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

Publication date: Available online 8 May 2015 Source:EuPA Open Proteomics Author(s): Francesco Finamore , Feliciano Priego-Capote , Severine Nolli , Pierre Fontana , Jean-Charles Sanchez 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. Graphical abstract
Source: EuPA Open Proteomics - Category: Bioinformatics Source Type: research