An overview of albumin and alpha-1-acid glycoprotein main characteristics: highlighting the roles of amino acids in binding kinetics and molecular interactions

Bteich, Michel

doi:10.1016/j.heliyon.2019.e02879

Cited by 96 publications

(94 citation statements)

References 94 publications

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“…However, the three-dimensional structure of albumin of rats—the principal animals used in pharmacological and toxicological experiments—has not been obtained yet. Considering the fact that albumin is able to bind almost all known drugs and toxic substances [ 65 , 66 ], this gap should be filled out. The percentage of identity of the primary structures of HSA and RSA is 73.0%, BSA and RSA—69.9%.…”

Section: Structural Characteristics Of Albumin and Their Interspecmentioning

confidence: 99%

The Universal Soldier: Enzymatic and Non-Enzymatic Antioxidant Functions of Serum Albumin

et al. 2020

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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.

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Section: Structural Characteristics Of Albumin and Their Interspecmentioning

confidence: 99%

The Universal Soldier: Enzymatic and Non-Enzymatic Antioxidant Functions of Serum Albumin

et al. 2020

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“…In the human, recombinant human serum albumin is an effective substitute for albumin purified from blood ( Bungum et al, 2002 ) and is less likely to introduce non-defined molecules into the culture medium. It should also be recognized that BSA is a biologically active molecule that can bind a host of small molecules, including long-chain fatty acids, bilirubin, tryptophan, thyroxine, hemins, heavy metals, and vitamins ( Kragh-Hansen et al, 2002 ; Bteich, 2019 ). Other proteins may provide a better environment for the embryo than BSA.…”

Section: Some Ways Forwardmentioning

confidence: 99%

The incompletely fulfilled promise of embryo transfer in cattle—why aren’t pregnancy rates greater and what can we do about it?

Hansen

2020

Journal of Animal Science

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Typically, bovine embryos are transferred into recipient females about day 7 after estrus or anticipated ovulation, when the embryo has reached the blastocyst stage of development. All the biological and technical causes for failure of a female to produce a blastocyst 7 d after natural or artificial insemination (AI) are avoided when a blastocyst-stage embryo is transferred into the female. It is reasonable to expect, therefore, that pregnancy success would be higher for embryo transfer (ET) recipients than for inseminated females. This expectation is not usually met unless the recipient is exposed to heat stress or is classified as a repeat-breeder female. Rather, pregnancy success is generally similar for ET and AI. The implication is that either one or more of the technical aspects of ET have not yet been optimized or that underlying female fertility that causes an embryo to die before day 7 also causes it to die later in pregnancy. Improvements in pregnancy success after ET will depend upon making a better embryo, improving uterine receptivity, and forging new tools for production and transfer of embryos. Key to accelerating progress in improving pregnancy rates will be the identification of phenotypes or phenomes that allow the prediction of embryo competence for survival and maternal capacity to support embryonic development.

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“…As shown in Figure A5 and Figure S1 , we found that hAGP had partial amino acid sequence similarity to CLases from C. noctiluca and V. hilgendorfii mainly in the region that includes amino acid residues involved in the drug-binding ability of hAGP [ 34 ]. When we focused on CLase, we noticed that the partial amino acid sequences probably included amino acid residues responsible for the luciferase activity based on the previous study of truncated CLases [ 38 , 39 ].…”

Section: Discussionmentioning

confidence: 99%

“…Numbers in parentheses indicate the positions of initial and last amino acid residues. Red characters indicate amino acids involved in the drug-binding ability of hAGP [ 34 ]. Navy-shaded characters marked with an asterisk (*) indicate identical amino acid residues.…”

Section: Figure A1mentioning

confidence: 99%

“…For further understanding of Cypridina bioluminescence through Goto’s hypothesis, we focused on human plasma alpha 1-acid glycoprotein (hAGP), also called orosomucoid. The glycoprotein hAGP is a plasma protein-like serum albumin and has one hydrophobic cavity responsible for its binding to basic drugs [ 34 , 35 , 36 ]. Chlorpromazine (CPZ) is one of the basic drugs that bind to hAGP ( Figure 1 ), and the cocrystal structure analysis showed that CPZ bound to the hydrophobic cavity [ 35 ].…”

Section: Introductionmentioning

confidence: 99%

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Luminescence of Cypridina Luciferin in the Presence of Human Plasma Alpha 1-Acid Glycoprotein

Kanie

Komatsu

Mitani

2020

IJMS

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The enzyme Cypridina luciferase (CLase) enables Cypridina luciferin to emit light efficiently through an oxidation reaction. The catalytic mechanism on the substrate of CLase has been studied, but the details remain to be clarified. Here, we examined the luminescence of Cypridina luciferin in the presence of several proteins with drug-binding ability. Luminescence measurements showed that the mixture of human plasma alpha 1-acid glycoprotein (hAGP) and Cypridina luciferin produced light. The total value of the luminescence intensity over 60 s was over 12.6-fold higher than those in the presence of ovalbumin, human serum albumin, or bovine serum albumin. In the presence of heat-treated hAGP, the luminescence intensity of Cypridina luciferin was lower than in the presence of intact hAGP. Chlorpromazine, which binds to hAGP, showed an inhibitory effect on the luminescence of Cypridina luciferin, both in the presence of hAGP and a recombinant CLase. Furthermore, BlastP analysis showed that hAGP had partial amino acid sequence similarity to known CLases in the region including amino acid residues involved in the drug-binding ability of hAGP. These findings indicate enzymological similarity between hAGP and CLase and provide insights into both the enzymological understanding of CLase and development of a luminescence detection method for hAGP.

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An overview of albumin and alpha-1-acid glycoprotein main characteristics: highlighting the roles of amino acids in binding kinetics and molecular interactions

Cited by 96 publications

References 94 publications

The Universal Soldier: Enzymatic and Non-Enzymatic Antioxidant Functions of Serum Albumin

The Universal Soldier: Enzymatic and Non-Enzymatic Antioxidant Functions of Serum Albumin

The incompletely fulfilled promise of embryo transfer in cattle—why aren’t pregnancy rates greater and what can we do about it?

Luminescence of Cypridina Luciferin in the Presence of Human Plasma Alpha 1-Acid Glycoprotein

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