Antioxidant and pro-oxidant actions of resveratrol on human serum albumin in the presence of toxic diabetes metabolites: Glyoxal and methyl-glyoxal

Abstract

Methylglyoxal (MGO) and glyoxal (GO) are attracting considerable attention because of their role in the onset of diabetes symptoms. Therefore, to comprehend the molecular fundamentals of their pathological actions is of the utmost importance. In this study, the molecular interactions between resveratrol (RES) and human serum albumin (HSA) and the ability of the stilbene to counteract the oxidative damage caused by pathological concentrations of MGO and GO to the human plasma protein, was assessed. The oxidation of Cys34 in HSA as well as the formation of specific protein semialdehydes AAS (α-aminoadipic), GGS (γ-glutamic) and the accumulation of Advanced Glycation End-products (AGEs) was investigated. Resveratrol was found to neutralize both α-dicarbonyls by forming adducts detected by HESI-Orbitrap-MS. This antioxidant action was manifested in a significant reduction of AGEs. However, RES-α-dicarbonyl conjugates oxidized Cys34 and lysine, arginine and/or proline by a nucleophilic attack on SH and ε-NH groups in HSA. The formation of specific semialdehydes in HSA after incubation with GO and MGO at pathological concentrations was reported for the first time in this study, and may be used as early and specific biomarkers of the oxidative stress undergone by diabetic patients. The pro-oxidative role of the RES-α-dicarbonyl conjugates should be further investigated to clarify whether this action leads to positive or harmful clinical consequences. The biological relevance of human protein carbonylation as a redox signaling mechanism and/or as a reflection of oxidative damage and disease should also be studied in future works.

The impact of resveratrol on toxicity and related complications of advanced glycation end products: A systematic review

“…Of five in vitro studies that investigated the effects of RSV on AGEs or RAGE formation, four studies indicated decreased levels of AGEs or RAGE in RSV‐treated models. The only study that did not report the antiglycation effect of RSV was that of Arcanjo et al, who examined inhibitory effects of RSV on AGE formation in glyoxal (GO)/ methylglyoxal (MGO)‐incubated human serum albumin (HSA) model . Eleven studies in this review determined the antiglycation capacity of RSV in animal models.…”

Intake of Oxidized Proteins and Amino Acids and Causative Oxidative Stress and Disease: Recent Scientific Evidences and Hypotheses

“…Yet, the role of dietary oxidative stress in the onset, progress, and severity of these diseases is, in most cases, a matter of study. Dietary recommendations for some of these diseases are commonly made, which recognizes the role of food components on the prevention of the disease or alleviation of the symptoms (Arcanjo, Luna, Madruga, & Estevez, ; Parasram, ; Sirota, Gorelik, Harris, Kohen, & Kanner, ; Uttara, Singh, Zamboni, & Mahajan, ). In recent years, sound scientific evidences from studies in experimental animals have contributed to identify the precise pathological mechanisms of dietary protein oxidation products.…”

Inhibition Mechanism of Catechin, Resveratrol, Butylated Hydroxylanisole, and Tert‐Butylhydroquinone on Carboxymethyl 1,2‐Dipalmitoyl‐sn‐Glycero‐3‐Phosphatidylethanolamine Formation

“…Arcanjo et al. () found that RES could react with GO in human serum, thereby reducing the accumulation of glycated proteins in the body. Our team's previous research confirmed that one of the formation pathways for glycated DPPE in the DPPE‐glucose model system is that PE reacted with the GO oxidized in the system to form CM‐DPPE (Lin et al., ).…”

“…Arcanjo et al. () found that RES could react with GO in human serum, thereby reducing the accumulation of glycated proteins in the body.…”

“…Oh and Shahidi () found that RES could inhibit DNA breakage by removing OH·. Arcanjo, Luna, Madruga, and Estevez () found that RES could react with GO in human serum, thereby reducing the accumulation of glycated proteins in the body. Butylated hydroxylanisole (BHA) and tert‐butylhydroquinone (TBHQ) are traditional synthetic antioxidants, and they have ability to remove OH· (Pires et al., ).…”