@conference{
author = "Penezic, Ana and Baralic, Marko and Spasojević, Ivan and Šunderić, Miloš and Miljus, Goran and Robajac, Dragana and Dobrijević, Zorana and Nedic, Olgica and Gligorijević, Nikola",
year = "2022",
abstract = "Albumin (HSA) is a multifunctional serum protein. Free Cys34 thiol group makes HSA a major source of free thiols in the circulation. HSA is also a dominant carrier of exchangeable copper pool with a high affinity binding site for this redox-active ion, located at the N-terminus. Combination of these two properties highlights HSA as a powerful circulatory antioxidant. The presence of free thiol groups in HSA and its copper binding capacity have been shown to be interconnected and essential for the binding and sequestering of copper ions, thus preventing metal-catalysed production of reactive oxygen species. End stage kidney disease (ESRD) is a condition accompanied by oxidative stress. The aim of this study was to examine changes in the antioxidative capacity of HSA and Cu(II) binding affinity in patients on peritoneal dialysis (PD), and relate it to the Cys34 thiol group content and structural changes of this molecule. HSA molecules are modified in ESRD patients on PD, having lower content of bound copper ions and thiol groups, reduced copper binding affinity and overall antioxidant capacity. An increased content of advanced glycation end-products and altered conformation was detected in HSA from PD patients. Function of HSA as a sequestrator of free Cu(II) ions, is impaired. A significant portion of the high-affinity metal-binding site was unable to interact with Cu(II) ions, as shown by EPR. Similar results on copper binding were obtained in subgroups of patients with and without diabetes mellitus, suggesting that ESRD and constant exposure to high glucose concentration during dialysis influenced protein modification. Since the concentration of Cu(II) in the circulation of these patients is much higher than in healthy persons and that Cu(II) binding capacity of albumin from patients is significantly lower, the albumin may be considered to turn from antioxidant to pro-oxidant activity.",
publisher = "Biohemijsko drustvo Srbije",
journal = ""Amazing Biochemistry" : [proceedings] / Serbian Biochemical Society, Eleventh Conference, Scientific meeting of an international character, September 22nd and 23rd, 2022, Novi Sad, Serbia",
title = "Albumin: antioxidant or pro-oxidant in patients on peritoneal dialysis?",
pages = "118",
url = "https://hdl.handle.net/21.15107/rcub_rimsi_2865"
}
