aspirin-mediated acetylation of haemoglobin increases in presence of high glucose concentration and decreases protein glycation外文.pdf

e u pa open proteomics 8 (2015) 116–127
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Aspirin-mediated acetylation of haemoglobin
increases in presence of high glucose
concentration and decreases protein glycation
Francesco Finamore a, Feliciano Priego-Capote b, Severine Nolli c,
Pierre Fontana c, Jean-Charles Sanchez a,∗
a Translational Biomarker Group (TBG), Department of Human Protein Sciences, University Medical Centre,
University of Geneva, 1211 Geneva 4, Switzerland
b Department of Analytical Chemistry, Annex C-3 Building, Campus of Rabanales, University of Còrdoba, Spain
c Division of Angiology and Haemostasis, University Hospitals of Geneva and Geneva Platelet Group,
Faculty of Medicine, Geneva, Switzerland
article info abstract
Article history: Glycation represents the first stage in the development of diabetic complications. Aspirin
Available online 8 May 2015 was shown to prevent sugars reacting with proteins, but the exact mechanism of this inter-
action was not well defined. We performed a quantitative analysis to calculate the levels of
Keywords: acetylation and glycation of haemoglobin, among others red blood cell (RBC) proteins, using
Protein glycation a label free approach. After glucose incubation, increases in the acetylation levels were seen
Aspirin-mediated acetylation for several haemoglobin subunits, while a parallel decrease of their glycation levels was
Red blood cells observed after aspirin incubation. These r