Aging Increases Hypoxia-Induced Endothelial Permeability and Blood-Brain Barrier Dysfunction by Upregulating Arginase-II

Aging Dis. 2024 Jan 17;15(6):2710-5415. doi: 10.14336/AD.2023.1225.

Abstract

Increased endothelial permeability plays an important role in blood-brain barrier (BBB) dysfunction and is implicated in neuronal injury in many diseased conditions. BBB disruption is primarily determined by dysfunction of endothelial cell-cell junctions. Deprivation of oxygen supply or hypoxia, a common feature of a variety of human diseases, is a major risk factor for BBB disruption. The molecular regulatory mechanisms of hypoxia-induced BBB dysfunction remain incompletely understood. The mitochondrial enzyme, arginase type II (Arg-II), has been shown to promote endothelial dysfunction. However, its role in hypoxia-induced BBB dysfunction has not been explored. In the C57BL/6J mouse model, hypoxia (8% O2, 24 hours) augments vascular Arg-II in the hippocampus, decreases cell-cell junction protein levels of Zonula occludens-1 (ZO-1), occludin, and CD31 in endothelial cells, increases BBB leakage in the brain in old mice (20 to 24 months) but not in young animals (3 to 6 months). These effects of hypoxia in aging are suppressed in arg-ii-/- mice. Moreover, the age-associated vulnerability of endothelial integrity to hypoxia is demonstrated in senescent human brain microvascular endothelial cell (hCMEC/D3) culture model. Further results in the cell culture model show that hypoxia augments Arg-II, decreases ZO-1 and occludin levels, and increases endothelial permeability, which is prevented by arg-ii gene silencing or by inhibition of mitochondrial reactive oxygen species (mtROS) production. Our study demonstrates an essential role of Arg-II in increased endothelial permeability and BBB dysfunction by promoting mtROS generation, resulting in decreased endothelial cell-cell junction protein levels under hypoxic conditions particularly in aging.

MeSH terms

  • Aging* / metabolism
  • Animals
  • Arginase* / genetics
  • Arginase* / metabolism
  • Blood-Brain Barrier* / metabolism
  • Blood-Brain Barrier* / pathology
  • Capillary Permeability / physiology
  • Endothelial Cells* / metabolism
  • Endothelium, Vascular / metabolism
  • Endothelium, Vascular / pathology
  • Hippocampus / metabolism
  • Hippocampus / pathology
  • Humans
  • Hypoxia* / metabolism
  • Male
  • Mice
  • Mice, Inbred C57BL*
  • Mice, Knockout
  • Up-Regulation

Substances

  • Arginase
  • Arg2 protein, mouse

Grants and funding

This work was supported by grants from the Swiss National Science Foundation [31003A_179261/1 and 310030_219 438/1 to Z.Y] and Swiss Heart Foundation [FF21021 to X.-F.M].