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

• The state of aspirin-acetylation and glycation was investigated on red blood cells.
• A mass spectrometry approach allowed the accurate elucidation of protein sites.
• The levels of acetylation and glycation were quantified on haemoglobin.
• Diagnostic based on HbA1c test may be biased by the presence of aspirin.

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.

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