The thiol pool in human plasma: The central contribution of albumin to redox processes
By L. Turell, Rafael Radi, B. Alvarez. Free Radical Biology & Medicine, 2013
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The plasma compartment has particular features regarding the nature and concentration of low and high molecular weight thiols and oxidized derivatives. Plasma is relatively poor in thiol-based antioxidants; thiols are in lower concentrations than in cells and mostly oxidized. The different thiol-disulfide pairs are not in equilibrium and the steady-state concentrations of total thiols as well as reduced versus oxidized ratios are maintained by kinetic barriers, including the rates of reactions and transport processes. The single thiol of human serum albumin (HSA-SH) is the most abundant plasma thiol. It is an important target for oxidants and electrophiles due to its reactivity with a wide variety of species and its relatively high concentration. A relatively stable sulfenic (HSA-SO3H) acid can be formed in albumin exposed to oxidants. Plasma increases in mixed disulfides (HSA-SSR) or in sulfinic (HSA-SO2H) and sulfonic (HSA-SO3H) acids are associated with different pathologies and may constitute biomarkers of the antioxidant role of the albumin thiol. In this work we provide a critical review of the plasma thiol pool with a focus on human serum albumin.
Subfields: Biochemistry, Molecular Biology, Pathology and Forensic Medicine
View Paper: https://www.semanticscholar.org/paper/ce261fa8e0f518bf44bf89231dddad2dd7176492
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Citations in the corpus
- A novel and automated assay for thiol/disulphide homeostasis. (2014, background): “The plasma thiol pool is mainly formed by albumin thiols, protein thiols and slightly formed by low-molecular-weight thiols such as cysteine (Cys), cysteinylglycine, glutathione, homocysteine and γ-glutamylcysteine [2].”