O-GlcNAcylation as a novel ammonia-induced posttranslational protein modification in cultured rat astrocytes

Metab Brain Dis. 2014 Dec;29(4):975-82. doi: 10.1007/s11011-013-9454-7. Epub 2013 Dec 1.

Abstract

Hepatic encephalopathy (HE) is a clinical manifestation of a low grade cerebral edema with a mutual interrelationship between osmotic- and oxidative stress. This leads to RNA oxidation and posttranslational protein modifications such as protein tyrosine nitration with pathophysiological relevance. Here, we report on O-GlcNAcylation as another ammonia-induced posttranslational protein modification in cultured rat astrocytes. NH4Cl induced O-GlcNAcylation of distinct proteins (25-250 kDa) in astrocytes in a dose- and time-dependent manner. Exposure of astrocytes to NH4Cl (5 mmol/l) for 48 h and 72 h significantly increased protein O-GlcNAcylation by about 2-fold and 4-fold, respectively. NH4Cl at a concentration of 1 mmol/l was sufficient to double protein O-GlcNAcylation in astrocytes after 72 h as compared to untreated controls. Ammonia-induced protein O-GlcNAcylation was sensitive towards glutamine-synthetase inhibition by methionine sulfoximine (MSO), but was not induced by hypoosmolarity (205 mosmol/l) or CH3NH3Cl (5 mmol/l). Increased protein O-GlcNAcylation in NH4Cl (5 mmol/l, 48 h)-treated astrocytes was fully reversible within 24 h after withdrawal of NH4Cl from culture medium. Amongst the proteins which are O-GlcNAcylated in response to ammonia, GAPDH was identified. It is concluded that ammonia induces reversible protein O-GlcNAcylation in astrocytes that depends on glutamine synthesis but not on astrocyte swelling per se or ammonia-induced pH-changes. In view of the complex involvement of O-GlcNAcylation in cell regulation, such as energy metabolism, apoptosis and circadian rhythmicity and in pathologies, such as neurodegenerative diseases, O-GlcNAcylation might contribute to the pathophysiology of hepatic encephalopathy.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acetylglucosamine / metabolism*
  • Ammonium Chloride / pharmacology*
  • Animals
  • Animals, Newborn
  • Astrocytes / metabolism*
  • Cells, Cultured
  • Glutamine / metabolism
  • Glyceraldehyde-3-Phosphate Dehydrogenase (Phosphorylating) / metabolism
  • Glycosylation
  • Hydrogen-Ion Concentration
  • Methylamines / pharmacology
  • N-Acetylglucosaminyltransferases / metabolism*
  • Nerve Tissue Proteins / metabolism*
  • Osmolar Concentration
  • Primary Cell Culture
  • Protein Processing, Post-Translational*
  • Rats
  • Rats, Wistar

Substances

  • Methylamines
  • Nerve Tissue Proteins
  • Ammonium Chloride
  • Glutamine
  • methylamine
  • Glyceraldehyde-3-Phosphate Dehydrogenase (Phosphorylating)
  • N-Acetylglucosaminyltransferases
  • O-GlcNAc transferase
  • Acetylglucosamine