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February 25, 20260 citations

Dynamic lysine acetylation and succinylation of platelet proteins regulates platelet storage lesion: mechanistic insights from multi-omics.

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XLXin LiaoCZChenlu ZhangMCMin Chen

Key Result

Dynamic lysine acetylation and succinylation of platelet proteins regulate platelet storage lesion, offering a framework to optimize storage and improve transfusion safety.

Key Points

  • The research aims to understand the impact of lysine acetylation and succinylation on platelet proteins and their role in platelet storage lesions.
  • Mapped proteomic changes and post-translational modifications (PTMs) in platelet proteins
  • Utilized multi-omics approaches to analyze protein dynamics during storage
  • Established experimental protocols to assess storage lesions
  • Identified specific lysine acetylation and succinylation patterns related to storage lesions
  • Demonstrated that modifying storage protocols can enhance platelet transfusion safety
  • Provided insights into the mechanisms underlying the regulation of platelet functionality during storage

Structured PICO

P
Population
Platelets (platelet storage lesion model)
O
Outcome
Proteomic abundance shifts and post-translational modification (PTM) dynamics (lysine acetylation and succinylation)

Mapping proteomic and PTM dynamics provides a foundational framework for optimizing platelet storage protocols and enhancing transfusion safety.

Abstract

By mapping the interplay between proteomic abundance shifts and PTM dynamics, this study provides a multidimensional understanding of PSL, establishing a foundational framework for optimizing storage protocols and enhancing transfusion safety.

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Cite This Study

Liao et al. (2026) studied this question. Dynamic lysine acetylation and succinylation of platelet proteins regulate platelet storage lesion, offering a framework to optimize storage and improve transfusion safety.

synapsesocial.com/papers/699e91d7f5123be5ed04fa76https://doi.org/10.1080/07853890.2026.2635200
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