Structural modifications of human albumin in diabetes

Guérin-Dubourg, Alexis; Catan, Aurélie; Bourdon, Emmanuel; Rondeau, Philippe

doi:10.1016/j.diabet.2011.11.002

Cited by 113 publications

(76 citation statements)

References 29 publications

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“…Fructosamine was determined using the method developed by Johnson et al [25] with the nitroblue tetrazolium (NBT) reagent and following a protocol described in a previous study [26]. The results are expressed as mmol/l of 1-deoxy-1-morpholinofructose (DMF), which is a synthetic ketoamine used as a primary standard.…”

Section: Biochemical Characterizationsmentioning

confidence: 99%

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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: Biochemical Characterizationsmentioning

confidence: 99%

“…The protocol is well described in a previous study [26]. The affinity of albumin for copper was also determined by fluorescence.…”

Section: Copper Binding Affinities Of Albuminmentioning

confidence: 99%

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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“…11,12 As a consequence of the greater susceptibility to glycation of albumin and other plasma proteins compared to intracellular proteins such as hemoglobin, the blood levels of GA exhibit a broader fluctuation than those of HbA1c, thus allowing an earlier detection of rapid changes of blood glucose. 12 Accordingly, the measurement of fructosamine and GA seems useful not only as an alternative index of glycemic control in conditions in which HbA1c is unreliable, but also for identifying impaired control of blood glucose before any noticeable changes in HbA1c may occur, 10,13 as well as for monitoring diabetics with fluctuating and/or poorly controlled diabetes. 14 A number of methods have been developed for the assessment of fructosamine in serum and plasma.…”

Section: Biochemistry and Biology Of Fructosamine And Glycated Albuminmentioning

confidence: 99%

Advantages and Pitfalls of Fructosamine and Glycated Albumin in the Diagnosis and Treatment of Diabetes

Danese

Montagnana

Nouvenne

et al. 2015

J Diabetes Sci Technol

167

139

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Diabetes is one of the most severe and frequent human disorders. According to recent statistics, this condition afflicts as many as 382 million persons around the globe, with an estimated prevalence of approximately 8.3% in 2013. At variance with other frequent pathologies such as cardiovascular disease and bacterial infections, the trend toward an increased prevalence is not expected to soon reverse. Worldwide, as many as 592 million individuals may be affected by diabetes in 2035, a remarkable 55% increase in prevalence over the next 2 decades. 1 Due to its high global prevalence and severe, frequently life-threatening complications (eg, retinopathy, nephropathy, neuropathy, cardiovascular disease), diabetes must be regarded as a serious and increasing global health burden. The most recent Standards of Medical Care in Diabetes published by the American Diabetes Association (ADA) emphasize that early diagnosis and monitoring are critical for preventing or delaying the onset of acute complications and lowering the risk of long-term complications of diabetes. 2 The current diagnostic criteria for this condition are based on the presence of (1) glycated hemoglobin (HbA1c) value ≥6.5% (ie, ≥48 mmol/mol), (2) fasting plasma glucose (FPG) ≥126 mg/dL (ie, ≥7.0 mmol/L), (3) 2-hour plasma glucose ≥200 mg/dL (ie, ≥11.1 mmol/L) during an oral glucose tolerance test (OGTT) using a 75 g glucose load, or (4) random plasma glucose ≥200 mg/dL (ie, ≥11.1 mmol/L). An increased risk of diabetes (ie, prediabetes) is defined in the presence of (1) HbA1c value between 5.7-6.4% (ie, 39-46 mmol/mol), (2) FPG between 100-126 mg/dL (ie, 5.6-6.9 mmol/L), (3) 2-hour plasma glucose between 140-199 mg/ dL (ie, 7.8-11.0 mmol/L) during an OGTT. With regard to diabetes monitoring, the glycemic targets for nonpregnant adults with diabetes include HbA1c value <7.0% (ie, <53 mmol/mol), preprandial capillary plasma glucose between 567227D STXXX10.

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“…Glycation of albumin in presence of various glycating agents like glucose and methyl glyoxal decreases free amino groups present in albumin [38]. Here presence of glucose as glycating agent reduced free amino group present in albumin.…”

Section: Structural Modifications Of Albuminmentioning

confidence: 98%

Zinc inhibits glycation induced structural, functional modifications in albumin and protects erythrocytes from glycated albumin toxicity

Tupe

Kulkarni

Adeshara

et al. 2015

International Journal of Biological Macromolecules

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Structural modifications of human albumin in diabetes

Cited by 113 publications

References 29 publications

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

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

Advantages and Pitfalls of Fructosamine and Glycated Albumin in the Diagnosis and Treatment of Diabetes

Zinc inhibits glycation induced structural, functional modifications in albumin and protects erythrocytes from glycated albumin toxicity

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