Identification and characterization of oxidized human serum albumin

  title={Identification and characterization of oxidized human serum albumin},
  author={Asami Kawakami and Kazuyuki Kubota and Naoyuki Yamada and Uno Tagami and Kenji Takehana and Ichiro Sonaka and Ei-Ichiro Suzuki and Kazuo Hirayama},
  journal={The FEBS Journal},
Human serum albumin (HSA) exists in both reduced and oxidized forms, and the percentage of oxidized albumin increases in several diseases. However, little is known regarding the pathophysiological significance of oxidation due to poor characterization of the precise structural and functional properties of oxidized HSA. Here, we characterize both the structural and functional differences between reduced and oxidized HSA. Using LC‐ESI‐TOFMS and FTMS analysis, we determined that the major… 
HPLC separation of human serum albumin isoforms based on their isoelectric points.
  • L. Turell, H. Botti, R. Radi
  • Biology
    Journal of chromatography. B, Analytical technologies in the biomedical and life sciences
  • 2014
Redox properties of serum albumin.
Quantitative analysis of cysteine-34 on the anitioxidative properties of human serum albumin in hemodialysis patients.
The results indicate that the (34) Cys residue of HSA may account for more than 40% of the antioxidant effect of H SA in vivo, and thus may exert a protective effect on vascular endothelium function via an antioxidative mechanism in chronic renal disease.
Albumin as a Biomarker
Evidence has accumulated to demonstrate that monitoring of the redox state of Cys-34 could not only be a useful marker for evaluating the progression of oxidative stress-related disease and the development of its complications but also in predicting therapeutic efficacy.
S-Thiolation Targets Albumin in Heart Failure
It is found for the first time that S-thiolation of albumin is increased in the plasma of HF patients and induced changes in the structure and antioxidant function of HSA, likely contributing to HF progression.
Sulfenic acid--a key intermediate in albumin thiol oxidation.
Crystal structure of pharmaceutical-grade human serum albumin.
Cys34-Cysteinylated Human Serum Albumin Is a Sensitive Plasma Marker in Oxidative Stress-Related Chronic Diseases
In conclusion, ESI-TOFMS is a suitable high throughput method for the rapid and sensitive quantification of Cys-Cys34-HSA in a large number of samples for evaluating oxidative stress related chronic disease progression or in response to a treatment.


Heterogeneity and oxidation status of commercial human albumin preparations in clinical use.
Regarding the recent article by Bar-Or et al. (1), there are a few further points that need to be taken into consideration when investigating the heterogeneity of commercially available human serum
Sulfenic acid formation in human serum albumin by hydrogen peroxide and peroxynitrite.
Human serum albumin (HSA), the most abundant protein in plasma, has been proposed to have an antioxidant role and HSA-SOH is proposed to serve as an intermediate in the formation ofLow molecular weight disulfides, which are the predominant plasma form of low molecular weight thiols, and in theformation of mixed HSA disulfide, which is present in approximately 25% of circulating HSA.
Glutathione-linked thiol peroxidase activity of human serum albumin: a possible antioxidant role of serum albumin in blood plasma.
  • M. Cha, I. H. Kim
  • Biology, Chemistry
    Biochemical and biophysical research communications
  • 1996
Results suggest that serum albumin acts as a major and predominate antioxidant exerting a glutathione-linked thiol peroxidase activity which removes reactive oxygen species such as H2O2 within blood plasma.
Albumin Thiolate Anion Is an Intermediate in the Formation of Albumin-S–S-Homocysteine*
Studies are presented to show that the formation of albumin-bound homocysteine proceeds through the generation of an albumin thiolate anion, and using an in vitro model system to study the mechanisms of this disulfide bond formation, it is shown that homocystine binds to albumin in two steps.
Alteration of Redox State of Human Serum Albumin before and after Hemodialysis
It is suggested that serum albumin may be a major extracellular antioxidant in maintenance hemodialysis patients, and that he modialysis may rescue serumalbumin reduction by inducing intermolecular sulfhydryl-disulfide exchange reaction.
Increased oxidized form of human serum albumin in patients with diabetes mellitus.
Crystal structural analysis of human serum albumin complexed with hemin and fatty acid
The structure of the HSA-hemin-myristate complex (PDB ID 1o9x) reveals the key polar and hydrophobic interactions that determine the hemin-binding specificity of HSA.
Oxidation of cysteine and homocysteine by bovine albumin.
  • M. Gabaldón
  • Chemistry, Biology
    Archives of biochemistry and biophysics
  • 2004