To Be, or Nox to Be, Endoplasmic Reticulum Stress in Hypertension
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See related article, pp 235–246
In the vasculature, reactive oxygen species (ROS) play key roles in signal transduction related to contraction, relaxation, hypertrophy, proliferation, migration, and cell death, and the Nox (NADPH oxidase) isozymes are a major source of these ROS.1 Over the past 20 years, it has been established that Nox enzymes have specific subcellular localizations.2 In fact, several studies have identified and refined the specific locations of Nox redox signaling pathways that are involved in vascular physiology and pathophysiology. For example, in cultured vascular smooth muscle cells (VSMC), Nox1 is colocalized with caveolin in caveolin-enriched fractions on the cell surface,3 whereas Nox4 is colocalized with vinculin at focal adhesions.3
Given that ROS production is a precisely controlled process during homeostatic conditions, disturbance of this mechanism could lead to excessive ROS production, oxidative stress, and irreversible injury to the vasculature. However, the connection between subcellular localization of Nox enzymes, and organelle dysfunction, especially in disease conditions, still needs clarification. In this issue of Hypertension, Camargo et al4 provide important evidence of Nox4 upregulation on the endoplasmic reticulum (ER), …