The effect of glycation on the structure, function and biological fate of human serum albumin as revealed by recombinant mutants

Nakajou, Keisuke; Watanabe, Hiroshi; Kragh‐Hansen, Ulrich; Maruyama, Toru; Otagiri, Masaki

doi:10.1016/j.bbagen.2003.08.001

Cited by 141 publications

(137 citation statements)

References 36 publications

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“…8,9,[30][31][32][33] The binding modes of these dansylated amino acids were largely confirmed by a recent structural study by Curry and coworkers. 34 They showed that ansyl-L-asparagine (DanN), dansyl-L-glutamate (DanE) and dansyl-L-arginine (DanR) with polar or charged amino acid binds to FA7 (Sudlow site I), while dansyl-L-phenylalanine (DanF), dansyl-L-norvaline (DanNV) and dansylsarcosine (DanSRC) with hydrophobic amino acid are specific for FA3/4 (Sudlow site II).…”

Section: Specificity Of Dansylated Compounds As Probes Of Hsa Bindingmentioning

confidence: 62%

A fluorescent fatty acid probe, DAUDA, selectively displaces two myristates bound in human serum albumin

et al. 2011

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11-(Dansylamino) undecanoic acid (DAUDA) is a dansyl-type fluorophore and has widely used as a probe to determine the binding site for human serum albumin (HSA). Here, we reported that structure of HSA-Myristate-DAUDA ternary complex and identified clearly the presence of two DAUDA molecules at fatty acid (FA) binding site 6 and 7 of HSA, thus showing these two sites are weak FA binding sites. This result also show that DAUDA is an appropriate probe for FA site 6 and 7 on HSA as previous studied, but not a good probe of FA binding site 1 that is likely bilirubin binding site on HSA.

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Section: Specificity Of Dansylated Compounds As Probes Of Hsa Bindingmentioning

confidence: 62%

A fluorescent fatty acid probe, DAUDA, selectively displaces two myristates bound in human serum albumin

et al. 2011

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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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“…No correlation was found between mutation-induced changes in the pharmacokinetic parameters and changes in alpha-helical content or changes in heat stability. 22) Nakajou et al 23) showed that the clearance of a recombinant triple-residue mutant (K199A/ K439A/K525A) is faster than that of the wild-type rHSA, confirming the influence of positive charges of lysine at positions 199, 439, and 525 of human albumin.…”

Section: Effect Of Genetic Variation On Hsamentioning

confidence: 92%

Pharmaceutically Important Pre- and Posttranslational Modifications on Human Serum Albumin

Otagiri

Chuang

2009

Biological & Pharmaceutical Bulletin

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Recombinant technology allows engineering and production of proteins with desirable properties. Human serum albumin has been developed with recombinant technology, and thus plays an increasing role as a drug carrier in the clinical setting. Genetic variations usually occur on the surface of the protein, and do not impose significant effects on the conformation of albumin. However, binding of fatty acids by genetic variants is affected according to the location of the mutation. Albumin undergoes three major posttranslational modifications, namely, oxidation, glycation, and S-nitrosylation. This review gives an account of the different posttranslational modifications that should be taken into consideration when designing albumin mutant analogues with desirable pharmaceutical properties.

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The effect of glycation on the structure, function and biological fate of human serum albumin as revealed by recombinant mutants

Cited by 141 publications

References 36 publications

A fluorescent fatty acid probe, DAUDA, selectively displaces two myristates bound in human serum albumin

A fluorescent fatty acid probe, DAUDA, selectively displaces two myristates bound in human serum albumin

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

Pharmaceutically Important Pre- and Posttranslational Modifications on Human Serum Albumin

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