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Serum albumin in health and disease: esterase, antioxidant, transporting and signaling properties

Belinskaia, Daria A., Voronina, Polina A., Shmurak, Vladimir I., Jenkins, Richard O., Goncharov, Nikolay V.·2021·International Journal of Molecular Sciences
DOI 10.3390/ijms221910318PMC PMC8508759
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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.

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  • Despite elimination of FBS, BSA often remains prevalent in cell culture media for nutrient transport and cellular stabilization.

    “Despite elimination of FBS, BSA often remains prevalent in cell culture media for nutrient transport and cellular stabilization (Francis, 2010; Price, 2017; Belinskaia et al., 2021).”

    From Challenges and solutions in transitioning to animal-free standards: a comprehensive analysis of components in human cell-based developmental neurotoxicity assays (2026) · cites this paper as Belinskaia et al., 2021

    Section 2 describes albumin’s ligand-transport function, including binding fatty acids, and Section 2.2 identifies BSA as a commonly used in vitro model of serum albumin (page numbers unavailable). The paper does not say that BSA remains prevalent in cell culture media after FBS removal or that it is used there for cellular stabilization. (LLM, conf=0.82)

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Authors
Belinskaia, D. A., Voronina, P. A., Shmurak, V. I., Jenkins, R. O., & Goncharov, N. V.
Affiliations
  • Sechenov Institute of Evolutionary Physiology and Biochemistry, Russian Academy of Sciences, Thorez 44, 194223 St. Petersburg, Russia
  • Leicester School of Allied Health Sciences, De Montfort University, The Gateway, Leicester LE1 9BH, UK
Venue
International Journal of Molecular Sciences
Publisher
MDPI AG
Published
2021-09-25
Volume
22
Issue
19
Pages
10318
ISSN
1422-0067
DOI
10.3390/ijms221910318
PMC
PMC8508759
Cited by
394
References
5
Language
en
Licence
creativecommons.org/licenses/by/4.0/ (vor)
Funders
the State assignment (AAAA-A18-118012290142-9)

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