The Effects of Storage on Platelet Proteome Assessed by Protein Expression Changes and Lysine Modification Changes Using Tmt Isobaric Labeling

Abstract

Purpose:To provide the first insight into the proteomic dynamics during platelet storage.Experiment design: In this study, based on TMT-labeled LC-MS/MS analysis, combined with antibody-affinity enrichment and purification for acetylated and succinylated peptides, we performed quantification of global proteomics, acetylome and succinylome.Simultaneously, dynamic molecular changes and functional transformation of platelet were also characterized under proper conditions stored for 1, 3, 5, 7 days, respectively.Results:3,100 proteins are quantified from a total of 3,609 proteins identified from platelets. Out of 1,308 acetylated sites identified in 648 proteins, 790 sites in 396 proteinsare quantifiable. There are 1,947 succinylated sites in 959 proteins in which 1,279 sites in 661 proteins are quantifiable.We screened the differential expression changes of global proteins, acetyl- and succinyl- proteins, and systematically interpreted their molecular functions, biological processes, cellular components, pathways and motif characters to fully investigate the molecular dynamics and biological functions of platelets. Conclusions and clinical relevance:This paper is the first systematic exploration of proteomes and modified proteomes of platelet dynamics during storage in the aim to improve our understanding of platelet biology, which may be a valuable reference for further research and clinical application.