O-GlcNAcylation regulates hyperglycemia-induced GPX1 activation

Biochem Biophys Res Commun. 2010 Jan 1;391(1):756-61. doi: 10.1016/j.bbrc.2009.11.133. Epub 2009 Nov 26.

Abstract

Hyperglycemia induces activation of glutathione peroxidase 1 (GPX1), an anti-oxidant enzyme essential for cell survival during oxidative stress. However, the mechanism of GPX1 activation is unclear. Here, we report that hyperglycemia-induced protein glycosylation by O-linked N-acetylglucosamine (O-GlcNAc) is crucial for activation of GPX1 and for its binding to c-Abl and Arg kinases. GPX1 itself is modified with O-GlcNAc on its C-terminus. We also demonstrate that pharmacological injection of the O-GlcNAcase inhibitor NTZ induces GPX1 activation in the mouse liver. Our findings suggest a crucial role for GPX1 and its O-GlcNAc modification in hyperglycemia and diabetes mellitus.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acetylglucosamine / metabolism*
  • Acylation
  • Animals
  • Cell Line
  • Diabetes Mellitus / enzymology*
  • Enzyme Activation
  • Female
  • Glutathione Peroxidase / genetics
  • Glutathione Peroxidase / metabolism*
  • Glutathione Peroxidase GPX1
  • Humans
  • Hyperglycemia / enzymology*
  • Mice
  • Mice, Inbred C3H
  • Mice, Inbred C57BL
  • Rats

Substances

  • Glutathione Peroxidase
  • Acetylglucosamine
  • Glutathione Peroxidase GPX1