Recent advances in arginine metabolism

Curr Opin Clin Nutr Metab Care. 2004 Jan;7(1):45-51. doi: 10.1097/00075197-200401000-00009.

Abstract

Purpose of review: Arginine metabolism has been a topic of intense interest over the past 15-20 years, primarily with regard to the role of arginine as the nitrogen donor for nitric oxide synthesis. However, other important aspects of arginine metabolism, such as arginine transport and arginine catabolism via the arginases, arginine decarboxylase or agmatinase, have been less well studied. The purpose of this review is to highlight recent studies on the urea cycle, agmatine metabolism, and the arginases.

Recent findings: Recent advances include the cloning of complementary DNA encoding agmatinase, N-acetylglutamate synthetase, and proteins involved in mitochondrial arginine transport, as well as initial investigations of their regulation and tissue-specific expression. The most exciting results of studies in this area over the past year or so have indicated new roles for the arginases in health and disease, as a result of their effects on the synthesis of nitric oxide, proline, or polyamines, or on the expression of specific genes by their ability to limit the availability of free arginine.

Summary: Recent studies have led to refinements in our understanding of the urea cycle. Agmatine metabolism is still largely a mystery, although the isolation of cloned cDNA for agmatinase and possibly also arginine decarboxylase should stimulate much needed investigations in this area. The most exciting findings in the field are coming from studies indicating new roles for the arginases in various diseases.

Publication types

  • Research Support, U.S. Gov't, Non-P.H.S.
  • Research Support, U.S. Gov't, P.H.S.
  • Review

MeSH terms

  • Agmatine / metabolism
  • Arginase / antagonists & inhibitors
  • Arginase / metabolism
  • Arginine / metabolism*
  • Humans
  • Respiratory Tract Diseases / metabolism
  • Urea / metabolism

Substances

  • Agmatine
  • Urea
  • Arginine
  • Arginase