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PMID: 8954792 Published · ppublish English Journal Article

Cloning and characterization of the human type II arginase gene.

Genomics ·Vol. 38 ·No. 2 ·1996-12-01 ·Pages 118-23

Vockley JG, Jenkinson CP, Shukla H, Kern RM, Grody WW, Cederbaum SD

Abstract

There are two forms of arginase in humans, both catalyzing the hydrolysis of arginine to ornithine and urea. Recent studies in animal models and in Type I arginase-deficient patients suggest that Type II arginase is inducible and may play an important role in the regulation of extra-urea cycle arginine metabolism by modulating cellular arginine concentrations. We PCR amplified and cloned the human Type II arginase gene, the first nonliver arginase gene reported in mammals. While sequence homology to Type I arginase, arginase activity data, and immunoprecipitation with an anti-AII antibody confirm the identity of this gene, Northern blot analysis demonstrates its differential expression in the brain, prostate, and kidney. Type II arginase may be an important part of the arginine regulatory system affecting nitric oxide synthase, arginine decarboxylase, kyotorphin synthase, and arginine-glycine transaminase activities and polyamine and proline biosynthesis.

MeSH Terms
Amino Acid Sequence Animals Arginase/classification,genetics Base Sequence Blotting, Northern Cloning, Molecular DNA, Complementary Humans Molecular Sequence Data Sequence Homology, Amino Acid Sequence Homology, Nucleic Acid
Chemicals
DNA, Complementary Arginase
Authors & Affiliations
6 authors, click to expand affiliations / ORCID
Vockley J G
Department of Molecular Diagnostics, SmithKline Pharmaceuticals, King of Prussia, Pennsylvania 19406, USA.
Jenkinson C P
Shukla H
Kern R M
Grody W W
Cederbaum S D
Article Info
Journal
Genomics
Abbr.
Genomics
ISSN
0888-7543
Published
1996-12-01
Pages
118-23
Language
English
Region
United States
NLM ID
8800135
Subset
IM
Grants
NIDDK NIH HHS · R01 DK079195 · United States
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