Three novel mutations in the liver-type arginase gene in three unrelated Japanese patients with argininemia
- Kumamoto Univ. (Japan)
- National Suzuka Hospital (Japan)
- National Children's Hospital, Tokyo (Japan)
Argininemia is caused by a hereditary deficiency of liver-type arginase (E.C.3.5.3.1.) and is characterized by psychomotor retardation and spastic tetraplegia. The authors examined findings in three Japanese patients with argininemia, by using the PCR, cloning, and sequencing procedures. They found three different mutations - G-to-A-365 in exon 4, G-to-C-703 in exon 7, and C-del-842 in exon 8 - thereby leading to mutant arginase proteins of W122X, G235R, and L282FS, respectively. Patient 1 was a compound heterozygote, inheriting the allele with G-to-A-365 from his mother and the allele with G-to-C-703 from his father. Patients 2 and 3 were homozygotes of the allele with G-to-C-703 and of the allele with C-del-842, respectively. Expression tests of these mutant arginases in Escherichia coli indicated that the mutant arginase of W122X did not remain a stable product. The other two mutant arginases - G235R and L282FS - were detected by immunoblot analyses. There was no evidence of activity of the three mutant arginases expressed in E. coli. The authors tentatively conclude that argininemia is heterogeneous, at the molecular level. 27 refs., 4 figs., 1 tab.
- OSTI ID:
- 6717399
- Journal Information:
- American Journal of Human Genetics; (United States), Vol. 51:6; ISSN 0002-9297
- Country of Publication:
- United States
- Language:
- English
Similar Records
Total beta-globin gene deletion has high frequency in Filipinos
Myosin VIIA mutation screening in 189 Usher syndrome type 1 patients
Related Subjects
ARGINASE
GENES
ARGININE
METABOLIC DISEASES
MUTATIONS
CLONING
DNA SEQUENCING
ESCHERICHIA COLI
PATIENTS
PROTEINS
AMIDASES
AMINO ACIDS
BACTERIA
CARBOXYLIC ACIDS
DISEASES
ENZYMES
HYDROLASES
MICROORGANISMS
NON-PEPTIDE C-N HYDROLASES
ORGANIC ACIDS
ORGANIC COMPOUNDS
STRUCTURAL CHEMICAL ANALYSIS
550400* - Genetics