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Am J Physiol Gastrointest Liver Physiol 280: G389-G399, 2001;
0193-1857/01 $5.00
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Vol. 280, Issue 3, G389-G399, March 2001

Rat colon ornithine and arginine metabolism: coordinated effects after proliferative stimuli

Xiaoli Han1, Michael N. Kazarinoff2, Nikolaus Seiler3, and Bruce A. Stanley1

1 Section of Technology Development and Research Resources H093, Pennsylvania State University College of Medicine, Hershey, Pennsylvania 17033-2390; 2 Division of Nutritional Sciences and Department of Biochemistry and Molecular Biology, Cornell University, Ithaca, New York 14853; and 3 Institut de Recherche Contre les Cancers de l'Appareil Digestif, Institut National de la Santé et de la Recherche Médicale, 67091 Strasbourg Cedex, France

Ornithine decarboxylase (ODC) catalyzes the first step in the polyamine biosynthetic pathway, a highly regulated pathway in which activity increases during rapid growth. Other enzymes also metabolize ornithine, and in hepatomas, rate of growth correlates with decreased activity of these other enzymes, which thus channels more ornithine to polyamine biosynthesis. Ornithine is produced from arginase cleavage of arginine, which also serves as the precursor for nitric oxide production. To study whether short-term coordination of ornithine and arginine metabolism exists in rat colon, ODC, ornithine aminotransferase (OAT), arginase, ornithine, arginine, and polyamine levels were measured after two stimuli (refeeding and/or deoxycholate exposure) known to synergistically induce ODC activity. Increased ODC activity was accompanied by increased putrescine levels, whereas OAT and arginase activity were reduced by either treatment, accompanied by an increase in both arginine and ornithine levels. These results indicate a rapid reciprocal change in ODC, OAT, and arginase activity in response to refeeding or deoxycholate. The accompanying increases in ornithine and arginine concentration are likely to contribute to increased flux through the polyamine and nitric oxide biosynthetic pathways in vivo.

ornithine decarboxylase; arginase; ornithine aminotransferase; tumor promoters; polyamines


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