The antioxidant properties of serum albumin

@article{Roche2008TheAP,
  title={The antioxidant properties of serum albumin},
  author={Marjolaine Roche and Philippe Rondeau and Nihar Ranjan Singh and Evelyne Tarnus and Emmanuel Bourdon},
  journal={FEBS Letters},
  year={2008},
  volume={582}
}
Redox properties of serum albumin.
The glycation of albumin: structural and functional impacts.
Redox homeostasis of albumin in relation to alpha-lipoic acid and dihydrolipoic acid.
TLDR
It is clear that the loss of biological activity of human serum albumin by MCO system appears of medical relevance and if LA exerts similar effects seen in the present study, it is possible that cellular prooxidant activity can also result consuming this unique antioxidant in certain doses.
The Universal Soldier: Enzymatic and Non-Enzymatic Antioxidant Functions of Serum Albumin
TLDR
It has been concluded that it is fundamentally possible to regulate the antioxidant properties of albumin with various ligands, and the binding and/or enzymatic features of the protein by changing its redox status.
Human serum albumin and its relation with oxidative stress.
TLDR
It is necessary to give a more detailed explanation of albumin and its relations with oxidative stress and its interactions with Reactive Oxygen Species.
Comparison of antioxidant properties of different therapeutic albumin preparations.
Endogenous non-enzymatic antioxidants in the human body.
Physiological antioxidant system and oxidative stress in stomach cancer patients with normal renal and hepatic function
TLDR
Lipid peroxidation measured as plasma Thio Barbituric Acid Reactive substances (TBARS), was found to be elevated significantly in stomach cancer compared to controls along with a decrease in plasma physiological antioxidant system.
Serum Albumin in Health and Disease: Esterase, Antioxidant, Transporting and Signaling Properties
TLDR
The esterase, antioxidant, transporting and signaling properties of albumin, as well as its structural and functional modifications and their significance in the pathogenesis of certain diseases are considered.
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References

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Albumin antioxidant capacity is modified by methylglyoxal.
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TLDR
It is proposed that Cys chiefly works as a free radical scavenger whereas Met mainly acts as a metal chelator in relation to anti-/prooxidant properties of HSA.
Glucose and free radicals impair the antioxidant properties of serum albumin
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TLDR
It is proposed that, considering the poor glucose control found in diabetics as well as the key role of oxidative stress in vascular complications, glycation‐mediated and free radical‐induced impairment of the antioxidant properties of albumin might be important parameters in vascular complication encountered in diabetes.
Physiological and pathological changes in the redox state of human serum albumin critically influence its binding properties
TLDR
The physiological or pathophysiological concentrations of different oxidatively modified albumin molecules vary over a wide range and are crucial in assessing the clinical relevance of altered ligand binding properties of a particularly modifiedalbumin species in various disease conditions.
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TLDR
This review examines the specific role of sulfur-containing amino acids in protein degradation and their possible interplay with the reversal of limited oxidative lesions, and the participation of proteins in the overall antioxidant defense is discussed, specifically the role of metallothionein as an intracellular antioxidant and that of albumin as a circulating antioxidant.
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TLDR
Results indicate that in vitro glycoxidative modification of HSA induced a marked loss of antioxidant activity of this molecule to copper-mediated oxidation of LDL, which may be caused by the generation of superoxide.
Impairment of the antioxidant properties of serum albumin in patients with diabetes: protective effects of metformin.
TLDR
Patients with T2DM have a decrease in the antioxidant properties of serum albumin which may aggravate oxidative stress and, thus, contribute to vascular and metabolic morbidities.
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Bilirubin attenuates radical‐mediated damage to serum albumin
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