Zinc enhances carnosine inhibitory effect against structural and functional age-related protein alterations in an albumi
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Zinc enhances carnosine inhibitory effect against structural and functional age-related protein alterations in an albumin glycoxidation model Hichem Moulahoum Figen Zihnioglu
. Faezeh Ghorbanizamani
. Suna Timur
.
Received: 13 July 2020 / Accepted: 25 September 2020 Ó Springer Nature B.V. 2020
Abstract Age-related complications including protein alterations seen in diabetes and Alzheimer’s disease are a major issue due to their accumulation and deleterious effects. This report aims to investigate the effect of zinc supplementation on the anti-glycoxidation activity of carnosine on the in vitro model of albumin-based protein modification. Besides, the therapeutic effect of this combination was tested through the addition of the molecules in tandem (cotreatment) or post initiation (post-treatment) of the protein modification process. Glycation was induced via the addition of glucose to which carnosine (5 mM) alone or with various zinc concentrations (125, 250, and 500 lM) were added either at 0 h or 24 h postglycation induction. On the other hand, protein oxidation was induced using chloramine T (20 mM) and treated in the same way with carnosine and zinc. The different markers of glycation (advanced glycation end products (AGEs), dityrosine, and beta-sheet formation (aggregation)) and oxidation (AOPP, advanced oxidation protein products) were estimated
H. Moulahoum (&) F. Ghorbanizamani S. Timur F. Zihnioglu Biochemistry Department, Faculty of Sciences, Ege University, 35100 Bornova, Izmir, Turkey e-mail: [email protected] S. Timur Central Research Test and Analysis Laboratory Application and Research Center, Ege University, 35100 Bornova, Izmir, Turkey
via fluorescence and colorimetric assays. Zinc addition induced a significant enhancement of carnosine activity by reducing albumin modification that outperformed aminoguanidine both in the co- and posttreatment protocols. Zinc demonstrated a supplementary effect in combination with carnosine highlighting its potential in the protection against age-related protein modifications processes such as the ones found in diabetes. Keywords Zinc Carnosine Glycoxidation Protein modification Aggregation Albumin
Introduction Aging is a snowballing phenomenon resulting from the accumulation of altered and dysfunctional proteins that contribute to the predisposition to age-related diseases (Krisko and Radman 2019). Glycation is a central mechanism in aging and is associated with diabetes mellitus. Its products contribute to long-term hyperglycemia and the production and accumulation of advanced glycation end-products (AGEs). This alteration is a long process that may take weeks, however, during this process, the interaction of the aldehydes and ketones found in sugars with the proteins’ amino groups (i.e. lysine and arginine) results in the formation of intermediate products such
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Biometals
as Schiff bases and Amadori products (Fournet et al. 2018; Heidari et al. 2020). AGEs attachment to macromolecule
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