Role of N-acetylglutamate turnover in urea synthesis of rats given proteins of different quality

J Nutr Sci Vitaminol (Tokyo). 2005 Apr;51(2):93-8. doi: 10.3177/jnsv.51.93.

Abstract

The purpose of this study was to find whether the synthesis and degradation of N-acetylglutamate would affect urea synthesis when the dietary protein quality was manipulated. Experiments were done on three groups of rats given diets containing 10 g gluten, 10 g casein or 10 g whole egg protein/100 g for 10 d. The urinary excretion of urea, the liver concentrations of N-acetylglutamate and free glutamate, the liver activity of N-acetylglutamate synthetase increased with the decline in quality of dietary protein. A reverse correlation was observed between the liver N-acetylglutamate degradation and liver Nacetylglutamate concentration. N-Acetylglutamate concentration in the liver was closely correlated with the concentration of glutamate and the N-acetylglutamate synthetase activity in the liver, and excretion of urea. These results suggest that the greater synthesis and the lower degradation rate of N-acetylglutamate in the liver of rats given the lower quality of protein increase the liver concentration of N-acetylglutamate and stimulate urea synthesis.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acetyltransferases / metabolism
  • Amino-Acid N-Acetyltransferase
  • Animals
  • Caseins / administration & dosage
  • Dietary Proteins / administration & dosage*
  • Egg Proteins / administration & dosage
  • Glutamates / analysis
  • Glutamates / metabolism*
  • Glutamic Acid / analysis
  • Glutens / administration & dosage
  • Kinetics
  • Liver / chemistry
  • Liver / enzymology
  • Liver / metabolism
  • Male
  • Rats
  • Rats, Wistar
  • Urea / metabolism*
  • Urea / urine

Substances

  • Caseins
  • Dietary Proteins
  • Egg Proteins
  • Glutamates
  • Glutamic Acid
  • Glutens
  • Urea
  • Acetyltransferases
  • Amino-Acid N-Acetyltransferase
  • N-acetylglutamic acid