Thiol disulfide exchange reactions in human serum albumin: the apparent paradox of the redox transitions of Cys34

The FEBS Journal
Alessio BocediGiorgio Ricci

Abstract

Human serum albumin (HSA) is characterized by 17 disulfides and by only one unpaired cysteine (Cys34 ), which can be free in the reduced albumin or linked as a mixed disulfide with cysteine, or in minor amount with other natural thiols, in the oxidized albumin. In healthy subjects, the level of the oxidized form is about 35%, but it rises up to 70% after oxidative insults or in patients with kidney diseases. Oxidized albumin is therefore considered a short-term biomarker of oxidative stress as its level may increase or decrease under appropriate redox inputs in discrete temporal spans. This paper defines, for the first time, the kinetic properties of reduced and oxidized Cys34 of HSA in their reactions with natural disulfides and thiols. Kinetic constants support the evidence that the Cys34 redox oscillations observed in vivo are mainly due to the interaction with cysteine and cystine without the involvement of any enzymatic support. This study gives also a plausible explanation for the absence of involvement of the 17 disulfides naturally present in HSA in these redox transitions. This inert behavior toward cysteine is marginally due to solvent accessibility or flexibility factors of these bonds but mainly to their strong ther...Continue Reading

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Aug 15, 2019·Antioxidants & Redox Signaling·Ling FuJing Yang
Dec 19, 2019·Chemistry : a European Journal·Victor M TormyshevElena G Bagryanskaya
Aug 23, 2020·Diagnostics·Małgorzata Krzystek-KorpackaKatarzyna Neubauer
Jan 31, 2021·Free Radical Biology & Medicine·Lucía TurellBeatriz Alvarez
Apr 4, 2021·Antioxidants·Stefanny M FigueroaCristián A Amador
Apr 4, 2021·Antioxidants·Fuka TabataKazuhiro Miyaji
Apr 26, 2021·Biophysical Chemistry·Prajna MishraSantosh Kumar Jha
Oct 5, 2021·Journal of the American Chemical Society·Tuuli A HakalaGonçalo J L Bernardes

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