NADPH oxidase 5 and renal disease

Curr Opin Nephrol Hypertens. 2015 Jan;24(1):81-7. doi: 10.1097/MNH.0000000000000081.

Abstract

Purpose of review: To highlight the latest novel developments in renal NADPH oxidase 5 (Nox5) biology, with an emphasis not only on diabetic nephropathy but also on many of the other renal disease contexts in which oxidative stress is implicated.

Recent findings: Nox-derived reactive oxygen species have been shown to contribute to a wide variety of renal diseases, particularly in the settings of chronic renal disease such as diabetic nephropathy. Although much emphasis has been placed on the role of NADPH oxidase 4 in this setting, a growing body of work continues to uncover the key roles for other Nox family members, not only in diabetic kidney disease, but also in a diverse array of renal pathological conditions. The most recently identified member of the Nox family, Nox5, has for the most part been overlooked in renal disease, partly owing to its absence from the rodent genome. New evidence suggests that Nox5 may be a contributing factor in glomerulopathies and altered tubular physiology. Furthermore, Nox5 appears to harbor a significant number of single-nucleotide polymorphisms that alter its enzymatic activity.

Summary: Given the unique structure and expression pattern of Nox5, it may prove to be an attractive therapeutic target in the treatment of renal disease.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Diabetic Nephropathies / enzymology
  • Humans
  • Membrane Proteins* / antagonists & inhibitors
  • Membrane Proteins* / genetics
  • Membrane Proteins* / metabolism
  • NADPH Oxidase 5
  • NADPH Oxidases* / antagonists & inhibitors
  • NADPH Oxidases* / genetics
  • NADPH Oxidases* / metabolism
  • Polymorphism, Single Nucleotide
  • Promoter Regions, Genetic
  • Reactive Oxygen Species / metabolism*
  • Renal Insufficiency, Chronic / drug therapy
  • Renal Insufficiency, Chronic / enzymology*

Substances

  • Membrane Proteins
  • Reactive Oxygen Species
  • NADPH Oxidase 5
  • NADPH Oxidases
  • NOX5 protein, human