Glycolytic reprogramming fuels myeloid cell-driven hypercoagulability

J Thromb Haemost. 2024 Feb;22(2):394-409. doi: 10.1016/j.jtha.2023.10.006. Epub 2023 Oct 20.

Abstract

Background: Myeloid cell metabolic reprogramming is a hallmark of inflammatory disease; however, its role in inflammation-induced hypercoagulability is poorly understood.

Objectives: We aimed to evaluate the role of inflammation-associated metabolic reprogramming in regulating blood coagulation.

Methods: We used novel myeloid cell-based global hemostasis assays and murine models of immunometabolic disease.

Results: Glycolysis was essential for enhanced activated myeloid cell tissue factor expression and decryption, driving increased cell-dependent thrombin generation in response to inflammatory challenge. Similarly, inhibition of glycolysis enhanced activated macrophage fibrinolytic activity through reduced plasminogen activator inhibitor 1 activity. Macrophage polarization or activation markedly increased endothelial protein C receptor (EPCR) expression on monocytes and macrophages, leading to increased myeloid cell-dependent protein C activation. Importantly, inflammation-dependent EPCR expression on tissue-resident macrophages was also observed in vivo. Adipose tissue macrophages from obese mice fed a high-fat diet exhibited significantly enhanced EPCR expression and activated protein C generation compared with macrophages isolated from the adipose tissue of healthy mice. Similarly, the induction of colitis in mice prompted infiltration of EPCR+ innate myeloid cells within inflamed colonic tissue that were absent from the intestinal tissue of healthy mice.

Conclusion: Collectively, this study identifies immunometabolic regulation of myeloid cell hypercoagulability, opening new therapeutic possibilities for targeted mitigation of thromboinflammatory disease.

Keywords: coagulation; fibrinolysis; inflammation; macrophages; protein C.

MeSH terms

  • Animals
  • Endothelial Protein C Receptor / metabolism
  • Glycolysis
  • Inflammation / metabolism
  • Mice
  • Mice, Inbred C57BL
  • Myeloid Cells / metabolism
  • Protein C* / metabolism
  • Thrombophilia* / etiology

Substances

  • Protein C
  • Endothelial Protein C Receptor