The Thiol Group Reactivity and the Antioxidant Property of Human Serum Albumin Are Controlled by the Joint Action of Fatty Acids and Glucose Binding
Autori
Uzelac, Tamara N.Smiljanić, Katarina
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Takić, Marija
Sarac, Ivana
Petovic-Oggiano, Gordana
Nikolić, Milan
![](/themes/MirageCherry/images/orcid.png)
Jovanović, Vesna B.
![](/themes/MirageCherry/images/orcid.png)
Članak u časopisu (Objavljena verzija)
Metapodaci
Prikaz svih podataka o dokumentuApstrakt
The binding of ubiquitous serum ligands (free fatty acids) to human serum albumin (HSA)
or its glycation can affect thiol group reactivity, thus influencing its antioxidant activity. The effects
of stearic acid (SA) and glucose binding on HSA structural changes and thiol group content and
reactivity were monitored by fluoroscopy and the Ellman method during a 14-day incubation in
molar ratios to HSA that mimic pathophysiological conditions. Upon incubation with 5 mM glucose,
HSA glycation was the same as HSA without it, in three different HSA:SA molar ratios (HSA:SA-
1:1-2-4). The protective effect of SA on the antioxidant property of HSA under different glucose
regimes (5-10-20 mM) was significantly affected by molar ratios of HSA:SA. Thiol reactivity was fully
restored with 5–20 mM glucose at a 1:1 HSA:SA ratio, while the highest thiol content recovery was in
pathological glucose regimes at a 1:1 HSA:SA ratio. The SA affinity for HSA increased significantly
(1.5- and 1.3-fo...ld, p < 0.01) with 5 and 10 mM glucose compared to the control. These results deepen
the knowledge about the possible regulation of the antioxidant role of HSA in diabetes and other
pathophysiological conditions and enable the design of future HSA-drug studies which, in turn, is
important for clinicians when designing information-based treatments.
Ključne reči:
antioxidant role / fatty acids / glucose / glycation / human serum albumin / thiol group content and reactivityIzvor:
International Journal of Molecular Sciences, 2024, 5, 2335-Izdavač:
- MDPI
Finansiranje / projekti:
- Ministarstvo nauke, tehnološkog razvoja i inovacija Republike Srbije, institucionalno finansiranje - 200168 (Univerzitet u Beogradu, Hemijski fakultet) (RS-MESTD-inst-2020-200168)
- Ministarstvo nauke, tehnološkog razvoja i inovacija Republike Srbije, institucionalno finansiranje - 200015 (Univerzitet u Beogradu, Institut za medicinska istraživanja) (RS-MESTD-inst-2020-200015)
Napomena:
- Article processing charge of 2610 CHF was covered by the joint effort of authors by combining their reviewers vouchers to cover the total APC.
Kolekcije
Institucija/grupa
Hemijski fakultet / Faculty of ChemistryTY - JOUR AU - Uzelac, Tamara N. AU - Smiljanić, Katarina AU - Takić, Marija AU - Sarac, Ivana AU - Petovic-Oggiano, Gordana AU - Nikolić, Milan AU - Jovanović, Vesna B. PY - 2024 UR - http://cherry.chem.bg.ac.rs/handle/123456789/6429 AB - The binding of ubiquitous serum ligands (free fatty acids) to human serum albumin (HSA) or its glycation can affect thiol group reactivity, thus influencing its antioxidant activity. The effects of stearic acid (SA) and glucose binding on HSA structural changes and thiol group content and reactivity were monitored by fluoroscopy and the Ellman method during a 14-day incubation in molar ratios to HSA that mimic pathophysiological conditions. Upon incubation with 5 mM glucose, HSA glycation was the same as HSA without it, in three different HSA:SA molar ratios (HSA:SA- 1:1-2-4). The protective effect of SA on the antioxidant property of HSA under different glucose regimes (5-10-20 mM) was significantly affected by molar ratios of HSA:SA. Thiol reactivity was fully restored with 5–20 mM glucose at a 1:1 HSA:SA ratio, while the highest thiol content recovery was in pathological glucose regimes at a 1:1 HSA:SA ratio. The SA affinity for HSA increased significantly (1.5- and 1.3-fold, p < 0.01) with 5 and 10 mM glucose compared to the control. These results deepen the knowledge about the possible regulation of the antioxidant role of HSA in diabetes and other pathophysiological conditions and enable the design of future HSA-drug studies which, in turn, is important for clinicians when designing information-based treatments. PB - MDPI T2 - International Journal of Molecular Sciences T1 - The Thiol Group Reactivity and the Antioxidant Property of Human Serum Albumin Are Controlled by the Joint Action of Fatty Acids and Glucose Binding VL - 5 SP - 2335 DO - 10.3390/ijms25042335 ER -
@article{ author = "Uzelac, Tamara N. and Smiljanić, Katarina and Takić, Marija and Sarac, Ivana and Petovic-Oggiano, Gordana and Nikolić, Milan and Jovanović, Vesna B.", year = "2024", abstract = "The binding of ubiquitous serum ligands (free fatty acids) to human serum albumin (HSA) or its glycation can affect thiol group reactivity, thus influencing its antioxidant activity. The effects of stearic acid (SA) and glucose binding on HSA structural changes and thiol group content and reactivity were monitored by fluoroscopy and the Ellman method during a 14-day incubation in molar ratios to HSA that mimic pathophysiological conditions. Upon incubation with 5 mM glucose, HSA glycation was the same as HSA without it, in three different HSA:SA molar ratios (HSA:SA- 1:1-2-4). The protective effect of SA on the antioxidant property of HSA under different glucose regimes (5-10-20 mM) was significantly affected by molar ratios of HSA:SA. Thiol reactivity was fully restored with 5–20 mM glucose at a 1:1 HSA:SA ratio, while the highest thiol content recovery was in pathological glucose regimes at a 1:1 HSA:SA ratio. The SA affinity for HSA increased significantly (1.5- and 1.3-fold, p < 0.01) with 5 and 10 mM glucose compared to the control. These results deepen the knowledge about the possible regulation of the antioxidant role of HSA in diabetes and other pathophysiological conditions and enable the design of future HSA-drug studies which, in turn, is important for clinicians when designing information-based treatments.", publisher = "MDPI", journal = "International Journal of Molecular Sciences", title = "The Thiol Group Reactivity and the Antioxidant Property of Human Serum Albumin Are Controlled by the Joint Action of Fatty Acids and Glucose Binding", volume = "5", pages = "2335", doi = "10.3390/ijms25042335" }
Uzelac, T. N., Smiljanić, K., Takić, M., Sarac, I., Petovic-Oggiano, G., Nikolić, M.,& Jovanović, V. B.. (2024). The Thiol Group Reactivity and the Antioxidant Property of Human Serum Albumin Are Controlled by the Joint Action of Fatty Acids and Glucose Binding. in International Journal of Molecular Sciences MDPI., 5, 2335. https://doi.org/10.3390/ijms25042335
Uzelac TN, Smiljanić K, Takić M, Sarac I, Petovic-Oggiano G, Nikolić M, Jovanović VB. The Thiol Group Reactivity and the Antioxidant Property of Human Serum Albumin Are Controlled by the Joint Action of Fatty Acids and Glucose Binding. in International Journal of Molecular Sciences. 2024;5:2335. doi:10.3390/ijms25042335 .
Uzelac, Tamara N., Smiljanić, Katarina, Takić, Marija, Sarac, Ivana, Petovic-Oggiano, Gordana, Nikolić, Milan, Jovanović, Vesna B., "The Thiol Group Reactivity and the Antioxidant Property of Human Serum Albumin Are Controlled by the Joint Action of Fatty Acids and Glucose Binding" in International Journal of Molecular Sciences, 5 (2024):2335, https://doi.org/10.3390/ijms25042335 . .