Literature DB >> 7873580

Age-related change in redox state of human serum albumin.

S Era1, K Kuwata, H Imai, K Nakamura, T Hayashi, M Sogami.   

Abstract

Human serum albumin (HSA) is the mixture of human mercaptalbumin (HMA, reduced form) and human nonmercaptalbumin (HNA, oxidized form). We developed a rapid and concise HPLC system to obtain the clear resolution of HSA into HMA and HNA, using an Asahipak GS-520H column. The mean value of the fraction of HMA (f(HMA)) for healthy young male subjects was 0.76 +/- 0.04 (n = 54). However, the f(HMA, 60-90) value for healthy elderly subjects (where the numbers in brackets indicate the range of ages) was 0.48 +/- 0.06 (n = 183). In healthy elderly subjects, f(HMA) was significantly lower than in healthy young male subjects, indicating that HSA in the elderly becomes more oxidized than in the young subjects. Consequently, we suggest that one of the important functions of serum albumin could be to participate in the maintenance of a constant redox potential in the extracellular fluids, thus securing a certain redox buffer capacity. f(HMA) on HSA might reflect this redox buffer capacity with age.

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Year:  1995        PMID: 7873580     DOI: 10.1016/0167-4838(94)00166-e

Source DB:  PubMed          Journal:  Biochim Biophys Acta        ISSN: 0006-3002


  30 in total

1.  Difference in redox status of serum and aqueous humor in senile cataract patients as monitored via the albumin thiol-redox state.

Authors:  Kenji Kawai; Tomoya Hayashi; Yukie Matsuyama; Takeshi Minami; Seiichi Era
Journal:  Jpn J Ophthalmol       Date:  2010-12-30       Impact factor: 2.447

Review 2.  Physiological and pathological changes in the redox state of human serum albumin critically influence its binding properties.

Authors:  K Oettl; R E Stauber
Journal:  Br J Pharmacol       Date:  2007-04-30       Impact factor: 8.739

3.  Effect of oxidative stress on the structure and function of human serum albumin.

Authors:  M Anraku; K Yamasaki; T Maruyama; U Kragh-Hansen; M Otagiri
Journal:  Pharm Res       Date:  2001-05       Impact factor: 4.200

4.  HPLC separation of human serum albumin isoforms based on their isoelectric points.

Authors:  Lucía Turell; Horacio Botti; Lucía Bonilla; María José Torres; Francisco Schopfer; Bruce A Freeman; Larissa Armas; Alejandro Ricciardi; Beatriz Alvarez; Rafael Radi
Journal:  J Chromatogr B Analyt Technol Biomed Life Sci       Date:  2013-11-20       Impact factor: 3.205

Review 5.  N-myristoyltransferase.

Authors:  R V Rajala; R S Datla; T N Moyana; R Kakkar; S A Carlsen; R K Sharma
Journal:  Mol Cell Biochem       Date:  2000-01       Impact factor: 3.396

Review 6.  The thiol pool in human plasma: the central contribution of albumin to redox processes.

Authors:  Lucía Turell; Rafael Radi; Beatriz Alvarez
Journal:  Free Radic Biol Med       Date:  2013-06-07       Impact factor: 7.376

7.  Validation of the chloramine-T induced oxidation of human serum albumin as a model for oxidative damage in vivo.

Authors:  Makoto Anraku; Ulrich Kragh-Hansen; Keiichi Kawai; Toru Maruyama; Yasuomi Yamasaki; Yoshinobu Takakura; Masaki Otagiri
Journal:  Pharm Res       Date:  2003-04       Impact factor: 4.200

8.  Methodology and applications of disease biomarker identification in human serum.

Authors:  Ziad J Sahab; Suzan M Semaan; Qing-Xiang Amy Sang
Journal:  Biomark Insights       Date:  2007-02-14

9.  Human astrocytes and aortic endothelial cells actively convert the oxidized form of albumin to the reduced form: reduced albumin might participate in redox regulation of nerve and blood vessel systems.

Authors:  Yukie Matsuyama; Tomoya Hayashi; Hiroyuki Terawaki; Tsuneo Negawa; Tomoyoshi Terada; Yukio Okano; Seiichi Era
Journal:  J Physiol Sci       Date:  2009-03-10       Impact factor: 2.781

10.  Albumin thiol oxidation and serum protein carbonyl formation are progressively enhanced with advancing stages of chronic kidney disease.

Authors:  Yukie Matsuyama; Hiroyuki Terawaki; Tomoyoshi Terada; Seiichi Era
Journal:  Clin Exp Nephrol       Date:  2009-04-11       Impact factor: 2.801

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