Current insights into the role of citrullination in thrombosis

R Madison Green; Paul R Thompson

doi:10.1016/j.cbpa.2023.102313

Current insights into the role of citrullination in thrombosis

Curr Opin Chem Biol. 2023 Aug:75:102313. doi: 10.1016/j.cbpa.2023.102313. Epub 2023 May 4.

Authors

R Madison Green¹, Paul R Thompson²

Affiliations

¹ Program in Chemical Biology, University of Massachusetts Chan Medical School, 364 Plantation Street, Worcester, MA 01605, USA; Department of Biochemistry and Molecular Biotechnology, University of Massachusetts Chan Medical School, 364 Plantation Street, Worcester, MA 01605, USA.
² Program in Chemical Biology, University of Massachusetts Chan Medical School, 364 Plantation Street, Worcester, MA 01605, USA; Department of Biochemistry and Molecular Biotechnology, University of Massachusetts Chan Medical School, 364 Plantation Street, Worcester, MA 01605, USA. Electronic address: paul.thompson@umassmed.edu.

PMID: 37148643
PMCID: PMC10523988 (available on 2024-08-01)
DOI: 10.1016/j.cbpa.2023.102313

Abstract

Protein citrullination is a post-translational modification of arginine that controls a diverse array of cellular processes, including gene regulation, protein stability, and neutrophil extracellular trap (NET) formation. Histone citrullination promotes chromatin decondensation and NET formation, a pro-inflammatory form of cell death that is aberrantly increased in numerous immune disorders. This review will provide insights into NETosis and how this novel form of cell death contributes to inflammatory diseases, with a particular emphasis on its role in thrombosis. We will also discuss recent efforts to develop PAD-specific inhibitors.

Publication types

Review

MeSH terms

Chromatin / metabolism
Citrullination
Extracellular Traps* / metabolism
Humans
Protein Processing, Post-Translational
Thrombosis* / metabolism

Substances

Chromatin

Grants and funding

R35 GM118112/GM/NIGMS NIH HHS/United States