Signaling by 4-hydroxy-2-nonenal: Exposure protocols, target selectivity and degradation

Arch Biochem Biophys. 2017 Mar 1:617:145-154. doi: 10.1016/j.abb.2016.11.003. Epub 2016 Nov 10.

Abstract

4-hydroxy-2-nonenal (HNE), a major non-saturated aldehyde product of lipid peroxidation, has been extensively studied as a signaling messenger. In these studies a wide range of HNE concentrations have been used, ranging from the unstressed plasma concentration to far beyond what would be found in actual pathophysiological condition. In addition, accumulating evidence suggest that signaling protein modification by HNE is specific with only those proteins with cysteine, histidine, and lysine residues located in certain sequence or environments adducted by HNE. HNE-signaling is further regulated through the turnover of HNE-signaling protein adducts through proteolytic process that involve proteasomes, lysosomes and autophagy. This review discusses the HNE concentrations and exposure modes used in signaling studies, the selectivity of the HNE-adduction site, and the turnover of signaling protein adducts.

Keywords: Adduct; Concentration; HNE; Oxidative stress; Redox signaling; Turnover.

Publication types

  • Review

MeSH terms

  • Aldehydes / chemistry*
  • Animals
  • Autophagy
  • Cysteine / chemistry
  • Histidine / chemistry
  • Humans
  • Lipid Peroxidation*
  • Lysine / chemistry
  • Lysosomes / chemistry
  • Oxidative Stress
  • Proteasome Endopeptidase Complex / chemistry
  • Protein Processing, Post-Translational
  • Signal Transduction*

Substances

  • Aldehydes
  • Histidine
  • Proteasome Endopeptidase Complex
  • 4-hydroxy-2-nonenal
  • Lysine
  • Cysteine