Enzymatic pattern of aldehyde metabolism during HL-60 cell differentiation

Biochem Biophys Res Commun. 1996 Jun 5;223(1):73-9. doi: 10.1006/bbrc.1996.0848.

Abstract

A number of metabolic changes, including modification of different enzyme activities, are linked to the acquisition of differentiated phenotype in HL-60 cells. Enzymes metabolizing aldehydes contribute to maintaining the intracellular steady-state concentration of aldehydes derived from lipid peroxidation. 4-Hydroxynonenal is one of the most important aldehydes produced by this process, and it is able to inhibit proliferation and induce differentiation of HL-60 human leukemic cells. We have now demonstrated that, after induction of HL-60 cell differentiation by 4-hydroxynonenal or DMSO, glutathione transferase activity increases in parallel to the degree of differentiation induction. Moreover, in 4-hydroxynonenal- or DMSO-treated cells, the concentration of reduced glutathione decreases five days after treatment. The rise of glutathione transferase activity, as well as the decrease of reduced glutathione, are possibly linked to the increase of detoxification capability of differentiated cells.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Alcohol Dehydrogenase / metabolism*
  • Aldehyde Dehydrogenase / metabolism*
  • Aldehyde Reductase / metabolism*
  • Aldehydes / metabolism*
  • Aldehydes / pharmacology
  • Cell Differentiation / physiology*
  • Cell Division
  • Dimethyl Sulfoxide / pharmacology
  • Glutathione Transferase / metabolism
  • HL-60 Cells
  • Humans
  • Kinetics
  • Lipid Peroxidation*
  • Phagocytosis

Substances

  • Aldehydes
  • Alcohol Dehydrogenase
  • Aldehyde Reductase
  • Aldehyde Dehydrogenase
  • Glutathione Transferase
  • 4-hydroxy-2-nonenal
  • Dimethyl Sulfoxide