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Molecular cloning of cDNA for nonhepatic mitochondrial arginase (arginase II) and comparison of its induction with nitric oxide synthase in a murine macrophage‐like cell line
Author(s) -
Gotoh Tomomi,
Sonoki Takashi,
Nagasaki Akitoshi,
Terada Kazutoyo,
Takiguchi Masaki,
Mori Masataka
Publication year - 1996
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(96)01015-0
Subject(s) - arginase , biochemistry , nitric oxide synthase , complementary dna , biology , microbiology and biotechnology , nitric oxide , mitochondrion , arginine , messenger rna , enzyme , amino acid , gene , endocrinology
Arginase exists in two isoforms. Liver‐type arginase (arginase I) is expressed almost exclusively in the liver and catalyzes the last step of urea synthesis, whereas the nonhepatic type (arginase II) is expressed in extrahepatic tissues. Arginase II has been proposed to play a role in down‐regulation of nitric oxide synthesis. A cDNA for human arginase II was isolated. A polypeptide of 354 amino acid residues including the putative NH 2 ‐terminal presequence for mitochondrial import was predicted. It was 59% identical with arginase I. The arginase II precursor synthesized in vitro was imported into isolated mitochondria and proteolytically processed. mRNA for human arginase II was present in the kidney and other tissues, but was not detected in the liver. Arginase II mRNA was coinduced with nitric oxide synthase mRNA in murine macrophage‐like RAW 264.7 cells by lipopolysaccharide. This induction was enhanced by dexamethasone and dibutyryl cAMP, and was prevented by interferon‐γ. Possible roles of arginase II in NO synthesis are discussed.