TY - JOUR
T1 - Cloning and characterization of the human type II arginase gene
AU - Vockley, Joseph G.
AU - Jenkinson, Christopher P.
AU - Shukla, Hridayabiranjan
AU - Kern, Rita M.
AU - Grody, Wayne W.
AU - Cederbaum, Stephen D.
N1 - Copyright:
Copyright 2017 Elsevier B.V., All rights reserved.
PY - 1996/12/1
Y1 - 1996/12/1
N2 - 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.
AB - 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.
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U2 - 10.1006/geno.1996.0606
DO - 10.1006/geno.1996.0606
M3 - Article
C2 - 8954792
AN - SCOPUS:0030447115
VL - 38
SP - 118
EP - 123
JO - Genomics
JF - Genomics
SN - 0888-7543
IS - 2
ER -