increased significantly. Circular dichroism spectra analysis revealed a transition in the protein structure from a β-sheet structure to an α-helical structure as the ionic strength decreased. The ionic strength had a significant impact on the interaction between protein and flavor compounds. Specifically, it impacted the expression of certain volatile components (p<0.05). Our study suggests that selecting the appropriate cooking method is crucial for both healthiness and sensory quality of processed hairtail products, and ionic strength mediation is superior in both aspects.

Evaluating the effects of low-frequency alternating magnetic field thawing on oxidation, denaturation, and gelling properties of porcine myofibrillar proteins

The impact of low-frequency alternating magnetic field thawing (LF-MFT) on the physicochemical and gelling properties of porcine myofibrillar proteins (MP) was studied. Results showed that compared to atmosphere thawing (AT), LF-MFT helped in inhibiting the oxidation and denaturation of protein during thawing, thereby maintaining a superior MP gel (P < 0.05). In particular, LF-MFT-4 (LF-MFT at 4 mT) could decrease the oxidation of MP, which might be due to having a higher content of total sulfhydryl and less carbonyl of MP than other thawing treatments. The denaturation of MP was reduced since LF-MFT-4 led to less aggregation and degradation than AT. The gelling properties were also retained, and a compact and homogeneous network structure was formed after LF-MFT-4, resulting in excellent water retention. These findings suggested that LF-MFT-4 improved the gelling properties of MP by inhibiting its oxidation and denaturation, demonstrating a potential application of LF-MFT in meat thawing.

Fabrication of depolymerized zein films via high-intensity ultrasound for ethylene adsorption packaging

The aim of the study was to prepare depolymerized zein (D-zein) films for fruit packaging. High-intensity ultrasound (HIU) treatment was employed to stretch the chemical structure of zein protein, and improve the ethylene adsorption efficiency of D-zein films. The study of circular dichroism spectra, fluorescence spectra, particle size, zeta-potential, and total sulfhydryl group content revealed that the depolymerized zein had stretched structure via a moderate HIU treatment (400 W, 15 min). The structural, mechanical, barrier properties, ethylene adsorption efficiency, and application were used to analyze the performance of the D-zein films. In all treatment groups, bananas coated with the D-zein-15 film exhibited favorable browning rate, weight loss rate, flesh hardness, and sensory properties during storage at 25 °C for 10 d. The results indicated that depolymerized zein films could improve the ethylene adsorption efficiency and effectively prolong the shelf life of bananas.

Catechins affect the oil-holding capacity of meat batters by changing the structure and emulsifying properties of surface proteins at the fat globules

The effects of different concentrations of catechins on the oil-holding capacity, myofibrillar proteins (MPs) structure and adsorbed properties of interfacial proteins in meat batters were investigated. The addition of 100 mg/kg catechin had no negative effects on the physicochemical properties of meat batter. However, 500 and 1500 mg/kg catechin caused an increase in drip loss and deterioration of dynamic rheological properties; the total sulfhydryl content, surface hydrophobicity and α-helix ratio of MPs decreased significantly (p < 0.05); in meat emulsions, the emulsifying property was reduced, the particle size increased, and less interfacial protein was absorbed on the fat globules. All concentrations of catechins significantly (p < 0.05) inhibited lipid oxidation in meat batters. Medium and high concentrations of catechins induced aggregation of MPs via covalent and noncovalent interactions between MPs and MPs or MPs and catechins, which destroyed the gel and emulsifying property of protein and eventually decrease the oil-holding capacity of meat batters.

Whey Protein Hydrolysate Improved the Structure and Function of Myofibrillar Protein in Ground Pork during Repeated Freeze-Thaw Cycles.

Whey protein hydrolysate (WPH) has made a breakthrough in inhibiting oxidative deterioration and improving the quality of meat products during storage. Based on our previous study of extracting the most antioxidant active fraction I (FI, the molecular weight < 1 kDa) from whey protein hydrolysates of different molecular weights, the present study continued to delve into the effects of WPH with fraction I on the structure and function of myofibrillar proteins (MP) in ground pork during the freeze-thaw (F-T) cycles. With the number of F-T cycles raised, the total sulfhydryl content, the relative contents of α-helix, Ca2+-ATPase activity, K+-ATPase activity, solubility, emulsion activity index (EAI), and emulsion stability index (ESI) of MP gradually decreased. Conversely, the carbonyl content and the relative content of random curl showed an increasing trend. In particular, the damage to the structure and the function of MP became more pronounced after three F-T cycles. But, during F-T cycles, FI stabilized the structure of MP. Compared to the control group, the 10% FI group showed a remarkable improvement (p < 0.05) in the total sulfhydryl content, Ca2+-ATPase activity, K+-ATPase activity, solubility, EAI and ESI after multiple F-T cycles, suggesting that 10% FI could effectively inhibit protein oxidation and had the influence of preserving MP function properties. In conclusion, WPH with fraction I can be used as a potential natural antioxidant peptide for maintaining the quality of frozen processed meat products.

Effect of pulsed light on myofibrillar protein of large yellow croaker (Pseudosciaena crocea) during refrigerated storage.

This study mainly evaluated the effect of different energies of pulsed light (PL) treatment (100, 200, 300, 400, and 500J/pulse) on myofibrillar protein (MP) of large yellow croaker during refrigerated storage. The results showed that PL treatment would cause a certain degree of oxidation to the MP of large yellow croaker at the initial stage, which showed that the total sulfhydryl content of the protein decreased, the carbonyl content and the average particle size increased, and the β-sheet to β-turn transformation, the tertiary structure of the protein unfolds, and the hydrophobic groups were exposed, causing the reduction of intrinsic fluorescence intensity. However, subsequent storage studies found that PL treatment could slow down the oxidation rate of MP. The decrease rate of total sulfhydryl content and the increase rate of carbonyl content in the 300J/pulse group were both reduced by about 1.7 times compared with the control group. At the same time, the PL treatment with this intensity could also better protect the secondary structure, tertiary structure, and microstructure of MP. This study provided theoretical basis and reference for analyzing the quality change rule and mechanism of large yellow croaker during refrigerated storage after PL treatment. Studies have shown that PL treatment can reduce the adverse changes of MP in large yellow croaker during cold storage.

Effect of water change on quality deterioration of Pacific white shrimp (Litopenaeus vannamei) during partial freezing storage

The correlation between water changes and quality deterioration of Litopenaeus vannamei during partial freezing storage was evaluated in this study. Significant increases in cross-sectional area and equivalent diameter are detected, but the roundness and longiness of the ice crystals show irregular growth. Within the extension of storage, the bound water (T2b) and immobilized water (T21) decreased significantly. However, the free water (T22) increased significantly. Quality determination showed significant decrease in total sulfhydryl and Ca2+-ATPase, but significant increase in disulfide bonds during storage. Correlation analysis revealed that cross-sectional area showed significant negative correlation with total sulfhydryl and Ca2+-ATPase, while significant positive correlation with disulfide bonds, respectively. The correlation between water distribution index and Ca2+-ATPase, disulfide bonds was significant, respectively. Predicted models for the growth of ice crystals with respect to cross-sectional area and equivalent diameter size have been developed with the help of the Arrhenius model.

Biotinylated caffeic acid covalent binding with myofibrillar proteins in alkaline conditions: Identification of protein-phenol adducts and alterations in protein properties.

In this study, the effects of covalent interactions between myofibrillar proteins (MP) and caffeic acid (CA) were investigated. Protein-phenol adducts were identified by biotinylated caffeic acid (BioC) used as a substitution of CA. The total sulfhydryls and free amines content were decreased (p<0.05). The α-helix structure of MP increased (p<0.05) and MP gel properties enhanced slightly at low dosages of CA (10 and 50μM), and both were impaired significantly (p<0.05) at high dosages of CA (250 and 1250μM). Two prominent adducts of myosin heavy chain (MHC)-BioC and Actin-BioC were identified by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE), which gradually increased at low concentrations of BioC (10 and 50μM), and raised significantly at the concentration of 1250μM. According to the correlation analysis, MHC-BioC and Actin-BioC adducts showed a significant negative correlation with gel properties, such as G', hardness, and water holding capacity (WHC) (p<0.01), which indicated that the covalent interactions between MP and CA significantly affected the quality of meat products.

Nickel chloride generates cytotoxic ROS that cause oxidative damage in human erythrocytes

BackgroundNickel is a heavy metal that is regarded as a possible hazard to living organisms due to its toxicity and carcinogenicity. Nickel chloride (NiCl2), an inorganic divalent Ni compound, has been shown to cause oxidative stress in cells by altering the redox equilibrium. We have investigated the effect of NiCl2 on isolated human erythrocytes under in vitro condition. MethodsIsolated erythrocytes were treated with different concentrations of NiCl2 (25–500 µM) for 24 h at 37 ºC. Hemolysates were prepared and several biochemical parameters were analyzed in them. ResultsTreatment of erythrocytes with NiCl2 enhanced the intracellular generation of reactive oxygen species (ROS). A significant increase in hydrogen peroxide levels and oxidation of proteins and lipids was also seen. This was accompanied by a reduction in levels of nitric oxide, glutathione, free amino groups and total sulfhydryl groups. NiCl2 treatment impaired both enzymatic and non-enzymatic defense systems, resulting in lowered antioxidant capacity and diminished ability of cells to quench free radicals and reduce metal ions. NiCl2 exposure also had an inhibitory effect on the activity of enzymes involved in pathways of glucose metabolism (glycolytic and pentose phosphate shunt pathways). Increased level of methemoglobin, which is inactive in oxygen transport, was also seen. The rate of heme breakdown increased resulting in the release of free iron. Exposure to NiCl2 led to considerable cell lysis, indicating damage to the erythrocyte membrane. This was supported by the inhibition of membrane bound enzymes and increase in the osmotic fragility of NiCl2 treated cells. NiCl2 treatment caused severe morphological alterations with the conversion of normal discocytes to echinocytes. All changes were seen in a NiCl2 concentration-dependent manner. ConclusionNiCl2 generates cytotoxic ROS in human erythrocytes which cause oxidative damage that can decrease the oxygen carrying capacity of blood and also lead to anemia.

Sub‑chronic administration of lead alters markers of oxidative stress, acetylcholinesterase and Na+K+‑ATPase activities in rat brain.

This study investigated the effects of sub‑chronic administration of lead (Pb) acetate on thiobarbituric acid reactive substances (TBA‑RS), total sulfhydryl content, protein carbonyl content, antioxidant enzymes (superoxide dismutase [SOD], catalase [CAT], glutathione peroxidase [GSH‑Px]), acetylcholinesterase (AChE), and Na+K+‑ATPase in the cerebral structures of rats. Male Wistar rats aged 60 days were treated with saline (control group) or Pb (treatment group), at various doses, by gavage, once a day for 35 days. The animals were sacrificed twelve hours after the last administration, and the cerebellum, hippocampus and cerebral cortex were removed. The results showed that Pb did not alter the evaluated oxidative stress parameters. Furthermore, Pb (64 and/or 128 mg/kg) altered SOD in the cerebellum, cerebral cortex and hippocampus. Pb (128 mg/kg) altered CAT in the cerebellum and cerebral cortex and GSH‑Px in the cerebral cortex. Also, Pb (64 mg/kg and 128 mg/kg) altered GSH‑Px in the cerebellum. Moreover, Pb (128 mg/kg) increased AChE in the hippocampus and decreased Na+K+‑ATPase in the cerebellum and hippocampus. In conclusion, sub‑chronic exposure to Pb (occupational and environmental intoxication) altered antioxidant enzymes, AChE, and Na+K+‑ATPase, contributing to cerebral dysfunction.

Effects of electric field intensity regulation on protein aggregation behaviour and foaming property of soybean 7S globulin

In this study, the aggregation behaviour of soybean 7S globulin after moderate electric field (MEF) treatment was investigated, and the influence of the electric field and temperature field on the structure and foaming property of the aggregates were analysed and compared with conventional water bath (COV). The results showed that MEF treatment enhanced the properties of the aggregates. The properties of the treated aggregates were significantly better than those of native 7S globulin. At an electric field strength of 8 V/cm, the solubility, turbidity, and particle size increased from 95.81 % to 99.37 %, 0.097 to 0.189 and 61.97 nm to 113.21 nm, respectively, and the absolute value of potential decreased from 23.56 mV to 22.12 mV. The SDS-PAGE and size exclusion chromatography (SEC) results showed that the electric field had a positive effect on the aggregate formation of the Fourier-transform infrared spectroscopy (FTIR), fluorescence spectroscopy, surface hydrophobicity (H0) and total sulfhydryl (SHT) results indicated that the spatial structure of the protein was changed by MEF treatment. The protein β-sheet content was reduced, and the Try that was originally buried inside the molecule was exposed, resulting in an increase in H0 and a decrease in SHT. The foaming property of the 7S globulin aggregates was improved by MEF treatment.

Effect of cryoprotectants on physicochemical and structural changes in repeated freeze–thawed egg white protein

The effect of cryoprotectants on the changes of physicochemical and structural properties of egg white protein (EWP) caused by repeated freeze-thaw (F-T) cycles was investigated. The cryoprotectants (4% trehalose + 0.3% carrageenan, TC; 1% xylo-oligosaccharide + 0.3% carrageenan, XC; 4% trehalose + 1% xylo-oligosaccharide, TX) were added to the egg white, and stored at F-T for 1, 3, and 5 cycles. The freezing protection effect of cryoprotectants on EWP was discussed by detecting carbonyl contents, total sulfhydryl group content, surface hydrophobicity, water-holding capacity (WHC) of heat-induced gel, SDS-PAGE and the secondary and tertiary structure of protein. The results showed that cryoprotectants could effectively inhibit the increase in surface hydrophobicity and carbonyl contents, and restrict the decrease in total sulfhydryl group content, WHC of heat-induced gel and endogenous fluorescence intensity (p < 0.05). The results can provide reference for the application of cryoprotectants in frozen EWP using in food industry.

Effect of Freezing on Soybean Protein Solution.

To investigate the impact of frozen storage conditions on the physicochemical properties of soybean protein and explore the underlying mechanisms, this study focused on soybean isolate (SPI), ß-soybean companion globulin (7S), and soybean globulin (11S). The protein solutions were prepared at a concentration of 2% and subjected to freezing for 1 and 5 days. Subsequently, the protein content, physicochemical properties, secondary structure, sulfhydryl content, and chemical interaction forces were assessed and analyzed using UV spectrophotometry, Zeta potential measurements, SDS-PAGE, Fourier infrared spectroscopy, and endogenous fluorescence photoemission spectroscopy. The obtained results revealed that the solubility and total sulfhydryl content of SPI, 7S, and 11S exhibited a decreasing trend with prolonged freezing time. Among them, 11S demonstrated the largest decrease in solubility and total sulfhydryl content, followed by SPI, and 7S the least. During freezing, the aromatic amino acids of SPI, 7S, and 11S molecules were exposed, leading to increased hydrophobicity, protein aggregation, and particle size enlargement, and the structure of the protein changed from disordered structure to ordered structure. After freezing, the polarity of the microenvironment of SPI, 7S, and 11S increased, and their maximum fluorescence emission wavelengths were red-shifted. Notably, the largest red shift of SPI was from 332 nm to 335 nm. As freezing time increased, the contribution of hydrogen bonding increased, while the contribution of hydrophobic interactions decreased. This indicates that freezing affects the hydrophobic interactions, hydrogen bonding, and other chemical forces of the protein. The growth of ice crystals leads to the unfolding of protein molecular chains, exposure of internal hydrophobic groups, enhancement of hydrophobicity, and alters the secondary structure of the protein.

Characterization and techno-functional properties of Tenebrio molitor larvae protein concentrate

Global population growth and an alarming rate of global warming conditions have driven the need for protein from alternative non-conventional sources, namely, insect proteins, through a sustainable approach. The protein concentrate of Tenebrio molitor larvae was examined for its suitability and applicability as a food ingredient. Protein was extracted through the acid-alkali method with ∼79% of extraction efficiency. The protein-bound polyphenols were extracted and quantified, and the anti-oxidant potential of protein-bound polyphenols and protein concentrate was assessed. The colour parameters of protein concentrate showed brighter colour (L*, 57.3) than the whole insect powder (L*, 39.0). The surface hydrophobicity of protein concentrate increased to 650, and an increase in the total and free sulfhydryl content (15.39 and 9.158 μmol/g, respectively) was also observed compared to the whole insect powder. Significantly higher protein solubility was observed at pH 2 (72.3%) and pH 11 (66.4%), as compared to near the pI (6.9% at pH 5 and 30.15% at pH 4). Several prominent proteins, including 86 and 56 kDa early-staged encapsulation-inducing proteins, cuticle proteins, and structural proteins were identified in protein concentrate. The techno-functional properties revealed that mealworm protein concentrate was superior to whole insect powder and comparable to whey protein isolate. These findings confirmed the excellent functional properties of mealworm protein concentrate, which can be further explored as a novel food ingredient.

The influence of Klotho protein and prooxidant-antioxidant balance combination on the mortality of HD patients.

End-stage renal disease patients on chronic hemodialysis (HD) have a shortened life expectancy compared to the general population. The aim of this study was to evaluate a possible link between three new and emerging factors in renal pathophysiology: Klotho protein, telomere length in peripheral blood mononuclear cells (TL) and redox status parameters before HD (bHD) and after HD (aHD), and to test mortality prediction capability of these emerging parameters in a population of HD patients. The study included 130 adult patients with average age 66 (54-72), on HD (3 times per week; 4-5h per session). Klotho level, TL, routine laboratory parameters, dialysis adequacy and redox status parameters: advanced oxidation protein products (AOPP), prooxidant-antioxidant balance (PAB), superoxide anion (O2.-), malondialdehyde (MDA), ischemia-modified albumin (IMA), total sulfhydryl group content (SHG), and superoxide dismutase (SOD) were determined. Klotho concentration was significantly higher aHD; 68.2 (22.6-152.9) vs. bHD 64.2 (25.5-119.8) (p = 0.027). The observed increase in TL was not statistically significant. AOPP, PAB, SHG, and SOD activity were significantly increased aHD (p > 0.001). The patients with the highest mortality risk score (MRS) had significantly higher PAB bHD (p = 0.002). Significantly lower O2.- (p < 0.001), SHG content (p = 0.072), and IMA (p = 0.002) aHD were found in patients with the lowest MRS values. Principal component analysis revealed redox balance-Klothofactor as a significant predictor of high mortality risk (p = 0.014). Decreased Klotho and TL attrition as well as redox status disturbance could be connected with higher mortality rate in HD patients.

Effects of thermal processing and temperature on the quality, protein oxidation, and structural characteristics of yak meat.

The aim of this study was to determine the effects of processing on the quality, protein oxidation, and structural properties of yak meat. The cooking loss, Warner-Bratzler shear force, meat color, texture, thiobarbituric acid reactive substance, total carbonyl content (TCC), total sulfhydryl content (TSC), and structural properties of yak meat under frying, drying, and boiling were measured. The results showed that the cooking loss rate, shear force, L* value, hardness, elasticity, and chewiness of yak meat increased (p < .05) and the a* value decreased (p < .05) with increasing central temperature after processing. Fried yak meat at 80°C had the lowest cooking loss rate of 42.21% and the lowest shear force of 50.86 N, which had better textural characteristics, followed by boiling, while the maximum cooking loss rate, hardness, and shear force were 1.40 times, 1.26 times, and 1.2 times that of frying, respectively. The thiobarbituric acid reactive substance was obtained after decoction and peaked at 1.88 ± 0.04 mmol/mg at 60°C. The highest TCC and the lowest TSC were obtained for dried proteins at 80°C. In addition, as the central temperature increased, the helical structure in the protein secondary structure decreased, the disordered structure increased, the fluorescence intensity of myofibrillar proteins decreased, and protein degradation occurred. It was concluded that dried yak meat had the highest protein oxidation and the worst quality, while fried yak meat had the lowest protein oxidation and the best quality.

Mechanisms underlying the anti-aging activity of bergamot (Citrus bergamia) extract in human red blood cells.

Introduction: Aging is a process characterised by a decline in physiological functions. Reactive species play a crucial role in the aging rate. Due to the close relationship between aging and oxidative stress, functional foods rich in phytochemicals are excellent candidates to neutralise age-related changes. Aim: This investigation aims to verify the potential protective role of bergamot (Citrus bergamia, Femminello cultivar) peel and juice extract in a model of aging represented by human red blood cells (RBCs) exposed to D-Galactose (DGal). Methods: Bergamot peel and juice extracts were subjected to RP-HPLC/PDA/MS for determination of their composition in bioactive compounds. Markers of oxidative stress, including ROS production, thiobarbituric acid reactive substances (TBARS) levels -a marker of lipid peroxidation, oxidation of total protein sulfhydryl groups, as well as the expression and anion exchange capability of band 3 and glycated haemoglobin (A1c) production have been investigated in RBCs treated with D-Gal for 24 h, with or without pre-incubation for 15 min with 5 μg/mL peel or juice extract. In addition, the activity of the endogenous antioxidant system, including catalase (CAT) and superoxide dismutase (SOD), as well as the diversion of the RBC metabolism from glycolysis towards the pentose phosphate pathway shunt, as denoted by activation of glucose-6-phosphate dehydrogenase (G6PDH), have been explored. Results: Data shown here suggest that bergamot peel and juice extract i) prevented the D-Gal-induced ROS production, and consequently, oxidative stress injury to biological macromolecules including membrane lipids and proteins; ii) significantly restored D-Gal-induced alterations in the distribution and ion transport kinetics of band 3; iii) blunted A1c production; iv) effectively impeded the over-activation of the endogenous antioxidant enzymes CAT and SOD; and v) significantly prevented the activation of G6PDH. Discussion: These results further contribute to shed light on aging mechanisms in human RBCs and identify bergamot as a functional food rich in natural antioxidants useful for prevention and treatment of oxidative stress-related changes, which may lead to pathological states during aging.

Serum redox markers in uncomplicated type 2 diabetes mellitus accompanied with abnormal iron levels.

This study aimed at evaluating the serum redox status in type 2 diabetes mellitus (T2DM) accompanied with an imbalance in iron concentrations. Diabetic patients were grouped according to serum iron levels [normal (DNFe), low (DLFe), and high (DHFe)], and their clinical and redox parameters [total sulfhydryl groups (tSH), uric acid (UA), and total bilirubin (tBILI) as non-enzymatic antioxidants, and malondialdehyde (MDA) and advanced oxidation products of proteins (AOPP) as markers of oxidative stress] were determined. Glucose and HbA1c levels in the T2DM patients did not differ in function of serum iron. T2DM was associated with reduced tSH levels. In the diabetic patients, tSH, UA, and tBILI negatively correlated with MDA, as well as HbA1c with UA. Accordingly, AOPP and MDA were higher in the diabetic groups compared to the controls. The reduced antioxidant capacity was particularly pronounced in the DLFe group, which was further characterized by lower levels of UA and tBILI compared to the other groups. Subsequently, the level of MDA in the DLFe group was higher compared to the DNFe and DHFe groups. The positive correlation between serum iron levels and the antioxidants UA and tBILI, in conjunction with the negative correlation between serum iron levels and the markers of oxidative stress in the diabetic patients, corroborated the indication that comparatively higher level of oxidative stress is present when T2DM coexists with decreased iron levels. T2DM-associated redox imbalance is characterized by a decrease in serum total sulfhydryl groups and low serum iron-associated reduction in uric acid and total bilirubin levels, accompanied by increased oxidative stress markers. The relatively noninvasive and simple determination of these parameters may be of considerable interest in monitoring the pathophysiological processes in T2DM patients, and may provide useful insights into the effects of potential therapeutic or nutritional interventions.