Aspirin-mediated acetylation of haemoglobin increases in presence of high glucose concentration and decreases protein glycation

Abstract

Aspirin-mediated acetylationRed blood cells Haemoglobin Mass spectrometry Label-free a b s t r a c t Glycation represents the first stage in the development of diabetic complications. Aspirin was shown to prevent sugars reacting with proteins, but the exact mechanism of this interaction was not well defined. We performed a quantitative analysis to calculate the levels of acetylation and glycation of haemoglobin, among others red blood cell (RBC) proteins, using a label free approach. After glucose incubation, increases in the acetylation levels were seen for several haemoglobin subunits, while a parallel decrease of their glycation levels was observed after aspirin incubation. These results suggest that, a mutual influence between these two modifications, occur at protein level.

Beyond COX-1: the effects of aspirin on platelet biology and potential mechanisms of chemoprevention

“…Perhaps the most important component of the blood-plasma milieu, hemoglobin, undergoes aspirin-dependent acetylation in vitro , and it is presumed to undergo similar modifications at high aspirin doses in vivo [ 101 ]. Studies of hemoglobin acetylation by aspirin demonstrated decreases in protein glycation, and in the presence of high glucose concentrations hemoglobin acetylation by aspirin is increased [ 102 ], an effect that has also been observed in serum albumin. Aspirin is able to acetylate a variety of lysine residues in the α and β chains of hemoglobin, without having an effect on its structural conformation or oxygen binding and transport functions [ 40 ].…”

Maillard Proteomics: Opening New Pages

“…In the most easy and straightforward way it can be increased by application of longer columns and gradients times, providing high peak capacity [ 220 ]. However, the coverage of modified proteome can be further increased by implementation of additional separation procedures, introduced in the general proteomics workflow as enrichment, depletion, or pre-fractionation steps [ 137 , 221 , 222 , 223 ]. Such multi-dimensional workflows allow reduction of matrix effects and, hence, provide better sensitivity [ 108 ].…”

“…Although this procedure can be applied both to protein mixtures and products of their enzymatic hydrolysis, enrichment on the level of digests was shown to be advantageous [ 52 , 219 ]. During the recent decade, the power of this method was confirmed with in vitro glycated proteins [ 219 , 222 , 228 ], human plasma [ 115 , 137 , 174 , 189 ] and even plant tissues [ 32 ]. To achieve higher recoveries of glycated peptides, two-step elution with warm (37 °C) aq.…”

Prevention of haemoglobin glycation by acetylsalicylic acid (ASA): A new view on old mechanism

“…ASA has been shown to acts as an anti-glycating agent [16,21], nevertheless, the exact molecular mechanism whereby ASA exerts its chemopreventive effects is not clearly understood. The acetylation of proteins has been suggested as a major factor involved in some of the unexplained effects of aspirin as well as inhibiting the protein glycation [21,31]. All three chemicals investigated in the present work, regarding their harnessing effect on Hb glycation, possess the fundamental structure as BA.…”

“…In diabetics, serum fructose concentration is increased 1.5 fold, meanwhile, such increase in RBCs showed to be 4-fold [9], which consequently introduce fructose as one of the main players of the Hb glycation or fructation. A considerable amount of literature has been published on the inhibitory effect of ASA on protein glycation [16,21,31]. Moreover, there are also some documents dealing with the side effects of ASA consumption [23,24].…”