USP25-PKM2-glycolysis axis contributes to ischemia reperfusion-induced acute kidney injury by promoting M1-like macrophage polarization and proinflammatory response

Clin Immunol. 2023 Jun:251:109279. doi: 10.1016/j.clim.2023.109279. Epub 2023 Mar 8.

Abstract

M1-like macrophages have been reported to play critical roles in acute kidney injury (AKI). Here, we elucidated the role of ubiquitin-specific protease 25 (USP25) in M1-like macrophages polarization and AKI. High USP25 expression was correlated with a decline in renal function in patients with acute kidney tubular injury and in mice with AKI. In contrast, USP25 knockout reduced M1-like macrophage infiltration, suppressed M1-like polarization, and improved AKI in mice, indicating that USP25 was necessary for M1-like polarization and proinflammatory response. Immunoprecipitation assay and liquid chromatography-tandem mass spectrometry showed that the M2 isoform of pyruvate kinase, muscle (PKM2) was a target substrate of USP25. Kyoto Encyclopedia of Genes and Genomes pathway analysis indicated the USP25 regulated aerobic glycolysis and lactate production during M1-like polarization via PKM2. Further analysis showed that the USP25-PKM2-aerobic glycolysis axis positively regulated M1-like polarization and exacerbated AKI in mice, providing potential therapeutic targets for AKI treatment.

Keywords: Acute kidney injury; Aerobic glycolysis; Ischemia-reperfusion; M1-like macrophage; PKM2; Ubiquitin-specific protease 25.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acute Kidney Injury*
  • Animals
  • Glycolysis
  • Ischemia / metabolism
  • Kidney / metabolism
  • Macrophages / metabolism
  • Mice
  • Mice, Inbred C57BL
  • Muscles
  • Pyruvate Kinase / metabolism
  • Reperfusion
  • Reperfusion Injury* / metabolism
  • Ubiquitin Thiolesterase / metabolism

Substances

  • Pyruvate Kinase
  • USP25 protein, mouse
  • Ubiquitin Thiolesterase