Glucosylated Albumin and Its Influence on Salicylate Binding

Mereish, Kulthoum A; Rosenberg, H.; Cobby, J. M.

doi:10.1002/jps.2600710223

Cited by 46 publications

(21 citation statements)

References 13 publications

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“…Conflicting findings have been reported on the affinity of glycated albumin to site I or II high-affinity binding drugs. [38][39][40][41][42] Methylglyoxal-derived hydroimidazolone is also a major glycation adduct of albumin and esterase activity of HSA modified by methylglyoxal to p-nitrophenyl acetate decreased. 43) Since the extent of modification, however, is small, the effect of methylglyoxal-derived hydroimidazolone can be hardly considered the cause.…”

Section: Discussionmentioning

confidence: 99%

Differences in Esterase Activity to Aspirin and <i>p</i>-Nitrophenyl Acetate among Human Serum Albumin Preparations

Tatsumi

Okada

Inagaki

et al. 2016

Biological & Pharmaceutical Bulletin

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Human serum albumin (HSA) has two major ligand-binding sites, sites I and II, and also hydrolyzes some compounds at both sites. In the present study, we investigated differences in esterase activity among HSA preparations, and also the effects of warfarin, indomethacin, and naproxen on the hydrolytic activities of HSA to aspirin and p-nitrophenyl acetate. The esterase activities of HSA to aspirin or p-nitrophenyl acetate were measured from the pseudo-first-order formation rate constant (k obs ) of salicylic acid or p-nitrophenol by HSA. Inter-lot variations were observed in the esterase activities of HSA to aspirin and p-nitrophenyl acetate; however, the esterase activity of HSA to aspirin did not correlate with that to p-nitrophenyl acetate. The inhibitory effects of warfarin and indomethacin on the esterase activity of HSA to aspirin were stronger than that of naproxen. In contrast, the inhibitory effect of naproxen on the esterase activity of HSA to p-nitrophenyl acetate was stronger than those of warfarin and indomethacin. These results suggest that the administration of different commercial HSA preparations and the co-administration with site I or II high-affinity binding drugs may change the pharmacokinetic profiles of drugs that are hydrolyzed by HSA.

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Section: Discussionmentioning

confidence: 99%

Differences in Esterase Activity to Aspirin and <i>p</i>-Nitrophenyl Acetate among Human Serum Albumin Preparations

Tatsumi

Okada

Inagaki

et al. 2016

Biological & Pharmaceutical Bulletin

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“…Alterations in drug and bilirubin binding capacity in vitro have been reported for glycosylated albumin [33,34]. However, relevant studies have not been performed in vivo to establish that, even in severe hyperglycaemia, glycosylation of albumin would be sufficient to compromise its physiological functions; for example, in the binding, transport and delivery of fatty acids.…”

Section: Plasma Proteinsmentioning

confidence: 99%

Non-enzymatic glycosylation and the chronic complications of diabetes: an overview

Kennedy¹,

1984

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“…This process, known as glycation, is a slow non-enzymatic reaction that initially involves the reaction of glucose with free amine groups on HSA to form a reversible Schiff base linkage, giving a glycosylamine residue [6][7][8]. The first step of this process is reversible; however, the glycosylamine can later undergo an Amadori rearrangement to form a stable fructosamine residue (i.e., an early stage glycation product).…”

Section: Introductionmentioning

confidence: 99%

“…These modifications are of interest since past studies have suggested that the glycation of HSA can lead to alterations in the binding of this protein to drugs such as phenytoin, salicylate, ibuprofen, phenylbutazone and warfarin [8,[21][22][23][24]. Furthermore, the effect of glycation appears to vary between different binding regions on HSA [23,24].…”

Section: Introductionmentioning

confidence: 99%

Characterization of glycation adducts on human serum albumin by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry

Cerny

Clarke³

et al. 2007

Clinica Chimica Acta

108

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Background-Non-enzymatic glycation of human serum albumin (HSA) is associated with the long-term complications of diabetes. We examined the structure and location of modifications on minimally glycated HSA and considered their possible impact on the binding of drugs to this protein.Methods-Minimally glycated and normal HSA (used as a control) were digested with trypsin, Glu-C or Lys-C, followed by fractionation of the resulting peptides and their analysis by matrixassisted laser desorption/ionization mass spectrometry (MALDI-TOF MS) to determine the structures and locations of glycation adducts.Results-Several specific lysine and arginine residues were identified as modification sites in minimally glycated HSA. Residues K12, K51, K199, K205, K439 and K538 were found to be modified through the formation of fructosyl-lysine, while the modification of K159 and K286 involved the formation of pyrraline, N ε -carboxymethyl-lysine respectively. Lysine K378 was found to give N ε -carboxyethyl-lysine in some forms of glycated HSA but fructosyl-lysine in other forms. Residues R160 and R472 produced a modification based on N ε -(5-hydro-4-imidazolon-2-yl) ornithine. Lysine R222 was modified to produce argpyrimidine, N ε -[5-(2,3,4-trihydroxybutyl)-5-hydro-4-imidazolon-2-yl]ornithine or tetrahydropyrimidine.Conclusions-With the exception of K12, K199, K378, K439 and K525, all of the observed sites of modification for minimally glycated HSA were new to this current study. The fact that many of these glycation-related modifications are located at or near known drug binding sites on HSA explains why some differences have been previously noted in the binding of certain drugs to normal vs glycated HSA.

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Glucosylated Albumin and Its Influence on Salicylate Binding

Cited by 46 publications

References 13 publications

Differences in Esterase Activity to Aspirin and <i>p</i>-Nitrophenyl Acetate among Human Serum Albumin Preparations

Differences in Esterase Activity to Aspirin and <i>p</i>-Nitrophenyl Acetate among Human Serum Albumin Preparations

Non-enzymatic glycosylation and the chronic complications of diabetes: an overview

Characterization of glycation adducts on human serum albumin by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry

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