Oxidative stresses induced by glycoxidized human or bovine serum albumin on human monocytes

Rondeau, Philippe; Singh, Nihar Ranjan; Caillens, H; Tallet, Frank; Bourdon, Emmanuel

doi:10.1016/j.freeradbiomed.2008.06.004

Cited by 58 publications

(44 citation statements)

References 61 publications

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“…Furthermore, we have observed toxic effects of HSA protein aggregates produced by CNBr fragmentation under denaturing conditions, and of HSA aggregates produced by glutaraldehyde treatment (data not shown). While the HSA-AGE preparations in this study did not display detectable toxic activity for the endothelium, similar preparations have been described as having oxidative properties that vary depending on the agents and conditions used for AGE formation [32,33]. Our current observations indicating the absence of significant oxidative toxicity in HSA-AGE preparations are that: HUVEC survival in the presence of HSA-AGE never fell below the levels seen in serumor albumin-deprived endothelium; the addition of native HSA overcame HUVEC apoptosis in the presence of HSA-AGE; and the anti-apoptotic activity of otherwise inactive HSA-AGE was restored by CNBr fragmentation.…”

Section: Huvec Exposed To Hsa-age 4 Were Apoptotic and Not Necroticmentioning

confidence: 46%

The anti-apoptotic activity of albumin for endothelium is inhibited by advanced glycation end products restricting intramolecular movement

Zoellner

Siddiqui

Kelly

et al. 2009

Cellular and Molecular Biology Letters

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Human serum albumin (HSA) inhibits endothelial apoptosis in a highly specific manner. CNBr fragmentation greatly increases the effectiveness of this activity, suggesting that this type of protection is mediated by a partially cryptic albumin domain which is transiently exposed by intramolecular movement. Advanced glycation end-product (AGE) formation in HSA greatly reduces its intra-molecular movement. This study aimed to determine if this inhibits the anti-apoptotic activity of HSA, and if such inactivation could be reversed by CNBr fragmentation. HSA-AGE was prepared by incubating HSA with glucose, and assessed using the fructosamine assay, mass spectrometry, SDS-PAGE and fluorometry. Low levels of AGE in the HSA had little effect upon its anti-apoptotic activity, but when the levels of AGE were high and the intra-molecular movement was reduced, endothelial cell survival was also found to be reduced to levels equivalent to those in cultures without HSA or serum (p > 0.001). Survival was restored by the inclusion of native HSA, despite the presence of HSA with high levels of AGE. Also, CNBr fragmentation of otherwise inactive HSA-AGE restored the anti-apoptotic activity for endothelium. Apoptosis was confirmed by DNA gel electrophoresis, transmission electron microscopy and fluorescence-activated cell sorting analysis, and there was no evidence for direct toxicity in the HSA-AGE preparations. The results are consistent with the proposed role of intra-molecular movement in exposing the anti-apoptotic domain in HSA for endothelium. The levels of AGE formation required to inhibit the anti-apoptotic activity of HSA exceeded those reported for diabetes. Nonetheless, the data from this study seems to be the first example of reduced protein function due to AGE-restricted intra-molecular movement.

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Section: Huvec Exposed To Hsa-age 4 Were Apoptotic and Not Necroticmentioning

confidence: 46%

The anti-apoptotic activity of albumin for endothelium is inhibited by advanced glycation end products restricting intramolecular movement

Zoellner

Siddiqui

Kelly

et al. 2009

Cellular and Molecular Biology Letters

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“…In vitro glycation of albumin-Albumin glycation was performed as previously described (65). Fatty acid-free human serum albumin (Sigma A1887) solutions were prepared in phosphate-buffered saline (PBS) (pH 7.4) at a concentration of 40 g.L -1 .…”

Section: Methodsmentioning

confidence: 99%

Glycation of human serum albumin impairs binding to the glucagon-like peptide-1 analogue liraglutide

Soudahome

Catan

Giraud

et al. 2018

Journal of Biological Chemistry

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“…An increased production of ROS was also observed in monocytes treated with MGmodified albumin [111]. Thus, MG induced thrombosis and inflammation by activating monocytes, induced apoptosis of neutrophils, and caused platelet-neutrophil aggregates [112].…”

Section: Methylglyoxal and Oxidative Stressmentioning

confidence: 87%

Aging: Drugs to Eliminate Methylglyoxal, a Reactive Glucose Metabolite, and Advanced Glycation Endproducts

Dhar¹,

Desai²

2012

Pharmacology

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Oxidative stresses induced by glycoxidized human or bovine serum albumin on human monocytes

Cited by 58 publications

References 61 publications

The anti-apoptotic activity of albumin for endothelium is inhibited by advanced glycation end products restricting intramolecular movement

The anti-apoptotic activity of albumin for endothelium is inhibited by advanced glycation end products restricting intramolecular movement

Glycation of human serum albumin impairs binding to the glucagon-like peptide-1 analogue liraglutide

Aging: Drugs to Eliminate Methylglyoxal, a Reactive Glucose Metabolite, and Advanced Glycation Endproducts

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