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Kinetics of Glycoxidation of Bovine Serum Albumin by Methylglyoxal and Glyoxal and Its Prevention by Various Compounds

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Kinetics of Glycoxidation of Bovine Serum Albumin by Methylglyoxal and Glyoxal and Its Prevention by Various Compounds Molecules 2014, 19, 4880-4896; doi:10.3390/molecules19044880 OPEN ACCESS molecules ISSN 1420-3049 www.mdpi.com/journal/molecules Article Kinetics of Glycoxidation of Bovine Serum Albumin by Methylglyoxal and Glyoxal and its Prevention by Various Compounds Izabela Sadowska-Bartosz 1,*, Sabina Galiniak 1 and Grzegorz Bartosz 1,2 1 Department of Biochemistry and Cell Biology, University of Rzeszów, Zelwerowicza St. 4, PL 35-601 Rzeszów, Poland 2 Department of Molecular Biophysics, University of Łódź, Pomorska 141/143, 90-236 Łódź, Poland * Author to whom correspondence should be addressed; E-Mail: [email protected]; Tel.: +48-17-875-5408; Fax: +48-17-872-1425. Received: 19 February 2014; in revised form: 9 March 2014 / Accepted: 10 March 2014 / Published: 17 April 2014 Abstract: The aim of this study was to compare several methods for measurement of bovine serum albumin (BSA) modification by glycoxidation with reactive dicarbonyl compounds (methylglyoxal ‒ MGO and glyoxal ‒ GO), for studies of the kinetics of this process and to compare the effects of 19 selected compounds on BSA glycation by the aldehydes. The results confirm the higher reactivity of MGO with respect to GO and point to the usefulness of AGE, dityrosine and N′-formylkynurenine fluorescence for monitoring glycation and evaluation of protection against glycation. Different extent of protection against glycation induced by MGO and GO was found for many compounds, probably reflecting effects on various stages of the glycation process. Polyphenols (genistein, naringin and ellagic acid) were found to protect against aldehyde-induced glycation; 1-cyano-4-hydroxycinnamic acid was also an effective protector. Keywords: glycation; kinetics; methylglyoxal; glyoxal; antioxidants 1. Introduction One of undesired and unavoidable consequences of metabolism are non-enzymatic reactions of aldehyde/ketone groups of reducing sugars with other cellular components, mainly proteins (glycation or Maillard reaction). Glycation can also occur with highly reactive sugar derivatives such as Molecules 2014, 19 4881 α-oxoaldehydes, glyoxal (GO), methylglyoxal (MGO) and 3-deoxyglucosone. α-Oxoaldehydes, which are important precursors of advanced glycation end products (AGEs), can be formed endogenously by degradation of glucose and early glycation products. GO is formed by lipid peroxidation and the degradation of monosaccharides, saccharide derivatives and glycated proteins. MGO can be generated under physiological conditions by non-enzymatic elimination of phosphate from dihydroacetone phosphate or glyceraldehyde-3-phosphate [1]. Additionally, MGO can also be formed as a side-product of different metabolic pathways (e.g., by enzymatic elimination of phosphate from glycerone phosphate, glyceraldehyde 3-phosphate or from 3-aminoacetone in the threonine catabolism, during lipid peroxidation and from the degradation of DNA) [2]. MGO is produced in a high amount in diabetes mellitus enzymatically e.g. by MGO synthase and cytochrome P450 IIE1 and also by non-enzymatic reactions because of the increase in non-enzymatic glycation [3]. In an advanced stage of diabetic complications in the case of ischemic tissue damage, hypoxia itself enhances local production of MGO in the ischemic zone [4]. Blood plasma MGO concentration was estimated to be in the order of 1–10 μM range [3]. Recent estimates of the concentrations of MGO and GO in human blood plasma are in the range 70–120 nM, while cellular concentrations of MGO are 1–5 μM and those of GO are 0.1–1 μM [5]. Increased MGO levels were found in whole blood samples of non-insulin-dependent diabetic patients (mean: 286.8, range: 54.7–2370 pmol/g blood) when compared to control subjects (mean: 79.8, range: 25.3–892.9 pmol/g blood) [4]. MGO in the free form is very unstable, has short biological survival times, and sophisticated techniques are required for its quantitative evaluation [6]. It has been reported that MGO binds to and modifies a number of proteins [7], and damages DNA, thus causing cellular toxicity [8]. Modification of human serum albumin (HSA) by MGO produced hotspot modification of Arg-410 with hydroimidazolone, Nδ-(5-hydro-5-methyl-4-imidazolon-2-yl)-ornithine (MG-H1) residue formation. Modification of Arg-410 by MGO was found in albumin glycated in vivo. MG-H1 residue formation in albumin and other plasma proteins is increased in clinical diabetes and end stage renal disease [5]. Molecular dynamics and modeling studies indicate that hydroimidazolone formation causes structural distortion leading to disruption of arginine-directed hydrogen bonding and loss of electrostatic interaction. Hydroimidazolone formation at Arg-410 inhibits drug binding and esterase activity [9]. A specific GO-derived AGE is a lysine-lysine crosslinking structure named GO-lysine dimer or GOLD. Investigators have reported an age-related increase of GOLD in human lens proteins as well as in diabetes [1]. The posttranslational modification of proteins by MGO is believed to contribute to aging, as well as to development of a number of diseases, including cancer, diabetes and other disorders. MGO-induced AGEs on mitochondrial proteins leads to a decline of mitochondrial function and have been hypothesized to act as a contributing factor in the phenomenon of so-called ―metabolic memory‖ [10]. Glycation is usually catalyzed by metals and associated with generation of reactive oxygen species (ROS) and oxidation so it is often referred to as glycoxidation although reducing derivatives are also formed in the course of this process [11]. Proteins, because of their high abundance, are the main substrate for glycoxidation. Glycoxidation is initiated by formation of early glycation products such as Schiff bases and Amadori products. Further modifications of the early stage glycation products, such as rearrangement, oxidation, polymerization and cleavage give rise to irreversible conjugates (AGEs). Although AGE formation takes place under physiological conditions, it is accelerated in hyperglycemia. Accumulation of glycation products is observed in human and animal tissues during Molecules 2014, 19 4882 aging and is associated with various diseases including, first of all, diabetes and diabetic nephropathy, microangiopathy and atherosclerosis [12–14]. The serum levels of AGEs have been found to be elevated also in other diseases, including, i.a. multiple sclerosis [15] and amyotrophic lateral sclerosis [16], and correlated with the severity of cognitive impairment in patients with cerebrovascular disease [13]. Studies of proteins containing either early stage glycation products or AGEs have become of great interest due to the suspected effects of glycation on protein function and tissue damage in diabetes. This effect has been well-studied for proteins with long life spans, such as collagen and lens crystallin, as well for some proteins with shorter life spans, such as hemoglobin. However, there has also been an increasing interest in the glycation of HSA and closely-related proteins (e.g., bovine serum albumin, BSA) [17]. Albumin represents the most abundant protein, constituting some 50% of the protein present in the plasma of normal healthy individuals and has a wide variety of physiological and pharmacological functions including the maintenance of oncotic pressure, binding and transport of diverse small size metabolites such as metal ions, fatty acids, bilirubin, drugs and nitric oxide, and contribution to the antioxidant capacity of blood plasma [2]. In vivo, the proportion of glycated albumin in healthy persons is between 1% and 10%; this proportion may increase two- to threefold in diabetes mellitus [18]. Therefore, this protein is not only a convenient but also very relevant model for studies of the reactions of glycoxidation. In view of the growing role of AGEs in diabetes and age associated pathologies, it has been suggested that inhibition of the formation of AGEs may prevent the progression of diabetic complications and slow down the ageing process. Pharmacological agents, such as aminoguanidine, tenilsetam, carnosine, metformin and pyridoxamine, have been investigated for inhibiting the formation of AGEs and/or the development of diabetic complications. Nevertheless, all of these compounds have side effects. It is thus critical to develop effective and safe agents to protect diabetics from complications [8]. Therefore, on-going screening and development of novel compounds that offer combined antioxidant and antiglycation properties will benefit to the treatment of diabetes mellitus [19]. The aim of the present study was twofold. Firstly, we wanted to compare several methods for measurement of BSA (as a model protein) modification by reactive dicarbonyl compounds (GO and MGO) for monitoring the kinetics of this process. Secondly, we compared the effects of 19 selected compounds on BSA glycoxidation induced by reactive dicarbonyls in search of compounds which can efficiently prevent this process. The compounds chosen included natural polyphenols (ellagic acid, genistein, naringin), natural (ascorbic acid, lipoic acid, cysteamine, Na-pyruvate, para-aminobenzoic acid) and synthetic (captopril, tiron, TEMPO, 4-hydroxy-TEMPO, 2,2,6,6-tetramethyl-4-(nonanoyl- amino)piperidin-1-yl]oxyl) antioxidants, an inhibitors of glycolysis (3-bromopyruvic acid), an antidiabetic drug (metformin), and a cyclic polyol (quinic acid). We included also 1-cyano-4-hydroxy- cinnamic acid, a compound we found to inhibit glycation by reducing sugars (submitted) and its parent compound,
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