Age-related change in redox state of human serum albumin

Era, Seiichi; Kuwata, Kazuo; Imai, Hisao; Nakamura, Koji; Hayashi, Tomoya; Sogami, Masaru

doi:10.1016/0167-4838(94)00166-e

Cited by 161 publications

(120 citation statements)

References 32 publications

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“…Although there is a good agreement between our simulation and the experimental spectra, it is worth mentioning that in HSA, as well in other proteins containing multiple cysteines, the ratio between thiols and disulfides may be different depending upon the redox conditions. Recent statistical studies on HSA samples taken from blood samples of different persons have shown that there is a correlation between the above mentioned ratio and the age of the individuals (Era et al, 1995).…”

Section: Figurementioning

confidence: 99%

Counting the number of disulfides and thiol groups in proteins and a novel approach for determining the local pK_afor cysteine groups in proteinsin vivo

Bellacchio

McFarlane

Rompel

et al. 2001

J Synchrotron Radiat

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X-ray Absorption Spectroscopy (XAS) is a powerful tool to investigate sulfur in biological molecules. The spectral features are sensitive to the local electronic and geometric environment of the atom; thus, they constitute a fingerprint of the different chemical forms in which the sulfur is present. This allows straightforward detection of the ratio between free thiols and disulfides. Intra-or inter-molecular disulfide bond formation between residues plays an important role in structural and conformational changes in proteins, and such changes can be investigated using sulfur XAS. Also, a thiolate-disulfide equilibrium is involved in the regulation of the redox potential in the cells by means of modulating the concentrations of the reduced (thiolate) and oxidized (disulfide) form of the tripeptide glutathione. Thus, we can monitor the redox state of a cell by means of sulfur XAS. Thiols also exhibit an acidbase equilibrium, and sulfur XAS can be used to determine the local pK a of the -SH group. Here we report examples of how sulfur XAS has been used for these applications.

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Section: Figurementioning

confidence: 99%

Counting the number of disulfides and thiol groups in proteins and a novel approach for determining the local pK_afor cysteine groups in proteinsin vivo

Bellacchio

McFarlane

Rompel

et al. 2001

J Synchrotron Radiat

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“…In addition, oxidized albumin possesses lower antioxidant levels and lower binding properties 1, 2, 3. Blood purification techniques, such as hemodialysis and albumin dialysis, increased the rate of HMA and decreased the rate of HNA 9, 10, 11.…”

Section: Discussionmentioning

confidence: 99%

“…High performance liquid chromatography (HPLC) was used for analysis of HMA, HNA‐1, and HNA‐2 1, 6. The HPLC system used in the present study consisted of a Model LC‐20A system and a Model RF‐10AXL fluorescence detector (excitation wavelength, 280 nm; emission wavelength, 340 nm), all from Simadzu Corporation (Kyoto, Japan).…”

Section: Methodsmentioning

confidence: 99%

“…In healthy adults, approximately 75% of serum albumin exists in reduced form (HMA) and 25% in oxidized form (HNA). The relative proportion of HNA reportedly increases in various clinical conditions 1, 2, 3. The use of high‐quality HAS preparations is important for applications involving the use of large volumes of this protein such as plasma exchange and treatment of hypovolemic shock.…”

Section: Introductionmentioning

confidence: 97%

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Comparison of quality of human serum albumin preparations in two pharmaceutical products

Nakae

Tomida

Kikuya

et al. 2017

Acute Medicine & Surgery

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AimHuman serum albumin (HSA) is known for its multiple functions, such as maintenance of colloid osmotic pressure, transport of endogenous and exogenous substances, and antioxidation. The aim of this study was to measure the redox state and concentrations of β‐d‐glucan and endotoxin to compare the quality of 5% HSA preparations from two different manufacturers.MethodsThe quality of 5% HSA preparations in two different pharmaceutical products (groups A and B) was compared in terms of the percentage of reduced and oxidized albumin and the contaminant level of β‐d‐glucan and endotoxin.ResultsThe percentage of human mercaptoalbumin in group A was significantly higher than that in group B (P < 0.01), whereas that of human non‐mercaptoalbumin‐2 in group A was significantly lower (P < 0.01). The concentration of β‐d‐glucan in group A was significantly lower than in group B (P < 0.01).ConclusionsThe present findings indicate the need for quality control of HSA preparations in applications involving the use of large volumes.

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“…Oxidation of HSA is also age related where in the elderly it becomes more oxidized than in young subjects. 35) Mild oxidation of HSA has no detectable effect on the binding of drugs to site I in subdomain IIA. In contrast, the ligand-binding property of site II and the esterase-like activity of oxidized HSA are decreased, most probably due to conformational changes in subdomain IIIA.…”

Section: Posttranslational Modification Of Albuminmentioning

confidence: 99%

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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Age-related change in redox state of human serum albumin

Cited by 161 publications

References 32 publications

Counting the number of disulfides and thiol groups in proteins and a novel approach for determining the local pK_afor cysteine groups in proteinsin vivo

Counting the number of disulfides and thiol groups in proteins and a novel approach for determining the local pK_afor cysteine groups in proteinsin vivo

Comparison of quality of human serum albumin preparations in two pharmaceutical products

Pharmaceutically Important Pre- and Posttranslational Modifications on Human Serum Albumin

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Age-related change in redox state of human serum albumin

Cited by 161 publications

References 32 publications

Counting the number of disulfides and thiol groups in proteins and a novel approach for determining the local pKafor cysteine groups in proteinsin vivo

Counting the number of disulfides and thiol groups in proteins and a novel approach for determining the local pKafor cysteine groups in proteinsin vivo

Comparison of quality of human serum albumin preparations in two pharmaceutical products

Pharmaceutically Important Pre- and Posttranslational Modifications on Human Serum Albumin

Contact Info

Product

Resources

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Counting the number of disulfides and thiol groups in proteins and a novel approach for determining the local pK_afor cysteine groups in proteinsin vivo

Counting the number of disulfides and thiol groups in proteins and a novel approach for determining the local pK_afor cysteine groups in proteinsin vivo