Abstract
Being one of the main proteins in the human body and many animal species, albumin plays a decisive role in the transport of various ions—electrically neutral and charged molecules—and in maintaining the colloidal osmotic pressure of the blood. Albumin is able to bind to almost all known drugs, as well as many nutraceuticals and toxic substances, largely determining their pharmaco- and toxicokinetics. Albumin of humans and respective representatives in cattle and rodents have their own structural features that determine species differences in functional properties. However, albumin is not only passive, but also an active participant of pharmacokinetic and toxicokinetic processes, possessing a number of enzymatic activities. Numerous experiments have shown esterase or pseudoesterase activity of albumin towards a number of endogeneous and exogeneous esters. Due to the free thiol group of Cys34, albumin can serve as a trap for reactive oxygen and nitrogen species, thus participating in redox processes. Glycated albumin makes a significant contribution to the pathogenesis of diabetes and other diseases. The interaction of albumin with blood cells, blood vessels and tissue cells outside the vascular bed is of great importance. Interactions with endothelial glycocalyx and vascular endothelial cells largely determine the integrative role of albumin. This review considers 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.
Highlights
Historical Aspects, Origin and Destination, and Evolutionary and Genetic Features of AlbuminAlbumin was probably the first protein that doctors of ancient civilizations paid attention to
We have previously proposed an explanation for albumin-mediated hydrolysis of some substrates by the existence of catalytic dyads His-Tyr or Lys-Tyr, in which histidine or lysine residues function as acid residues and proton donors, and the tyrosine residue is a catalytic base [66]
It is believed that the development of benign hyperglycemia in birds coincided with a radical restructuring of their genome, which resulted in the loss of important genes, including the gene encoding GLUT4, a transporter responsible for insulin-dependent glucose transport in insulin-sensitive cells of other vertebrates
Summary
Historical Aspects, Origin and Destination, and Evolutionary and Genetic Features of Albumin. All albuminoids are evolutionarily connected with serum albumin [6,7] It is one of the most evolutionarily changeable proteins; in different species, the differences between albumin domains can reach 70–80%. The alb gene of human serum albumin (HSA) consists of 16,961 base pairs from the putative cap site to the first poly(A) site. It is divided into 15 exons, which are symmetrically located in three domains. The possible effects of some point mutations on the ligand-binding capacity of HSA were investigated in the interactions of five structurally characterized genetic variants of the protein with warfarin, salicylate and diazepam, which are pharmaceuticals with high affinity for albumin [15].
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