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Am J Physiol Regul Integr Comp Physiol 279: R2237-R2242, 2000;
0363-6119/00 $5.00
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Vol. 279, Issue 6, R2237-R2242, December 2000

Arginase I: a limiting factor for nitric oxide and polyamine synthesis by activated macrophages?

Diane Kepka-Lenhart1, Sanjay K. Mistry1, Guoyao Wu2, and Sidney M. Morris Jr.1

1 Department of Molecular Genetics and Biochemistry, University of Pittsburgh School of Medicine, Pittsburgh, Pennsylvania 15261; and 2 Department of Animal Science, Texas A & M University, College Station, Texas 77843

Because arginase hydrolyzes arginine to produce ornithine and urea, it has the potential to regulate nitric oxide (NO) and polyamine synthesis. We tested whether expression of the cytosolic isoform of arginase (arginase I) was limiting for NO or polyamine production by activated RAW 264.7 macrophage cells. RAW 264.7 cells, stably transfected to overexpress arginase I or beta -galactosidase, were treated with interferon-gamma to induce type 2 NO synthase or with lipopolysaccharide or 8-bromo-cAMP (8-BrcAMP) to induce ornithine decarboxylase. Overexpression of arginase I had no effect on NO synthesis. In contrast, cells overexpressing arginase I produced twice as much putrescine after activation than did cells expressing beta -galactosidase. Cells overexpressing arginase I also produced more spermidine after treatment with 8-BrcAMP than did cells expressing beta -galactosidase. Thus endogenous levels of arginase I are limiting for polyamine synthesis, but not for NO synthesis, by activated macrophage cells. This study also demonstrates that it is possible to alter arginase I levels sufficiently to affect polyamine synthesis without affecting induced NO synthesis.

nitric oxide synthase; ornithine decarboxylase; putrescine; RAW 264.7


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