Glucose and free radicals impair the antioxidant properties of serum albumin

Bourdon, Emmanuel; Loreau, Nadine; Blache, Denis

doi:10.1096/fasebj.13.2.233

Cited by 274 publications

(181 citation statements)

References 57 publications

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“…Both in the red blood cell hemolysis and in ORAC assays, the presence of copper in BSA samples seems to reinforce the free radical trapping capacities of albumin. However, the strengthening in the antiradical capacity of glycated albumin following copper induced-oxidation appears to be in total opposition with previous findings [56]. Even if antioxidant property of albumin seems not to be impaired, there is evidence that the protective role of the protein on cellular system is dramatically altered in the presence of metals, as attested by MTT and FACS results.…”

Section: Discussioncontrasting

confidence: 61%

Deciphering metal-induced oxidative damages on glycated albumin structure and function

Baraka-Vidot¹,

Navarra

Leone

et al. 2014

Biochimica et Biophysica Acta (BBA) - General Subjects

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Background: Metal ions such as copper or zinc are involved in the development of neurodegenerative pathologies and metabolic diseases such as diabetes mellitus. Albumin structure and functions are impaired following metaland glucose-mediated oxidative alterations. The aim of this study was to elucidate effects of Cu(II) and Zn(II) ions on glucose-induced modifications in albumin by focusing on glycation, aggregation, oxidation and functional aspects. Methods: Aggregation and conformational changes in albumin were monitored by spectroscopy, fluorescence and microscopy techniques. Biochemical assays such as carbonyl, thiol groups, albumin-bound Cu, fructosamine and amine group measurements were used. Cellular assays were used to gain functional information concerning antioxidant activity of oxidized albumins. Results: Both metals promoted inhibition of albumin glycation associated with an enhanced aggregation and oxidation process. Metal ions gave rise to the formation of β-amyloid type aggregates in albumin exhibiting impaired antioxidant properties and toxic activity to murine microglia cells (BV2). The differential efficiency of both metal ions to inhibit albumin glycation, to promote aggregation and to affect cellular physiology is compared. Conclusions and general significance: Considering the key role of oxidized protein in pathology complications, glycation-mediated and metal ion-induced impairment of albumin properties might be important parameters to be followed and fought.

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Section: Discussioncontrasting

confidence: 61%

Deciphering metal-induced oxidative damages on glycated albumin structure and function

Baraka-Vidot¹,

Navarra

Leone

et al. 2014

Biochimica et Biophysica Acta (BBA) - General Subjects

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“…21,23 Thus, albumin may represent a quantitatively important component in the efficient antiox- Figure 4, aliquots of total RNA (20 g) isolated from HepG2 cells were electrophoresed, and Northern blot analysis was performed with the use of corresponding cDNA probes specific for HSA or GAPDH as described in Methods. B, Quantitative analysis was performed by scanning of blots and normalized against GAPDH.…”

Section: Discussionmentioning

confidence: 99%

“…22 Moreover, our recent data bring further support to the proposal that in addition to its plasma concentration, the quality of the albumin molecule may be related to its biological properties. 23 We reported that glucose and free radicals impair the antioxidant properties of serum albumin. The serum level of albumin is mainly related to its synthesis and catabolism but also to its transcapillary escape.…”

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confidence: 97%

Involvement of Oxysterols and Lysophosphatidylcholine in the Oxidized LDL–Induced Impairment of Serum Albumin Synthesis by HEPG2 Cells

Bourdon

Loreau

Davignon

et al. 2000

ATVB

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Abstract-Oxidized low density lipoproteins (Ox-LDLs) are increasingly thought to be a key element in atherogenesis. We have previously reported that serum albumin has important antioxidant properties and that a reduced synthesis of albumin may represent a crucial point in the overall antioxidant defense. In the present work, we aimed at determining whether Ox-LDL could modulate albumin synthesis in cultured human hepatocytes (HepG2 cells). With the use of enzyme immunoassay and radiolabeled leucine incorporation followed by specific immunoprecipitation, Ox-LDL was found to lead to a dose-dependent decrease in albumin secretion. Moreover, the protein synthesis and mRNA levels were decreased in the presence of Ox-LDL, as assessed by Northern blot analysis. Because oxysterols and lysophospholipids are key components of Ox-LDL, we tested the effects of oxysterols (7-ketocholesterol and 25-hydroxycholesterol) and lysophosphatidylcholine on albumin secretion and expression. In our experimental conditions, we found that incubations with oxysterols or lysophosphatidylcholine at pathophysiological concentrations similar to those measured in Ox-LDLs reproduced the above-mentioned inhibitory effects on albumin synthesis. On the basis of our in vitro data, we propose that this newly described biological effect of Ox-LDL might partly explain the findings of epidemiological studies indicating that reduced levels of serum albumin are associated with increased mortality. (Arterioscler Thromb Vasc

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“…Researches performed in our group focus on the effects of oxidative modifications induced by the glycation of albumin on its structure, antioxidant properties, and on cell physiology [6][7][8][21][22][23][24][25][26][27]. The implication of glycoxidized albumin in the generation of oxidative stress and damages on cells still needs to be better specified.…”

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confidence: 99%

Oxidative damage in diabetics: Insights from a graduate study in La Reunion University

Girard¹,

Rondeau²,

Catan³

et al. 2014

Biochem Molecular Bio Educ

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Due to the growing incidence of diabetes in developed nations, there is a compelling case to be made for teaching graduate students more deeply about mechanisms underlying this disease. Diabetes is associated with enhanced oxidative stress and protein glycation via the covalent binding of glucose molecules. Albumin represents the major plasmatic protein and undergoes enhanced glycoxidative modifications in diabetic condition. La Reunion Island, a French department located in the Indian Ocean exhibit a growing incidence of diabetes. At the University of La Reunion, our research group named GEICO (Groupe d'Etude sur l'Inflammation Chronique et l'Obesite) participated to foster research and training in diabetes context and focuses on the impact of glycated albumin mediated oxidative stress on cell physiopathology. A laboratory course was designed by our group to introduce graduate students to cutting edge techniques in redox biology while providing insights into scientific processes and methods. This two weeks research laboratory training took place at CYROI, a local biotechnology center that provides advanced facilities for research, business, and education. Using histochemistry, molecular biology, biochemical techniques, student investigated oxidative damages in liver from leptin receptor deficient diabetic mice compared to control littermates. In addition, they used an in vitro model by assaying oxidative impact of glycated albumin on hepatoma carcinoma HepG2 cells. This article gives an overview of the organization and protocol used by the students during their two weeks training in the laboratory. Therefore, it may be helpful for teaching graduate students techniques used in research laboratory working on redox biology. V C 2014 by The International Union of Biochemistry and Molecular Biology, 42(5): 435-442, 2014.

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Glucose and free radicals impair the antioxidant properties of serum albumin

Cited by 274 publications

References 57 publications

Deciphering metal-induced oxidative damages on glycated albumin structure and function

Deciphering metal-induced oxidative damages on glycated albumin structure and function

Involvement of Oxysterols and Lysophosphatidylcholine in the Oxidized LDL–Induced Impairment of Serum Albumin Synthesis by HEPG2 Cells

Oxidative damage in diabetics: Insights from a graduate study in La Reunion University

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