4-Hydroxynonenal (HNE) modified proteins in metabolic diseases

Free Radic Biol Med. 2017 Oct;111:309-315. doi: 10.1016/j.freeradbiomed.2016.10.497. Epub 2016 Nov 1.

Abstract

4-Hydroxynonenal (HNE) is one of the quantitatively most important products of lipid peroxidation. Due to its high toxicity it is quickly metabolized, however, a small share of HNE avoids enzymatic detoxification and reacts with biomolecules including proteins. The formation of HNE-protein-adducts is one of the accompanying processes in oxidative stress or redox disbalance. The modification of proteins might occur at several amino acids side chains, leading to a variety of products and having effects on the protein function and fate. This review summarizes current knowledge on the formation of HNE-modified proteins, their fate in mammalian cells and their potential role as a damaging agents during oxidative stress. Furthermore, the potential of HNE-modified proteins as biomarkers for several diseases are highlighted.

Keywords: 4-hydroxynonenal; HNE metabolism; HNE-modified Proteins; Proteasome; Proteolysis.

Publication types

  • Review

MeSH terms

  • Alcohol Dehydrogenase / genetics
  • Alcohol Dehydrogenase / metabolism
  • Aldehyde Dehydrogenase / genetics
  • Aldehyde Dehydrogenase / metabolism
  • Aldehydes / metabolism*
  • Animals
  • Biomarkers / metabolism
  • Glutathione Transferase / genetics
  • Glutathione Transferase / metabolism
  • Heat-Shock Proteins / genetics
  • Heat-Shock Proteins / metabolism
  • Humans
  • Hydrolysis
  • Lipid Peroxidation
  • Metabolic Diseases / genetics
  • Metabolic Diseases / metabolism*
  • Metabolic Diseases / pathology
  • Oxidative Stress
  • Proteasome Endopeptidase Complex / metabolism*
  • Protein Processing, Post-Translational*
  • Proteolysis

Substances

  • Aldehydes
  • Biomarkers
  • Heat-Shock Proteins
  • Alcohol Dehydrogenase
  • Aldehyde Dehydrogenase
  • Glutathione Transferase
  • Proteasome Endopeptidase Complex
  • 4-hydroxy-2-nonenal