Albumin antioxidant capacity is modified by methylglyoxal

Faure, Patrice; Troncy, Lysiane; Lecomte, Marc; Wiernsperger, Nicolas; Lagarde, Michel; Ruggiero, Daniel; Halimi, Serge

doi:10.1016/s1262-3636(07)70183-0

Cited by 71 publications

(40 citation statements)

References 26 publications

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“…In a previous study [14], type 2 diabetic patients showed a 0.7¡0.48 difference in thiol groups between patients and controls. As the present OSA patients were supposed to be only suffering from insulin resistance, a mean difference of 0.6 with the same SD was expected.…”

Section: Statistical Analysis Sample Size Power Calculationmentioning

confidence: 73%

“…Albumin represents the most abundant protein in the circulatory system with a significant antioxidant activity, which is principally related to the protein's capacity to bind metal ions and scavenge free radicals [13][14][15]. It has been demonstrated that, besides its plasma concentration, structural modifications induced by glucose or free radicals impaired the antioxidant properties of albumin.…”

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confidence: 99%

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Impairment of serum albumin antioxidant properties in obstructive sleep apnoea syndrome

Faure¹,

Tamisier²,

Jp³

et al. 2008

Eur Respir J

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Antioxidant counteraction of oxidative stress has been poorly explored in obstructive sleep apnoea (OSA). Serum albumin is a major antioxidant agent and structural modifications induced by glucose or free radicals impair its antioxidant properties.The aim of the present study was to compare antioxidant capacities and structural changes of albumin in nonobese OSA patients and healthy volunteers.Albumin structural changes were studied by quenching of fluorescence in the presence of acrylamide. Albumin thiols and fructosamines, reflecting oxidation-and glycation-induced changes in serum albumin, respectively, were assessed. Albumin structural changes were demonstrated by a significant decrease in quenching of fluorescence in OSA patients. Oxidation, resulting in a significant decrease in thiol groups (3.7¡0.7 versus 2.3¡0.4 mmol?g -1 protein), and glycation, associated with a significant increase in fructosamines (226.6¡27 versus 286¡44.4 mmol?L -1 ), were found when comparing healthy volunteers with OSA patients. There was a significant relationship between both parameters and sleep apnoea severity. After continuous positive airway pressure intervention, albumin thiol groups were reassessed in seven of the 16 OSA patients and increased significantly from 2.25¡0.39 to 2.79¡0.31 mmol?g -1 protein.Obstructive sleep apnoea patients demonstrated a reduction in serum albumin antioxidant properties that may aggravate oxidative stress and, thus, contribute to cardiovascular and metabolic morbidities.

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Section: Statistical Analysis Sample Size Power Calculationmentioning

confidence: 73%

mentioning

confidence: 99%

Impairment of serum albumin antioxidant properties in obstructive sleep apnoea syndrome

Faure¹,

Tamisier²,

Jp³

et al. 2008

Eur Respir J

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“…Oxidative stress can cause several types of molecular lesions to the HSA molecule. The main PTMs relevant to the pathophysiology of HSA include: thiolation, carbonylation, advanced glycoxidation and oxidation (AGE and AOPP, respectively) that have been documented in a series of studies on CKD as well as under other conditions of oxidative stress [28,29,30,31,32,33,34,35]. These PTMs, and in particular carbonylation, which have been observed as an extensive modification in the plasma of HD patients after the isolation and in-depth analysis of the HSA protein [35,36,37], may interfere with the biological functions of HSA.…”

Section: Human Serum Albumin As a Source Of Nondialyzable Uremic Toxinsmentioning

confidence: 99%

“…These PTMs, and in particular carbonylation, which have been observed as an extensive modification in the plasma of HD patients after the isolation and in-depth analysis of the HSA protein [35,36,37], may interfere with the biological functions of HSA. These are the result of conformational alterations (that may produce for instance an increased negative charge and the exposure of hydrophobic regions), the functional consequences of which may include: an impaired site II ligand-binding capability, decreased drug-binding and antioxidant activity, and also defective biochemical evaluation during the application of common assay procedures used in routine analysis to measure the levels of this protein (reviewed by Alvarez et al and Michelis et al [32,38]).…”

Section: Human Serum Albumin As a Source Of Nondialyzable Uremic Toxinsmentioning

confidence: 99%

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Nondialyzable Uremic Toxins

et al. 2013

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Nondialyzable uremic toxins can be defined as solutes producing adverse biological effects that consequently to peculiar physicochemical features (mainly their large size and hydrophobic character) cannot leave the blood stream through a dialysis membrane. These are the subject of great interest for the scientific community, in that emerging evidence suggests that such uremic retention solutes may contribute a main role to the complex inflammatory and vascular comorbidity of the uremic syndrome. Treatments based on most efficient diffusive or convective protocols of dialysis and pharmacological therapies cannot prevent nor correct such clinical symptoms. Protein-bound solutes and other proteinaceous components present in excess in the uremic milieu are thus natural candidates for explaining the resistance of uremic toxicity to current regimens of therapy. Intense research is in progress to identify molecular species and mechanisms of toxicity, but the real challenge of our times is to develop innovative clinical protocols that may remove or prevent the formation/toxicity of nondialyzable uremic solutes. These include high-efficacy protein-leaking dialyzers, adsorption techniques, frequent dialysis, and pharmacological therapies. These aspects are examined in this review paper, paying particular attention to covalent posttranslational modifications of plasma proteins produced as a consequence of oxidative, nitrosative and carbonyl stress. These represent an emerging trait in the pathobiology of inflammatory and age-related disorders, deserving further consideration in chronic kidney disease.

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Antioxidant and reactive oxygen species scavenging properties of cellular albumin in HepG2 cells is mediated by the glutathione redox system

Seidkhani-Nahal

Allameh

Soleimani

2018

Biotech and App Biochem

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This study was carried out to examine the role of intracellular albumin in the modulation of oxidative damage induced by glutathione modifiers in HepG2 cells. Also, the relationship of albumin synthesis with oxidative stress factors including antioxidants was studied. HepG2 cell culture was supplemented with glutathione modifiers; L-Buthionine-sulfoximine (BSO; 0.1 and 1.0 mM) or N-acetyl cysteine (NAC; 1 and 10 mM) and the cell viability and changes in reduced glutathione (GSH), oxidized glutathione (GSSG), reactive oxygen species (ROS), catalase, and superoxide dismutase were measured. Besides, albumin expression at protein and mRNA levels was determined in cells pretreated with BSO or NAC. Kinetic studies showed that albumin expression in HepG2 cells is correlated with GSH and GSSG levels. Changes in albumin expression at protein and mRNA levels reached their maximum (19% and 55%, respectively) in the cells 6 H after NAC treatments. A substantial decrease in intracellular albumin due to BSO (27%) was associated with a significant increase in the generation of cellular ROS (17%). In contrast, increased albumin synthesis (intracellular and secretory) was associated with inhibition in cellular ROS. Overall data may suggest that albumin expression in coordination with the glutathione redox system is part of the antioxidant defense mechanism in liver cells. C 2018

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Albumin antioxidant capacity is modified by methylglyoxal

Cited by 71 publications

References 26 publications

Impairment of serum albumin antioxidant properties in obstructive sleep apnoea syndrome

Impairment of serum albumin antioxidant properties in obstructive sleep apnoea syndrome

Nondialyzable Uremic Toxins

Antioxidant and reactive oxygen species scavenging properties of cellular albumin in HepG2 cells is mediated by the glutathione redox system

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