Cloning and characterization of the mouse and rat type II arginase genes

Mol Genet Metab. 1998 Mar;63(3):168-75. doi: 10.1006/mgme.1997.2669.

Abstract

Two forms of arginase, both catalyzing the hydrolysis of arginine to ornithine and urea, are found in animals ranging from amphibians to mammals. In humans, inherited deficiency of hepatic or type I arginase results in hyperargininemia, a syndrome characterized by periodic episodes of hyperammonemia, spasticity, and neurological deterioration. In these patients, a second extrahepatic or type II arginase activity is significantly increased, an induction that may partially compensate for the lack of AI activity and apparently mitigates some of the clinical effects of the condition. Cloning and characterization of the human AII cDNA was recently accomplished. The cloning, sequencing, and partial characterization of the mouse and rat AII cDNAs are reported herein. The DNA sequences predicted polypeptides of 354 amino acids, including a N-terminal mitochondrial import signal. Sequence homology to the human type II arginase, arginase activity data, and immunoprecipitation with an anti-AII antibody confirm the identity of these cloned genes as rodent extrahepatic type II arginases.

Publication types

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

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Arginase / chemistry
  • Arginase / genetics*
  • Arginase / metabolism
  • Cloning, Molecular*
  • DNA, Complementary
  • Escherichia coli / metabolism
  • Female
  • Humans
  • Male
  • Mice
  • Mice, Inbred C57BL
  • Molecular Sequence Data
  • Phylogeny
  • Precipitin Tests
  • Rats
  • Rats, Sprague-Dawley
  • Sequence Homology, Amino Acid
  • Urea / metabolism

Substances

  • DNA, Complementary
  • Urea
  • Arg2 protein, rat
  • Arginase

Associated data

  • GENBANK/U90886
  • GENBANK/U90887