Abstract
As a carrier of many biologically active compounds, blood is exposed to oxidants to a greater extent than the intracellular environment. Serum albumin plays a key role in antioxidant defence under both normal and oxidative stress conditions. This review evaluates data published in the literature and from our own research on the mechanisms of the enzymatic and non-enzymatic activities of albumin that determine its participation in redox modulation of plasma and intercellular fluid. For the first time, the results of numerous clinical, biochemical, spectroscopic and computational experiments devoted to the study of allosteric modulation of the functional properties of the protein associated with its participation in antioxidant defence are analysed. 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. The perspectives for using the antioxidant properties of albumin in practice are discussed.
Highlights
Leicester School of Allied Health Sciences, De Montfort University, The Gateway, Leicester LE1 9BH, UK; Research Institute of Hygiene, Occupational Pathology and Human Ecology, bld.93 p.o
In biochemical in vitro experiments, we have shown that green tea extract (GTE) polyphenols have an activating effect on the true esterase activity of the protein in Sudlow site I towards paraoxon [167] and have suggested that GTE promotes the transport and the utilisation of OPs by albumin in the bloodstream
In the light of new data, it is possible that the major polyphenol of GTE epigallocatechin gallate (EGCG) has an additional effect: by binding to albumin, it affects the reactivity of the Cys34, enhances its antioxidant properties, weakens the strength of oxidative stress and thereby reduces the intensity of delayed effects of poisoning
Summary
The production of reactive oxygen species (ROS) and reactive nitrogen species (RNS) is an inherent property of all tissues. Blood as a carrier of biologically active compounds is exposed to oxidants to a greater extent than the intracellular environment, but the concentration of antioxidants in plasma is much lower than in cells [50], and it is albumin that plays one of the key roles in the antioxidant defence of the body under normal conditions and in oxidative stress [51,52]. Due to the deletion at position 116, the numbering of amino the redox site (Cys34) of HSA, BSA and RSA. The structure of a protein contains a number of amino acids and amino acid sequencesexcept that for the homologous substitution at position 407, are located at a sufficient distance from the catalytic tyrosine Tyr411(Tyr410). We consider three main activities of albumin associated with redox modulation of blood plasma and interstitial fluid
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