Clinical Implications Associated with the Oxidative Modification-Induced Functional Impairment of Albumin in Oxidative Stress-Related Diseases

DOI
  • Watanabe Hiroshi
    Faculty of Life Science, Kumamoto University Department of Biopharmaceutics, Graduate School of Pharmaceutical Sciences, Kumamoto University
  • Imafuku Tadashi
    Department of Biopharmaceutics, Graduate School of Pharmaceutical Sciences, Kumamoto University
  • Maruyama Toru
    Faculty of Life Science, Kumamoto University Department of Biopharmaceutics, Graduate School of Pharmaceutical Sciences, Kumamoto University

Bibliographic Information

Other Title
  • 酸化ストレス関連疾患における酸化型・還元型アルブミンモニタリングと臨床的有用性

Abstract

<p>Recent research findings indicate that the posttranslational modification of human serum albumin (HSA) such as oxidation, glycation, truncation, dimerization and carbamylation is related to certain types of diseases. We report herein on a simple and rapid analytical method, using an ESI-TOFMS technique, that allows posttranslational modifications of HSA to be quantitatively and qualitatively evaluated with a high degree of sensitivity. In patients with chronic liver disease, chronic renal disease and diabetes mellitus, an increase in the level of oxidized Cys-34 of HSA accompanied by a decrease in the level of reduced Cys-34 was observed. The redox status of Cys-34 was correlated with ligand binding and the anti-oxidative functions of HSA. Available evidence indicates that monitoring the redox state of Cys-34 could, not only be a useful marker for evaluating the progression of disease and its complications, but also would permit therapeutic efficacy to be predicted. The redox state of Cys-34 was also used as an index of the quality of HSA preparations. These data suggest that monitoring the posttranslational modifications of HSA can be important, since the function of HSA is related, not only to its serum concentration, but also to the preservation of its structural integrity under disease conditions.</p>

Journal

  • Proteome Letters

    Proteome Letters 4 (1), 9-17, 2019

    Japanese Proteomics Society

Details 詳細情報について

  • CRID
    1390001288153560704
  • NII Article ID
    130007680391
  • DOI
    10.14889/jpros.4.1_9
  • ISSN
    24322776
  • Text Lang
    ja
  • Data Source
    • JaLC
    • CiNii Articles
  • Abstract License Flag
    Disallowed

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