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Updated: Jan 31, 2026

Quantification of Site-specific Protein Lysine Acetylation and Succinylation Stoichiometry Using Data-independent Acquisition Mass Spectrometry
Published on: April 4, 2018
Shotgun proteomics data on the impact of hyperglycaemia on platelet protein acetylation by aspirin
Francesco Finamore1, Jean-Luc Reny2,3, Sarah Malacarne4
1Translational Biomarker Group, Faculty of Medicine, University of Geneva, Geneva, Switzerland.
Abstract:
This data article associated with the manuscript "A high glucose levels is associated with decreased aspirin-mediated acetylation of platelet cyclooxygenase (COX)-1 at serine 529: a pilot study" (Finamore et al., 2018) refers to the shotgun proteomics approach carried out on platelet protein extracts from diabetic patients and healthy controls. Platelet proteins were in vitro incubated with 500 µM aspirin for 30 min at 37 °C to enhance the acetylation process. After protein digestion with trypsin, DDA data were acquired on a Thermo QExactive plus using 3 technical replicate injections per sample. Here, we were able to elucidate the preferential sites of aspirin-induced acetylation on a significant fraction of the platelet proteome and to quantify the impact of diabetes on the effect of aspirin on several platelet proteins. Data are available via ProteomeXchange with identifier PXD011582.
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