Serum Albumin: Comparison
View Latest Version
Please note this is a comparison between Version 1 by Nikolay Goncharov and Version 4 by Catherine Yang.

Being one of the most abundant proteins in human and other mammals, albumin plays a crucial role in transporting various endogenous and exogenous molecules and maintaining of colloid osmotic pressure of the blood. It is not only the passive but also the active participant of the pharmacokinetic and toxicokinetic processes possessing a number of enzymatic activities. A free thiol group of the albumin molecule determines the participation of the protein in redox reactions. Its activity is not limited to interaction with other molecules entering the blood: of great physiological importance is its interaction with the cells of blood, blood vessels and also outside the vascular bed. This topic review contains data on the enzymatic, inflammatory and antioxidant properties of serum albumin. 

Albumin is one of the most abundant proteins in human and other mammals. It plays a crucial role in maintaining of colloid osmotic pressure of the blood, and is able to bind and transport various endogenous and exogenous molecules. Albumin is not only the passive but also active participant of the pharmacokinetic and toxicokinetic processes possessing a number of enzymatic activities: (pseudo)esterase, paraoxonase, phosphotriesterase, thioesterase, glutathione peroxidase, cysteine peroxidase and some others. The albumin molecule contains a free thiol group within the amino acid residue Cys34, which largely determines the participation of the protein in redox reactions. This topic review contains data on the enzymatic and antioxidant properties of serum albumin; the prospects for the therapeutic application of the functional features of the protein are discussed.

  • albumin
  • blood plasma
  • enzymatic activities
  • oxidative stress
Albumin is a family of globular proteins, the most common of which are the serum albumins. All the proteins of the albumin family are water-soluble and moderately soluble in concentrated salt solutions. The key qualities of albumin are those of an acidic, highly soluble and very stable protein, able to withstand temperatures of 60 °C for 10 h

Introduction

Albumin is one of the most abundant proteins in human and other mammals. In humans, it is synthesised in the liver at a rate of about 0.7 mg per hour (i.e. 10-15 mg per day); the half-life of human serum albumin (HSA) is about 19-20 days

[1]. Human serum albumin (HSA) has a total of 83 positively charged residues (Arg + Lys) and 98 negatively charged residues (Asp + Glu), with a theoretical pI of 5.12. Albumins are commonly found in blood plasma and differ from other blood proteins in that they are not glycosylated. Several other blood transport proteins are evolutionarily related to serum albumin, including alpha-fetoprotein, vitamin D-binding protein and afamin

. The molecule of HSA is formed by one polypeptide chain, consisting of 585 amino acid residues. In albumins of other species, the length of the polypeptide chain can vary; in particular, bovine serum albumin (BSA) contains 584 amino acid residues, rat serum albumin (RSA) – 583 residues. Three homologous domains (I, II, III), consisting of two subdomains (A, B) form a three-dimensional structure of the protein, which is rather labile. The three-dimensional structure of HSA was resolved rather late, only in the 1990s

[2]

. A similar structure of BSA was obtained in 2012

[3]. This family is only found in vertebrates

. However, the three-dimensional structure of RSA has not been obtained yet. The percentage of identity of the primary structures of HSA and RSA is 73.0%, BSA and RSA – 69.9%. In the absence of crystallographic data, the three-dimensional structure of a protein can be obtained with the help of homologous modeling. Homologous models of RSA have already been constructed recently

[4]. The four canonical human albumins are arranged on chromosome 4 region 4q13.3 in a tandem manner [5]. The human albumin gene is 16,961 nucleotides long from the putative ‘cap’ site to the first poly(A) addition site. It is split into 15 exons that are symmetrically placed within the three domains thought to have arisen by triplication of a single primordial domain.

.

Humans are not the only organisms for which serum albumin plays a critical role; albumin has also been characterised in an extensive number of species, including (but not limited to) canines, chickens, several species of frogs, lampreys, pigs and salamanders (an exhaustive list can be found at albumin.org

Previously, it was assumed that the albumin molecule had the shape of an elongated or flattened ellipsoid ("cigar" or "pill"), but X-ray analysis showed that the protein has the shape of a heart

[6]). Albumin-like proteins, which were sequenced from a sea urchin, were found to have a cysteine binding pattern similar to that seen amongst other proteins in the albumin family

. Albumin normally is not covered with hydrocarbons and can bind different endogenous and exogenous ligands: water and predominantly divalent metal cations, fatty acids, hormones, bilirubin, transferrin, nitric oxide, aspirin, warfarin, ibuprofen, phenylbutazone, etc.

[7].
The precursor of serum albumin (preproalbumin) has the N-terminal peptide, which is cut off before the protein leaves the rough endoplasmic reticulum. The product of this removal (proalbumin) is transported to the Golgi apparatus. In secretory granules, the limited proteolysis occurs and the mature non-glycosylated albumin is secreted into the extracellular environment

. Ligand binding occurs at two primary sites (Sudlow sites I and II) and several secondary ones, the exact number of which is unknown. The structure of albumin is rather labile and tends towards allosteric modulation: binding of a ligand in one site can affect the efficiency of binding in another. When albumin interacts with different substances, the effects of cooperativity and allosteric modulation occurs, which is more prevalent in multimeric macromolecules

[1]. Synthesis occurs in the polysomes of hepatocytes, and in healthy adults, 10–15 g/day of albumin can be produced; this accounts for nearly 10% of total protein synthesis in the liver [8]. While 30% of albumin is maintained in the plasma, the remaining pool is found predominantly in skin and muscle tissue.
The molecule of HSA consists of 585 amino acids forming one polypeptide chain. The length of the primary sequence can be different in albumins of other species; for example, 584 amino acids in bovine serum albumin (BSA) and 583 residues in rat serum albumin (RSA). The amino acid compositions of HSA and RSA are 73.0% identical, of BSA and RSA—69.9%. Molecular weight of HSA based on amino acid composition is 66.439 kDa, BSA—66.267 kDa, RSA—65.871 kDa; however, the values of molecular weight can vary because of post-translational modifications and genetic variants. The secondary structure of the protein contains about 67% helical structures next to 33% of turn and extended chain configurations without any β-sheets [9] (F

. The albumin molecule contains 17 disulfide bonds and one free thiol group in Cys34. The latter largely determines the participation of albumin in redox reactions. The number of disulfide bonds and Cys34 are conserved in all types of albumin.

Enzymatiguc pre 1

). The three-dimensional structure of HSA was resolved rather late, only in the 1990s

operties

Albumin is not only the passive but also active participant of the pharmacokinetic and toxicokinetic processes. Numerous experiments showed the esterase or pseudoesterase activity of albumin against α-naphtylacetate and p-nitrophenylacetate (NPA), fatty acid esters, aspirin, ketoprofene glucuronide, cyclophosphamide, nicotinic acid esters, octanoyl ghrelin , nitroacetanilide, nitrofluoroacetanilide, and organophosphorus pesticides

[10]. A similar structure of BSA was obtained in 2012

. Acetylation is a typical example of the pseudoesterase activity of albumin (the pseudo first order reaction) when the consumption of the substrate is due to not its hydrolysis but the formation of covalent bonds with the participation of many amino acid residues (sites) of the albumin molecule. Acetylation of albumin by NPA was found to occur at 82 amino acids (aa) sites including lysine (59 aa), serine (10 aa), threonine (8 aa), tyrosine (4 aa), and aspartate (1 aa) residues

[11], but the three-dimensional structure of albumin of rats, the principal animals used in pharmacological and toxicological experiments, has not been obtained yet. Three homologous domains (I, II, III), consisting of two subdomains (A, B) form a three-dimensional structure of the protein, which is rather labile (F

, with adducts of acetylation at the lysine residues being more stable.

Of special interest is the phosphatase activity of albumin, i.e. the phosphomonoesterase (EC 3.1.3…?)[12], RNA-hydrolase or phosphodiesterase (EC 3.1.4.16 ?)[13], and phosphotriesterase (EC 3.1.8.1 and 3.1.8.2)[14][15] activities. The subclass 3.1.8 (hydrolases of phosphotriesters) contains aryldialkylphosphatase (EC 3.1.8.1) and diisopropylfluorophosphatase (EC 3.1.8.2) [16][17]. Aryldialkylphosphatase is better known as paraoxonase; this enzyme hydrolyzes esters of tribasic phosphoric acid, of dibasic phosphonic acid, and of monobasic phosphinic acid. The feature of this enzyme is inhibition with chelating agents, because divalent cations (mainly Ca2+) are required for its activity[18]. As it was shown, albumin has all functions of paraoxonase. However, the fundamental difference of albumin is the lack of dependence on Ca2+. This fact is used for the differential analysis of the activities of these enzymes[15][19][20][21]. In toxicology, understanding the mechanistic interactions of organophosphates with albumin is a special problem, and its solution could help in the development of new types of antidotes[22].

Among the other activities of serum albumin, one should note its prostaglandin D synthase and other activities associated with prostanoid metabolism[23][24][25][26][27][28][29][30], particularly catalytic dehydration of 15-keto PGE2 in the Arg257 site with the formation of 15-keto PGA2. Quite exotic activities for albumin are glucuronidase activity (e.g., hydrolysis of S-carprofen glucuronide, nonsteroidal anti-inflammatory drugs, with the participation of tyrosine and lysine residues)[31][32][33] and the enolase activity[34][35]; the significance of the latter is difficult to overestimate with respect to the differential diagnostics of benign and malignant tumors.

In 1986, concern was expressed over the fact that the current classification of esterases did not reflect the real state of things. Albumin was just used as an example of the protein which exhibits the esterase activity but has no place in the classification[36] [36]. Unfortunately, these words were not heard. The broad substrate specificity and no dependence on Ca2+ do not allow for the identification of albumin as any of the enzymes with their numbers in the enzyme nomenclature. The place of albumin in the nomenclature of enzymes remains yet to be determined.

Albumigun and re 1

).

dox modulation

/media/item_content/202204/62568a4f90796encyclopedia-01-00009-g001.png
Figure 1. The structure of serum albumin. Domains I, II and III are shown in purple, blue and green, respectively; each domain consists of two subdomains A and B. The albumin molecule does not contain β-sheets, α-helices are presented as cylinders. To create the figure, a three-dimensional structure of human serum albumin from the PDB database, code 3JQZ

In physiological conditions, about 80% of all detected plasma thiols are albumin thiols[37]. The Cys34 residue is able to neutralise such ROS and RNS as hydrogen peroxide (H2O2), peroxynitrite (ONOO-), superoxide anion and hypochlorous acid (HOCl), being oxidised to sulfenic acid (HSA-SOH)[38][39]. There is a list of the albumin activities associated with redox modulation of blood plasma and intercellular liquid. Here are the thioesterase[40][41], glutathione peroxidase and cysteine peroxidase activities, as well as the peroxidase activity towards lipid hydroperoxides[42][43][44][45]. The important role of two cysteine residues of albumin, Cys392 and Cys438 should be noted, which form redox active disulfide in the complex of albumin with palmitoyl-CoA [45]. Albumin is a trap of radicals due to six methionine residues, but Cys34 is the most important for this function[38][46]. The N-terminal region of human albumin, Asp-Ala-His-Lys, in the complex with cuprum ions has the superoxide dismutase activity[47]. Albumin can stoichiometrically inactivate hydrogen peroxide and peroxynitrite due to reversible oxidation of the Cys34 residue to the sulfenic acid derivative[38]. This group of activities may probably be supplemented by the cyanide detoxification reaction with the formation of thiocyanate, which is catalyzed by the regions of subdomain IIIA without the involvement of Tyr411[48]. Finally, it should be noted the prooxidant properties of albumin, which mean that the albumin-bound Cu2+ ions strengthen the formation of ascorbate radical, followed by oxidation of the formed Cu+ ions by molecular oxygen and protons again to Cu2+[49]. Albumin is usually one of the first proteins to be influenced oxidative stress, therefore its redox status is widely used as a biomarker of various pathological conditions. It is known that in chronic liver and kidney diseases, as well as in diabetes mellitus, the percentage of cysteinylated albumin (Cys34-S-S-Cys) is markedly increased[50]. In recent years, it has been shown that oxidised albumin can be a biomarker of the severity of such diseases as hyperparathyroidism[51], acute ischemic stroke[52], Parkinson's disease[53], Alzheimer disease[54], Duchenne muscular dystrophy[55], etc. Fujii et al.[56] performed a comprehensive study of 281 Japanese residents: the ratio of oxidised/reduced albumin, the thickness of the intima-media complex of the carotid arteries, and the number of plaques in the carotid arteries (the latter two indicators characterise the risk of atherosclerosis) were measured. An inverse relationship was found between the level of oxidised albumin and the risk of atherosclerosis. Violi et al. have recently shown that HSA level is independently associated with mortality in COVID-19

[1257], was used.

. The researchers suggested that it might be connected with antioxidant and anticoagulant properties of albumin.

There are dozens of genetic variants of HSA (for exhaustive list see

In addition to the direct oxidation of Cys34, albumin can undergo other chemical modifications that affect its structure and conformation, which in turn can lead to modulation of its antioxidant properties. Glycation is one of these modifications, which is the covalent binding of glucose or another monosaccharide to the side chains of lysines and arginines[58]. To date, more than 60 albumin glycation sites have been described, but many researchers agree that Lys525 is the most reactive of them[59][60][61]. Modifications caused by glycation have an important effect on the functional properties of albumin, mainly associated with the changes of its conformation. As in the case of the effect of Cys34 oxidation on the binding activity of Sudlow sites, the data on the effect of glycation on the antioxidant properties of albumin are contradictory: in some cases, the antioxidant properties are weakened, while in others, on the contrary, they are enhanced[62][63][64][65]. The review of Rondeau and Bourdon

[658]). Possible effects of some single point mutations on the ligand-binding capabilities of HSA were investigated by studying the interactions between the strongly bound drugs warfarin, salicylate and diazepam, and five structurally characterised genetic variants of the protein

 provides a detailed analysis of the results of various experiments aimed at studying this effect. The authors suggest that the controversial behavior of glycosylated albumin in biochemical experiments might be due to interspecies differences, the nature and concentration of the involved carbohydrates (glucose, methylglyoxal), and the conditions of incubation with monosaccharides. The differences between human and bovine albumin described in the review are of particular interest: glycation of HSA sharply decreases its antioxidant activity, while glycation of BSA tends to enhance its antioxidant properties. These data correlate with the results of computational experiments aimed at studying the effect of the redox status of HSA and BSA on their binding and esterase activity towards paraoxon

[1366]. Equilibrium dialysis data revealed pronounced reductions in high affinity binding of all three ligands to HSA Canterbury (313 Lys→Asn) and to HSA Parklands (365 Asp→His). By contrast, unchanged binding of the drugs was found in the case of HSA Verona (570 Glu→Lys). Salicylate was the only drug bound with a lower affinity to HSA Niigata (269 Asp→Gly), whereas binding of both salicylate and diazepam to HSA Roma (321 Glu→Lys) were moderately reduced. In about half of the cases of diminished binding, the primary association constant was reduced by 1 order of magnitude, giving rise to an increase in the unbound fraction of the drugs of 500% or more at therapeutically relevant molar ratios of drug and protein. Changes in protein charge play minor importance for reduced binding, though conformational changes in the 313–365 region of the proteins seem to be the main cause for diminished binding of these ligands [1367].

. According to the data, human and bovine albumins react differently to the oxidation of Cys34 to sulfenic and sulfinic acids.

Albumin normally is not covered with hydrocarbons and can bind different endogenous and exogenous ligands: water and metal cations, fatty acids, hormones, bilirubin, transferrin, nitric oxide, aspirin, warfarin, ibuprofen, phenylbutazone, etc.

Fatty acids (FAs) appear to play the main role in the regulation of the antioxidant properties of albumin. For the first time, this conclusion was made by Gryzunov and co-authors[49][68]. Binding of FAs changed the conformations of Sudlow sites I and II and increased the fluorescence quantum yield of the probes dansylamide (ligand of Sudlow site I) and dansylsarcosine (ligand of Sudlow site II); also, FAs strenthened the reactivity of Cys34 thiol group towards 5,5'-dithiobis-2-nitrobenzoic acid (DTNB) having increased its steric availability. The authors hypothesised that FAs, when bound to albumin, simultaneously regulated it’s both transport and antioxidant functions, serving as a necessary intermediary between these activities[49]. Roche et al.[38] discuss the ability of albumin to bind polyunsaturated fatty acids (PUFAs) and bilirubin, and thus indirectly further enhance the antioxidant defense of the body. It is known that albumin-bound bilirubin can inhibit lipid peroxidation. Bilirubin binds at Site III of albumin

[1469]. Ligand binding occurs at two primary sites (Sudlow site I in subdomain IIA and Sudlow site II in subdomain IIIA) and several secondary ones. When albumin interacts with different substances, the effects of cooperativity and allosteric modulation occurs, which is usually inherent to multimeric macromolecules

. As for PUFAs, according to the authors, it is possible that in combination with albumin, they are protected from peroxidation. The amino acids Arg117, Lys351, and Lys475 are responsible for the interaction of the protein with PUFA molecules

Therapeutic application of albumin

Attempts are being made to use albumin not only as an informant about the condition of patients, but also as a therapeutic agent. An interesting application of the redox properties of albumin was proposed by Japanese scientists

. It is known that reactive sulfur species (RSS) are able to neutralise ultraviolet radiation products (for example, ROS and NO) that promote melanin synthesis. However, the instability of RSS limits their use as inhibitors of melanin synthesis. The authors proposed a method for using albumin as the RSS delivery system. It was shown that thiolated albumin (obtained by the incubation of albumin and sodium polysulfide) significantly inhibited melanin synthesis in B16 melanoma cells. The researchers also suggested that albumin modified in such way could be used in cosmetology to whiten the skin. In the research of Schneider et al.

[1671]. The albumin molecule contains 17 disulfide bonds and one free thiol group in Cys34, which determines the participation of albumin in redox reactions.

, the possibility of using human albumin solution to protect patients of an intensive care unit (ICU) from bacterial infections was studied. The polypeptide vasostatin-1 is known to have antimicrobial properties and play a key role in protecting the body from gram-positive bacteria. However, the oxidised form of vasostatin loses its antibacterial properties. Oxidative processes are often developed in ICU patients, which means that they are more at risk of infection. The study showed that continuous infusion of 4% albumin reduced the risk of nosocomial infections. By mixing albumin with oxidised vasostatin-1 and using a high-performance liquid chromatography (HPLC) method, the authors demonstrated that albumin reduced the oxidised form of vasostatin, thereby increasing its antibacterial properties.

References

  1. Peters, T., Jr. All about albumin. In Biochemistry, Genetics, and Medical Applications; Academic Press Ltd: London, UK, 1996. Peters, Jr. T. . All about albumin. Biochemistry, genetics, and medical applications. ; Academic Press Ltd: London, 1996; pp. 432.
  2. Haefliger, D.N.; Moskaitis, J.E.; Schoenberg, D.R.; Wahli, W. Amphibian albumins as members of the albumin, alpha-fetoprotein, vitamin D-binding protein multigene family. J. Mol. Evol. 1989, 29, 344–354. Xiao Min He; Daniel C. Carter; Atomic structure and chemistry of human serum albumin. Nature 1992, 358, 209-215, 10.1038/358209a0.
  3. Lichenstein, H.S.; Lyons, D.E.; Wurfel, M.M.; Johnson, D.A.; McGinley, M.D.; Leidli, J.C.; Trollinger, D.B.; Mayer, J.P.; Wright, S.D.; Zukowski, M.M. Afamin is a new member of the albumin, alpha-fetoprotein, and vitamin D-binding protein gene family. J. Biol. Chem. 1994, 269, 18149–18154. Anna Bujacz; Structures of bovine, equine and leporine serum albumin. Acta Crystallographica Section D Biological Crystallography 2012, 68, 1278-1289, 10.1107/s0907444912027047.
  4. Li, S.; Cao, Y.; Geng, F. Genome-Wide Identification and Comparative Analysis of Albumin Family in Vertebrates. Evol. Bioinform. Online 2017, 13, 1176934317716089. K. I. Taborskaya; D. A. Belinskaya; N. V. Goncharov; P. V. Avdonin; Building a three-dimensional model of rat albumin molecule by homology modeling. Journal of Evolutionary Biochemistry and Physiology 2017, 53, 384-393, 10.1134/s0022093017050040.
  5. Nishio, H.; Heiskanen, M.; Palotie, A.; Bélanger, L.; Dugaiczyk, A. Tandem arrangement of the human serum albumin multigene family in the sub-centromeric region of 4q: Evolution and chromosomal direction of transcription. J. Mol. Biol. 1996, 259, 113–119. Gabriel Zazeri; Ana Paula Ribeiro Povinelli; Marcelo De Freitas Lima; Marinônio Lopes Cornélio; Experimental Approaches and Computational Modeling of Rat Serum Albumin and Its Interaction with Piperine. International Journal of Molecular Sciences 2019, 20, 2856, 10.3390/ijms20122856.
  6. Albumin. Available online: http://albumin.org/ (accessed on 22 December 2020).D. Carter; X. He; Structure of human serum albumin. Science 1990, 249, 302-303, 10.1126/science.2374930.
  7. Godin, R.E.; Urry, L.A.; Ernst, S.G. Alternative splicing of the Endo16 transcript produces differentially expressed mRNAs during sea urchin gastrulation. Dev. Biol. 1996, 179, 148–159. Mauro Fasano; Stephen Curry; Enzo Terreno; Monica Galliano; Gabriella Fanali; Pasquale Narciso; Stefania Notari; Paolo Ascenzi; The extraordinary ligand binding properties of human serum albumin. IUBMB Life 2005, 57, 787-796, 10.1080/15216540500404093.
  8. Quinlan, G.J.; Martin, G.S.; Evans, T.W. Albumin: Biochemical properties and therapeutic potential. Hepatology 2005, 41, 1211–1219. Paolo Ascenzi; Alessio Bocedi; Stefania Notari; Gabriella Fanali; Riccardo Fesce; Mauro Fasano; Allosteric Modulation of Drug Binding to Human Serum Albumin. Mini-Reviews in Medicinal Chemistry 2006, 6, 483-489, 10.2174/138955706776361448.
  9. Lu, R.; Li, W.W.; Katzir, A.; Raichlin, Y.; Yu, H.Q.; Mizaikoff, B. Probing the secondary structure of bovine serum albumin during heat-induced denaturation using mid-infrared fiberoptic sensors. Analyst 2015, 140, 765–770. Paolo Ascenzi; Mauro Fasano; Allostery in a monomeric protein: The case of human serum albumin. Biophysical Chemistry 2010, 148, 16-22, 10.1016/j.bpc.2010.03.001.
  10. He, X.M.; Carter, D.C. Atomic structure and chemistry of human serum albumin. Nature 1992, 358, 209–215. N. V. Goncharov; D. A. Belinskaya; A.V. Razygraev; A. I. Ukolov; On the enzymatic activity of albumin. Russian Journal of Bioorganic Chemistry 2015, 41, 113-124, 10.1134/s1068162015020041.
  11. Bujacz, A. Structures of bovine, equine and leporine serum albumin. Acta Crystallogr. D Biol. Crystallogr. 2012, 68, 1278–1289. Oksana Lockridge; Weihua Xue; Andrea Gaydess; Hasmik Grigoryan; Shi-Jian Ding; Lawrence M. Schopfer; Steven H. Hinrichs; Patrick Masson; Pseudo-esterase Activity of Human Albumin. Journal of Biological Chemistry 2008, 283, 22582-22590, 10.1074/jbc.m802555200.
  12. Hein, K.L.; Kragh-Hansen, U.; Morth, J.P.; Jeppesen, M.D.; Otzen, D.; Møller, J.V.; Nissen, P. Crystallographic analysis reveals a unique lidocaine binding site on human serum albumin. J. Struct. Biol. 2010, 171, 353–360. C H Kwon; K Maddison; L LoCastro; R F Borch; Accelerated decomposition of 4-hydroxycyclophosphamide by human serum albumin.. Cancer Research 1987, 47, 1505–1508.
  13. Kragh-Hansen, U.; Brennan, S.O.; Galliano, M.; Sugita, O. Binding of warfarin, salicylate, and diazepam to genetic variants of human serum albumin with known mutations. Mol. Pharmacol. 1990, 37, 238–242. Yulia V. Gerasimova; Tatyana V. Bobik; Natalia Ponomarenko; Makhmut M. Shakirov; Marina A. Zenkova; Nikolai V. Tamkovich; Tatyana V. Popova; Dmitry G. Knorre; Tatyana S. Godovikova; RNA-hydrolyzing activity of human serum albumin and its recombinant analogue. Bioorganic & Medicinal Chemistry Letters 2010, 20, 1427-1431, 10.1016/j.bmcl.2009.12.095.
  14. Fasano, M.; Curry, S.; Terreno, E.; Galliano, M.; Fanali, G.; Narciso, P.; Notari, S.; Ascenzi, P. The extraordinary ligand binding properties of human serum albumin. IUBMB Life 2005, 57, 787–796. Bin Li; Florian Nachon; Marie-Thérèse Froment; Laurent Verdier; Jean-Claude Debouzy; Bernardo Brasme; Emilie Gillon; Lawrence M. Schopfer; Oksana Lockridge; Patrick Masson; et al. Binding and Hydrolysis of Soman by Human Serum Albumin. Chemical Research in Toxicology 2008, 21, 421-431, 10.1021/tx700339m.
  15. Ascenzi, P.; Bocedi, A.; Notari, S.; Fanali, G.; Fesce, R.; Fasano, M. Allosteric modulation of drug binding to human serum albumin. Mini Rev. Med. Chem. 2006, 6, 483–489. Miguel A. Sogorb; Sara García-Argüelles; Victoria Carrera; Eugenio Vilanova; Serum Albumin is as Efficient as Paraxonase in the Detoxication of Paraoxon at Toxicologically Relevant Concentrations. Chemical Research in Toxicology 2008, 21, 1524-1529, 10.1021/tx800075x.
  16. Ascenzi, P.; Fasano, M. Allostery in a monomeric protein: The case of human serum albumin. Biophys. Chem. 2010, 148, 16–22. Nomenclature Committee of the International Union of Biochemistry and Molecular Biology (NC-IUBMB). The Enzyme List, Class 3—Hydrolases. Generated from the ExplorEnz database. September 2010. Available online: http://www.enzyme-database.org/downloads/ec3.pdf (accessed on 29 October 2020).
  17. Schomburg, D.; Schomburg, I. . Springer Handbook of Enzymes. EC Number Index. Class 2–3.2 Transferases, Hydrolases.; Schomburg, D.; Schomburg, I. , Eds.; Springer-Verlag: Heidelberg/Berlin, Germany; New York, NY, USA, 2013; pp. 698.
  18. Kurdyukov, I.D.; Shmurak, V.I.; Nadeev, A.D.; Voitenko, N.G.; Prokofieva, D.S.; Goncharov, N.V.; “Esterase status” of an organism at exposure by toxic substances and pharmaceuticals. Toksikol. Vestnik (Toxicol. Bull.) 2012, 6, 6-13.
  19. Miguel A Sogorb; Eugenio Vilanova; Enzymes involved in the detoxification of organophosphorus, carbamate and pyrethroid insecticides through hydrolysis. Toxicology Letters 2002, 128, 215-228, 10.1016/s0378-4274(01)00543-4.
  20. Miguel A. Sogorb; Eugenio Vilanova; Serum albumins and detoxication of anti-cholinesterase agents. Chemico-Biological Interactions 2010, 187, 325-329, 10.1016/j.cbi.2010.03.001.
  21. Miguel A. Sogorb; Victoria Carrera; Eugenio Vilanova; Hydrolysis of carbaryl by human serum albumin. Archives of Toxicology 2004, 78, 629-634, 10.1007/s00204-004-0584-x.
  22. Nikolay V. Goncharov; Daria A. Belinskaia; Vladimir I. Shmurak; Maxim A. Terpilowski; R. O. Jenkins; Pavel V. Avdonin; Serum Albumin Binding and Esterase Activity: Mechanistic Interactions with Organophosphates. Molecules 2017, 22, 1201, 10.3390/molecules22071201.
  23. T Watanabe; S Narumiya; T Shimizu; O Hayaishi; Characterization of the biosynthetic pathway of prostaglandin D2 in human platelet-rich plasma. Journal of Biological Chemistry 1982, 257, 14847–14853.
  24. F A Fitzpatrick; M A Wynalda; Albumin-catalyzed metabolism of prostaglandin D2. Identification of products formed in vitro. Journal of Biological Chemistry 1983, 258, 11713–11718.
  25. Y. Kikawa; S. Narumiya; M. Fukushima; H. Wakatsuka; O. Hayaishi; 9-Deoxy-delta 9, delta 12-13,14-dihydroprostaglandin D2, a metabolite of prostaglandin D2 formed in human plasma.. Proceedings of the National Academy of Sciences 1984, 81, 1317-1321, 10.1073/pnas.81.5.1317.
  26. F A Fitzpatrick; W F Liggett; M A Wynalda; Albumin-eicosanoid interactions. A model system to determine their attributes and inhibition.. Journal of Biological Chemistry 1984, 259, 2722–2727.
  27. Jinsheng Yang; Charles E. Petersen; Chung-Eun Ha; Nadhipuram V Bhagavan; Structural insights into human serum albumin-mediated prostaglandin catalysis. Protein Science 2002, 11, 538-545, 10.1110/ps.28702.
  28. Michael J. Kimzey; Hussein N. Yassine; Brent M. Riepel; George Tsaprailis; Terrence J. Monks; Serrine S. Lau; New site(s) of methylglyoxal-modified human serum albumin, identified by multiple reaction monitoring, alter warfarin binding and prostaglandin metabolism. Chemico-Biological Interactions 2011, 192, 122-128, 10.1016/j.cbi.2010.09.032.
  29. Satoru Yamaguchi; Giancarlo Aldini; Sohei Ito; Nozomi Morishita; Takahiro Shibata; Giulio Vistoli; Marina Carini; Koji Uchida; Δ12-Prostaglandin J2as a Product and Ligand of Human Serum Albumin: Formation of an Unusual Covalent Adduct at His146. Journal of the American Chemical Society 2010, 132, 824-832, 10.1021/ja908878n.
  30. M.A. Wynalda; F.A. Fitzpatrick; Albumins stabilize prostaglandin I2. Prostaglandins 1980, 20, 853-861, 10.1016/0090-6980(80)90138-0.
  31. N Dubois-Presle; F Lapicque; M H Maurice; S Fournel-Gigleux; J Magdalou; M Abiteboul; G Siest; P Netter; Stereoselective esterase activity of human serum albumin toward ketoprofen glucuronide.. Molecular Pharmacology 1995, 47, 647-653.
  32. Hélène Georges; Nathalie Presle; Thierry Buronfosse; Sylvie Fournel-Gigleux; Patrick Netter; Jacques Magdalou; Françoise Lapicque; In vitro stereoselective degradation of carprofen glucuronide by human serum albumin. Characterization of sites and reactive amino acids. Chirality 2000, 12, 53-62, 10.1002/(sici)1520-636x(2000)12:2<53::aid-chir1>3.3.co;2-t.
  33. Adrienne M. Williams; Ronald G. Dickinson; Studies on the reactivity of acyl glucuronides—VI. Biochemical Pharmacology 1994, 47, 457-467, 10.1016/0006-2952(94)90176-7.
  34. Z Drmanovic; S Voyatzi; D Kouretas; D Sahpazidou; A Papageorgiou; O Antonoglou; Albumin possesses intrinsic enolase activity towards dihydrotestosterone which can differentiate benign from malignant breast tumors. Anticancer Research 1999, 19, 4113–4124.
  35. Sadaharu Matsushita; Yu Isima; Victor T. Giam Chuang; Hiroshi Watanabe; Sumio Tanase; Toru Maruyama; Masaki Otagiri; Functional Analysis of Recombinant Human Serum Albumin Domains for Pharmaceutical Applications. Pharmaceutical Research 2004, 21, 1924-1932, 10.1023/b:pham.0000045248.03337.0e.
  36. J Pen; J J Beintema; Nomenclature of esterases. Biochemical Journal 1986, 240, 933, 10.1042/bj2400933.
  37. Lucía Turell; Rafael Radi; Beatriz Alvarez; The thiol pool in human plasma: The central contribution of albumin to redox processes. Free Radical Biology and Medicine 2013, 65, 244-253, 10.1016/j.freeradbiomed.2013.05.050.
  38. Marjolaine Roche; Philippe Rondeau; Nihar Ranjan Singh; Evelyne Tarnus; Emmanuel Bourdon; The antioxidant properties of serum albumin. FEBS Letters 2008, 582, 1783-1787, 10.1016/j.febslet.2008.04.057.
  39. Myriam Taverna; Anne-Lise Marie; Jean-Paul Mira; Bertrand Guidet; Specific antioxidant properties of human serum albumin. Annals of Intensive Care 2013, 3, 4, 10.1186/2110-5820-3-4.
  40. Anders Overgaard Pedersen; Jørgen Jacobsen; Reactivity of the Thiol Group in Human and Bovine Albumin at pH 3-9, as Measured by Exchange with 2,2′-Dithiodipyridine. JBIC Journal of Biological Inorganic Chemistry 1980, 106, 291-295, 10.1111/j.1432-1033.1980.tb06022.x.
  41. Raghunath P. Agarwal; Michael Phillips; Richard A. McPherson; Preston Hensley; Serum albumin and the metabolism of disulfiram. Biochemical Pharmacology 1986, 35, 3341-3347, 10.1016/0006-2952(86)90433-8.
  42. Harald John; Felicitas Breyer; Jörg Oliver Thumfart; Hans Höchstetter; Horst Thiermann; Jörg Oliver Thumfart; Matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF MS) for detection and identification of albumin phosphylation by organophosphorus pesticides and G- and V-type nerve agents. Analytical and Bioanalytical Chemistry 2010, 398, 2677-2691, 10.1007/s00216-010-4076-y.
  43. Rachel Hurst; Yong-Ping Bao; Saxon Ridley; Gary Williamson; Phospholipid hydroperoxide cysteine peroxidase activity of human serum albumin. Biochemical Journal 1999, 338, 723-728, 10.1042/0264-6021:3380723.
  44. Mee-Kyung Cha; Il-Han Kim; Glutathione-Linked Thiol Peroxidase Activity of Human Serum Albumin: A Possible Antioxidant Role of Serum Albumin in Blood Plasma. Biochemical and Biophysical Research Communications 1996, 222, 619-625, 10.1006/bbrc.1996.0793.
  45. Heeyong Lee; I H Kim; Thioredoxin-linked lipid hydroperoxide peroxidase activity of human serum albumin in the presence of palmitoyl coenzyme A. Free Radical Biology and Medicine 2001, 30, 327-333, 10.1016/s0891-5849(00)00483-4.
  46. Yasunori Iwao; Yu Ishima; Junji Yamada; Taishi Noguchi; Ulrich Kragh-Hansen; Katsumi Mera; Daisuke Honda; Ayaka Suenaga; Toru Maruyama; Masaki Otagiri; et al. Quantitative evaluation of the role of cysteine and methionine residues in the antioxidant activity of human serum albumin using recombinant mutants. IUBMB Life 2012, 64, 450-454, 10.1002/iub.567.
  47. David Bar-Or; Leonard T. Rael; Edward P. Lau; Nagaraja K.R. Rao; Gregory W. Thomas; James V. Winkler; Richard L. Yukl; Robert G. Kingston; C.Gerald Curtis; An Analog of the Human Albumin N-Terminus (Asp-Ala-His-Lys) Prevents Formation of Copper-Induced Reactive Oxygen Species. Biochemical and Biophysical Research Communications 2001, 284, 856-862, 10.1006/bbrc.2001.5042.
  48. Rebecca Jarabak; John Westley; Localization of the sulfur-cyanolysis site of serum albumin to subdomain 3-ab. Journal of Biochemical Toxicology 1991, 6, 65-70, 10.1002/jbt.2570060109.
  49. Y.A. Gryzunov; A. Arroyo; J.-L. Vigne; Q. Zhao; V.A. Tyurin; C.A. Hubel; R.E. Gandley; Y.A. Vladimirov; R.N. Taylor; V.E. Kagan; et al. Binding of fatty acids facilitates oxidation of cysteine-34 and converts copper–albumin complexes from antioxidants to prooxidants. Archives of Biochemistry and Biophysics 2003, 413, 53-66, 10.1016/s0003-9861(03)00091-2.
  50. Kohei Nagumo; Motohiko Tanaka; Victor Tuan Giam Chuang; Hiroko Setoyama; Hiroshi Watanabe; Naoyuki Yamada; Kazuyuki Kubota; Kazutaka Matsushita; Akira Yoshida; Hideaki Jinnouchi; et al.Makoto AnrakuDaisuke KadowakiYu IshimaYutaka SasakiMasaki OtagiriToru Maruyama Cys34-Cysteinylated Human Serum Albumin Is a Sensitive Plasma Marker in Oxidative Stress-Related Chronic Diseases. PLOS ONE 2014, 9, e85216, 10.1371/journal.pone.0085216.
  51. Wesam Ahmad Nasif; Mohammed H. Mukhtar; Hoda M. El-Emshaty; Ahmed H. Alwazna; Redox State of Human Serum Albumin and Inflammatory Biomarkers in Hemodialysis Patients with Secondary Hyperparathyroidism During Oral Calcitriol Supplementation for Vitamin D. The Open Medicinal Chemistry Journal 2018, 12, 98-110, 10.2174/1874104501812010098.
  52. Leonard T. Rael; Jan Leonard; Kristin Salottolo; Raphael Bar-Or; Russell E. Bartt; Jeffrey C. Wagner; David Bar-Or; Plasma Oxidized Albumin in Acute Ischemic Stroke Is Associated With Better Outcomes. Frontiers in Neurology 2019, 10, 709, 10.3389/fneur.2019.00709.
  53. Shin‐Ichi Ueno; Taku Hatano; Ayami Okuzumi; Shinji Saiki; Yutaka Oji; Akio Mori; Takahiro Koinuma; Motoki Fujimaki; Haruka Takeshige‐Amano; Akihide Kondo; et al.Naoyuki YoshikawaTakahiro NojiriMakoto KuranoKeiko YasukawaYutaka YatomiHitoshi IkedaNobutaka Hattori Nonmercaptalbumin as an oxidative stress marker in Parkinson’s and PARK2 disease. Annals of Clinical and Translational Neurology 2020, 7, 307-317, 10.1002/acn3.50990.
  54. Montserrat Costa; Raquel Horrillo; Ana María Ortiz; Alba Pérez; Anna Mestre; Agustín Ruiz; Mercè Boada; Salvador Grancha; Increased Albumin Oxidation in Cerebrospinal Fluid and Plasma from Alzheimer’s Disease Patients. Journal of Alzheimer's Disease 2018, 63, 1395-1404, 10.3233/jad-180243.
  55. Miranda D. Grounds; Jessica R. Terrill; Basma A. Al-Mshhdani; Marisa N. Duong; Hannah G. Radley-Crabb; Peter G. Arthur; Biomarkers for Duchenne muscular dystrophy: myonecrosis, inflammation and oxidative stress. Disease Models & Mechanisms 2020, 13, dmm043638, 10.1242/dmm.043638.
  56. Ryosuke Fujii; Jun Ueyama; Arisa Aoi; Naohiro Ichino; Keisuke Osakabe; Keiko Sugimoto; Koji Suzuki; Nobuyuki Hamajima; Kenji Wakai; Takaaki Kondo; et al. Oxidized human serum albumin as a possible correlation factor for atherosclerosis in a rural Japanese population: the results of the Yakumo Study. Environmental Health and Preventive Medicine 2018, 23, 1-7, 10.1186/s12199-017-0690-z.
  57. Francesco Violi; Roberto Cangemi; Giulio Francesco Romiti; Giancarlo Ceccarelli; Alessandra Oliva; Francesco Alessandri; Matteo Pirro; Pasquale Pignatelli; Miriam Lichtner; Anna Carraro; et al.Francesco CipolloneDamiano D'ardesFrancesco PuglieseClaudio Maria Mastroianni Is Albumin Predictor of Mortality in COVID-19?. Antioxidants & Redox Signaling 2020, Online ahead of print, Online ahead of print, 10.1089/ars.2020.8142.
  58. Philippe Rondeau; Emmanuel Bourdon; The glycation of albumin: Structural and functional impacts. Biochimie 2011, 93, 645-658, 10.1016/j.biochi.2010.12.003.
  59. Jeanethe Anguizola; Ryan Matsuda; Omar S. Barnaby; K.S. Hoy; Chunling Wa; Erin DeBolt; Michelle Koke; David S. Hage; Review: Glycation of human serum albumin. Clinica Chimica Acta 2013, 425, 64-76, 10.1016/j.cca.2013.07.013.
  60. Alena Soboleva; Gregory Mavropolo-Stolyarenko; Tatiana Karonova; Domenika Thieme; Wolfgang Hoehenwarter; Christian Ihling; Vasily E. Stefanov; Tatiana Grishina; Andrej Frolov; Multiple Glycation Sites in Blood Plasma Proteins as an Integrated Biomarker of Type 2 Diabetes Mellitus.. International Journal of Molecular Sciences 2019, 20, 2329, 10.3390/ijms20092329.
  61. Hongyan Qiu; Lan Jin; Jian Chen; Min Shi; Feng Shi; Mansen Wang; Daoyuan Li; Xiaohui Xu; Xinhuan Su; Xianlun Yin; et al.Wenhua LiXiaoMing ZhouRobert J. LinhardtZhe WangLianli ChiQunye Zhang Comprehensive Glycomic Analysis Reveals That Human Serum Albumin Glycation Specifically Affects the Pharmacokinetics and Efficacy of Different Anticoagulant Drugs in Diabetes. Diabetes 2020, 69, 760-770, 10.2337/db19-0738.
  62. Emmanuel Bourdon; Nadine Loreau; Denis Blache; Glucose and free radicals impair the antioxidant properties of serum albumin. The FASEB Journal 1999, 13, 233-244, 10.1096/fasebj.13.2.233.
  63. Serge Chesne; Philippe Rondeau; Sergio Armenta; Emmanuel Bourdon; Effects of oxidative modifications induced by the glycation of bovine serum albumin on its structure and on cultured adipose cells. Biochimie 2006, 88, 1467-1477, 10.1016/j.biochi.2006.05.011.
  64. Philippe Rondeau; Nihar Ranjan Singh; Henri Caillens; Frank Tallet; Emmanuel Bourdon; Oxidative stresses induced by glycoxidized human or bovine serum albumin on human monocytes. Free Radical Biology and Medicine 2008, 45, 799-812, 10.1016/j.freeradbiomed.2008.06.004.
  65. Alma Martinez Fernandez; Luca Regazzoni; Maura Brioschi; Erica Gianazza; Piergiuseppe Agostoni; Giancarlo Aldini; Cristina Banfi; Pro-oxidant and pro-inflammatory effects of glycated albumin on cardiomyocytes. Free Radical Biology and Medicine 2019, 144, 245-255, 10.1016/j.freeradbiomed.2019.06.023.
  66. D. A. Belinskaia; M. A. Terpilovskii; A. A. Batalova; N. V. Goncharov; Effect of Cys34 Oxidation State of Albumin on Its Interaction with Paraoxon according to Molecular Modeling Data. Russian Journal of Bioorganic Chemistry 2019, 45, 535-544, 10.1134/s1068162019060086.
  67. D. A. Belinskaia; A.A. Batalova; N.V. Goncharov; Effect of the bovine serum albumin redox state on its interaction with paraoxon as determined by molecular modeling [Article in Russian].. J. Evol. Biochem. Physiol. 2020, 56, 376-379, 10.31857/s004445292003002x.
  68. 68. Gryzunov, Y.A. Properties of albumin binding centers: a method of their exploration in biological fluids and its trial for evaluation of the organism status [In Russian]. Thesis for the degree of Doctor of Sciences (Doktor nauk). Federal research and clinical center of physical-chemical medicine. Moscow, Russia. 2003.
  69. Patricia A. Zunszain; Jamie Ghuman; Antony F. McDonagh; Stephen Curry; Crystallographic Analysis of Human Serum Albumin Complexed with 4Z,15E-Bilirubin-IXα. Journal of Molecular Biology 2008, 381, 394-406, 10.1016/j.jmb.2008.06.016.
  70. Mayumi Ikeda; Yu Ishima; Ryo Kinoshita; Victor T.G. Chuang; Nanami Tasaka; Nana Matsuo; Hiroshi Watanabe; Taro Shimizu; Tatsuhiro Ishida; Masaki Otagiri; et al.Toru Maruyama A novel S-sulfhydrated human serum albumin preparation suppresses melanin synthesis.. Redox Biology 2018, 14, 354-360, 10.1016/j.redox.2017.10.007.
  71. Francis Schneider; Anne-Florence Dureau; Sophie Hellé; Cosette Betscha; Bernard Senger; Gérard Cremel; Fouzia Boulmedais; Jean-Marc Strub; Angelo Corti; Nicolas Meyer; et al.Max GuillotPierre SchaafMarie-Hélène Metz-Boutigue A Pilot Study on Continuous Infusion of 4% Albumin in Critically Ill Patients. Critical Care Explorations 2019, 1, e0044, 10.1097/cce.0000000000000044.
More
© Text is available under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/)
ScholarVision Creations
Feedback