Hepatic glutaminase expression: Relationship to kidney-type glutaminase and to the urea cycle

Research output: Contribution to journalReview articlepeer-review

49 Scopus citations

Abstract

Glutamine functions as a major transport form of nitrogen and carbon within the body. In the liver, glutamine is hydrolyzed by a unique liver- type, phosphate-activated glutaminase, and the end products of hepatic glutamine catabolism are glucose and urea. Other tissues possess a different, kidney-type, glutaminase isozyme. The predicted amino acid sequences for the two glutaminases show a high degree of identity, indicating that they are products of different but related genes. Hepatic glutaminase activity is increased during diabetes, starvation, and on feeding high-protein diets, and decreased on feeding low-protein diets, whereas renal glutaminase appears to be regulated only by changes in acid-base status. Changes in the rate of gene transcription are the principal mechanism responsible for the long-term regulation of hepatic glutaminase, but the renal enzyme is regulated at the level of mRNA turnover. The pattern of regulation of hepatic glutaminase parallels that seen for genes encoding key enzymes of gluconeogenesis and urea synthesis, and indicates coordinate regulation of expression in keeping with the role of hepatic glutamine catabolism in these pathways.

Original languageEnglish (US)
Pages (from-to)1468-1474
Number of pages7
JournalFASEB Journal
Volume7
Issue number15
DOIs
StatePublished - 1993

All Science Journal Classification (ASJC) codes

  • Biotechnology
  • Biochemistry
  • Molecular Biology
  • Genetics

Keywords

  • gluconeogenesis
  • glutaminase
  • glutamine
  • liver
  • urea synthesis

Fingerprint

Dive into the research topics of 'Hepatic glutaminase expression: Relationship to kidney-type glutaminase and to the urea cycle'. Together they form a unique fingerprint.

Cite this