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(Received for publication, October 2, 1996, and in revised form, November 7, 1996)
From the Nitric oxide is synthesized by nitric-oxide
synthase from arginine, a common substrate of arginase. Rat peritoneal
macrophages were cultured in the presence of bacterial
lipopolysaccharide (LPS), and expression of the inducible isoform of
nitric-oxide synthase (iNOS) and liver-type arginase (arginase I) was
analyzed. mRNAs for iNOS and arginase I were induced by LPS in a
dose-dependent manner. iNOS mRNA appeared 2 h
after LPS treatment and increased to a near maximum at 8-12 h. On the
other hand, arginase I mRNA that was undetectable prior to the
treatment began to increase after 4 h with a lag time and reached
a maximum at 12 h. Immunoblot analysis showed that iNOS and
arginase I proteins were also induced. mRNA for arginase II, an
arginase isozyme, was not detected in the LPS-activated peritoneal
cells. mRNA for CCAAT/enhancer-binding protein
Volume 272, Number 6,
Issue of February 7, 1997
pp. 3689-3693
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.
§
,§
,
,
,
Department of Molecular Genetics, the
§ Second Department of Internal Medicine, and the
¶ Second Department of Pathology, Kumamoto University School of
Medicine, Kuhonji 4-24-1, Kumamoto 862, Japan
(C/EBP), a
transactivator of the arginase I gene, was also induced, and the
induction was more rapid than that of arginase I mRNA. Changes in
iNOS and arginase I mRNAs were also examined in LPS-injected rats
in vivo. iNOS mRNA increased rapidly in the lung and
spleen, reached a maximum 2-6 h after the LPS treatment, and decreased
thereafter. Arginase I mRNA was induced markedly and more slowly in
both tissues, reaching a maximum in 12 h. Thus, arginase I appears
to have an important role in down-regulating nitric oxide synthesis in
murine macrophages by decreasing the availability of arginine, and the
induction of arginase I is mediated by C/EBP.
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