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Regulation of the genes for arginase isoforms and related enzymes in mouse macrophages by lipopolysaccharide

Regulation of the genes for arginase isoforms and related enzymes in mouse macrophages by... Abstract Arginase exists in two isoforms, the hepatic (arginase I) and extrahepatic types (arginase II). Arginase I is markedly induced in rat peritoneal macrophages and rat tissues in vivo by bacterial lipopolysaccharide (LPS). In contrast, both arginase I and arginase II are induced in LPS-activated mouse peritoneal macrophages. In the present study, expression of arginase isoforms and related enzymes was studied in mouse tissues in vivo and in peritoneal macrophages with RNA blot and immunoblot analyses and enzyme assay. When mice were injected intraperitoneally with LPS, inducible nitric oxide synthase (iNOS) and arginase II were induced early in the lung and spleen. mRNAs for argininosuccinate synthase (AS) and ornithine decarboxylase (ODC) were also induced early. In comparison, arginase I was induced later in the lung. Early induction of iNOS, arginase II, AS, ODC, and cationic amino acid transporter 2 and late induction of arginase I were observed in LPS-activated peritoneal macrophages. These results indicate that the genes for the two arginase isoforms are regulated differentially. Possible roles of the arginase isoforms in the regulation of nitric oxide production and in polyamine synthesis are discussed. arginase I arginase II nitric oxide nitric oxide synthase Footnotes Address for reprint requests and other correspondence: M. Mori, Dept. of Molecular Genetics, Kumamoto Univ. School of Medicine, Honjo 2-2-1, Kumamoto 860-0811, Japan (E-mail: masa@gpo.kumamoto-u.ac.jp ). We thank our colleagues for the comments and discussion and Gary Wright of this laboratory for critically reading the manuscript. This work was supported in part by Grants-in-Aid (0557020 and 09276103) from the Ministry of Education, Science, Sports, and Culture of Japan to M. Mori and a grant from Taisho Pharmaceutical (Tokyo, Japan) to M. Mori. The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked “ advertisement ” in accordance with 18 U.S.C. §1734 solely to indicate this fact. Copyright © 1999 the American Physiological Society http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png AJP - Endocrinology and Metabolism The American Physiological Society

Regulation of the genes for arginase isoforms and related enzymes in mouse macrophages by lipopolysaccharide

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Publisher
The American Physiological Society
Copyright
Copyright © 2011 the American Physiological Society
ISSN
0193-1849
eISSN
1522-1555
Publisher site
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Abstract

Abstract Arginase exists in two isoforms, the hepatic (arginase I) and extrahepatic types (arginase II). Arginase I is markedly induced in rat peritoneal macrophages and rat tissues in vivo by bacterial lipopolysaccharide (LPS). In contrast, both arginase I and arginase II are induced in LPS-activated mouse peritoneal macrophages. In the present study, expression of arginase isoforms and related enzymes was studied in mouse tissues in vivo and in peritoneal macrophages with RNA blot and immunoblot analyses and enzyme assay. When mice were injected intraperitoneally with LPS, inducible nitric oxide synthase (iNOS) and arginase II were induced early in the lung and spleen. mRNAs for argininosuccinate synthase (AS) and ornithine decarboxylase (ODC) were also induced early. In comparison, arginase I was induced later in the lung. Early induction of iNOS, arginase II, AS, ODC, and cationic amino acid transporter 2 and late induction of arginase I were observed in LPS-activated peritoneal macrophages. These results indicate that the genes for the two arginase isoforms are regulated differentially. Possible roles of the arginase isoforms in the regulation of nitric oxide production and in polyamine synthesis are discussed. arginase I arginase II nitric oxide nitric oxide synthase Footnotes Address for reprint requests and other correspondence: M. Mori, Dept. of Molecular Genetics, Kumamoto Univ. School of Medicine, Honjo 2-2-1, Kumamoto 860-0811, Japan (E-mail: masa@gpo.kumamoto-u.ac.jp ). We thank our colleagues for the comments and discussion and Gary Wright of this laboratory for critically reading the manuscript. This work was supported in part by Grants-in-Aid (0557020 and 09276103) from the Ministry of Education, Science, Sports, and Culture of Japan to M. Mori and a grant from Taisho Pharmaceutical (Tokyo, Japan) to M. Mori. The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked “ advertisement ” in accordance with 18 U.S.C. §1734 solely to indicate this fact. Copyright © 1999 the American Physiological Society

Journal

AJP - Endocrinology and MetabolismThe American Physiological Society

Published: Jul 1, 1999

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