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

FEBS Letters

Sonoki, Takashi¹  Takiguchi, Masaki¹  Gotoh, Tomomi¹  Nagasaki, Akitoshi¹  Terada, Kazutoyo¹  Mori, Masataka¹ 

[1] Department of Molecular Genetics, Kumamoto University School of Medicine, Kuhonji 4-24-1, Kumamoto 862, Japan

关键词: Arginase II;    Gene induction;    Mitochondria;    Nitric oxide synthase;    Macrophage;    Lipopolysaccharide;    LPS;    lipopolysaccharide;    NO;    nitric oxide;    NOS;    nitric oxide synthase;    iNOS or NOS2;    inducible isoform of NOS;    OTC;    ornithine transcarbamylase;    PCR;    polymerase chain reaction;   

DOI  :  10.1016/0014-5793(96)01015-0

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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 NH₂-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.

【 授权许可】

Unknown