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Decrease in Reduced‐Form Albumin Among Chronic Kidney Disease Patients: New Insights in Cardiovascular Complications
Author(s) -
Terawaki Hiroyuki,
Era Seiichi,
Nakayama Masaaki,
Hosoya Tatsuo
Publication year - 2011
Publication title -
therapeutic apheresis and dialysis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.415
H-Index - 53
eISSN - 1744-9987
pISSN - 1744-9979
DOI - 10.1111/j.1744-9987.2010.00889.x
Subject(s) - medicine , human serum albumin , cysteine , kidney disease , albumin , redox , high performance liquid chromatography , serum albumin , human kidney , disease , disulfide bond , human albumin , kidney , biochemistry , chromatography , chemistry , organic chemistry , enzyme
From the perspective of free cysteine residue (Cys‐34), human serum albumin (HSA) comprises a mixture of human mercaptoalbumin (HMA), in which the Cys‐34 is not oxidized, human non‐mercaptoalbumin (HNA)‐1, which has a disulfide bond that can be reversibly oxidized, mainly by cysteine, and HNA‐2, which is strongly oxidized to form sulfinic (‐SO 2 H) or sulfonic (‐SO 3 H) species. We have developed a convenient high‐performance liquid chromatographic (HPLC) system for the clear separation of HSA into HMA, HNA‐1 and HNA‐2, and we have studied the dynamic changes of HSA‐redox under various states of chronic kidney disease, in both a clinical and an experimental setting. In this article, we discuss the relationship between HSA‐redox (especially the decrease of the reduced form), dialyzable uremic toxins and incident cardiovascular disease based on our recent investigations.