Abstract
Meloxicam is a non-steroidal anti-inflammatory drug, which has a preferential inhibitory effect to cyclooxyganase-2 (COX-2). Although the drug inhibits prostaglandin synthesis, the exact mechanism of meloxicam is still unknown. This is the first study to assess the effect of meloxicam on protein glyco-oxidation as well as antioxidant activity. For this purpose, we used an in vitro model of oxidized bovine serum albumin (BSA). Glucose, fructose, ribose, glyoxal and methylglyoxal were used as glycating agents, while chloramine T was used as an oxidant. We evaluated the antioxidant properties of albumin (2,2-di-phenyl-1-picrylhydrazyl radical scavenging capacity, total antioxidant capacity and ferric reducing antioxidant power), the intensity of protein glycation (Amadori products, advanced glycation end products) and glyco-oxidation (dityrosine, kynurenine, N-formylkynurenine, tryptophan and amyloid-β) as well as the content of protein oxidation products (advanced oxidation protein products, carbonyl groups and thiol groups). We have demonstrated that meloxicam enhances the antioxidant properties of albumin and prevents the protein oxidation and glycation under the influence of various factors such as sugars, aldehydes and oxidants. Importantly, the antioxidant and anti-glycating activity is similar to that of routinely used antioxidants such as captopril, Trolox, reduced glutathione and lipoic acid as well as protein glycation inhibitors (aminoguanidine). Pleiotropic action of meloxicam may increase the effectiveness of anti-inflammatory treatment in diseases with oxidative stress etiology.
Highlights
An integral part of cellular oxygen metabolism is the production of reactive oxygen species (ROS) [1]
We evaluated the antioxidant properties of albumin (DPPH, Total Antioxidant Capacity (TAC), Ferric Reducing Antioxidant Power (FRAP)), the intensity of protein glycation (Amadori products, advanced glycation end products (AGEs)) and glyco-oxidation as well as the content of protein oxidation products (AOPP, Protein Carbonyls (PC) and thiol groups)
The presence of glucose resulted in increased contents of protein glyco-oxidation products—
Summary
An integral part of cellular oxygen metabolism is the production of reactive oxygen species (ROS) [1]. Oxygen free radicals are involved in many physiological processes; under long-term exposure to pro-oxidant agents, the formation of ROS becomes greater than the ability of cells to eliminate them [1]. Disturbances in oxidative-reductive homeostasis (in favor of the oxidation reactions) result in oxidative stress. This process leads to oxidative damage to biomolecules such as proteins, lipids and DNA and is believed to be the cause or effect of several contemporary diseases [2,3,4]. The low probability of direct ROS reactions with lipids and DNA indicates that proteins are the most important target for free radicals. In a typical mammalian cell, over 70% of hydroxyl radicals (OH) react with proteins [5]
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