Structural and functional insights into S-thiolation of human serum albumins

• Published in: Scientific reports Vol. 8; no. 1; pp. 932 - 12
• Main Authors: Nakashima, Fumie, Shibata, Takahiro, Kamiya, Kohei, Yoshitake, Jun, Kikuchi, Ryosuke, Matsushita, Tadashi, Ishii, Isao, Giménez-Bastida, Juan A., Schneider, Claus, Uchida, Koji
• Format: Journal Article
• Language: English
• Published: London Nature Publishing Group UK 17.01.2018; Nature Publishing Group
• Subjects: 631/45/612; 631/92/458; 64/60; 82/16; 82/29; 82/58; Animals; Chemical bonds; Cysteine; Cysteine - chemistry; Cysteine - metabolism; Disulfide bonds; Disulfides - chemistry; Disulfides - metabolism; Homocysteine; Human serum albumin; Humanities and Social Sciences; Humans; Hydrophobicity; Hyperlipidemia; Ligands; Mice; Mice, Inbred C57BL; Mice, Knockout; Molecular Weight; multidisciplinary; Oxidation; Oxidation-Reduction; Residues; Science; Science (multidisciplinary); Serum Albumin, Human - chemistry; Serum Albumin, Human - metabolism; Structure-function relationships; Sulfhydryl Compounds - chemistry; Sulfhydryl Compounds - metabolism; Sulfide compounds; Thiols

Human serum albumin (HSA) is the most abundant serum protein, contributing to the maintenance of redox balance in the extracellular fluids. One single free cysteine residue at position 34 is believed to be a target of oxidation. However, the molecular details and functions of oxidized HSAs remain ob...