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Journal of Histochemistry and Cytochemistry, Vol. 51, 1151-1160, September 2003, Copyright © 2003, The Histochemical Society, Inc.

ARTICLE

Widespread Expression of Arginase I in Mouse Tissues: Biochemical and Physiological Implications

Hong Yua,b, Paul K. Yooa,c, Claudia C. Aguirrea,b, Rosemarie W. Tsoaa,c, Rita M. Kerna,b, Wayne W. Grodya,c,d,e, Stephen D. Cederbauma,b,d,e, and Ramaswamy K. Iyera,c
a Mental Retardation Research Center, David Geffen School of Medicine at UCLA, Los Angeles, California
b Departments of Psychiatry, David Geffen School of Medicine at UCLA, Los Angeles, California
c Pathology and Laboratory Medicine, David Geffen School of Medicine at UCLA, Los Angeles, California
d Pediatrics, David Geffen School of Medicine at UCLA, Los Angeles, California
e Human Genetics, David Geffen School of Medicine at UCLA, Los Angeles, California

Correspondence to: Ramaswamy K. Iyer, Pathology and Laboratory Medicine, David Geffen School of Medicine at UCLA, 650 Charles Young Drive (South), Los Angeles, CA 90095-1732. E-mail: riyer@mednet.ucla.edu

Arginase I (AI), the fifth and final enzyme of the urea cycle, detoxifies ammonia as part of the urea cycle. In previous studies from others, AI was not found in extrahepatic tissues except in primate blood cells, and its roles outside the urea cycle have not been well recognized. In this study we undertook an extensive analysis of arginase expression in postnatal mouse tissues by in situ hybridization (ISH) and RT-PCR. We also compared arginase expression patterns with those of ornithine decarboxylase (ODC) and ornithine aminotransferase (OAT). We found that, outside of liver, AI was expressed in many tissues and cells such as the salivary gland, esophagus, stomach, pancreas, thymus, leukocytes, skin, preputial gland, uterus and sympathetic ganglia. The expression was much wider than that of arginase II, which was highly expressed only in the intestine and kidney. Several co-localization patterns of AI, ODC, and OAT have been found: (a) AI was co-localized with ODC alone in some tissues; (b) AI was co-localized with both OAT and ODC in a few tissues; (c) AI was not co-localized with OAT alone in any of the tissues examined; and (d) AI was not co-localized with either ODC or OAT in some tissues. In contrast, AII was not co-localized with either ODC or OAT alone in any of the tissues studied, and co-localization of AII with ODC and OAT was found only in the small intestine. The co-localization patterns of arginase, ODC, and OAT suggested that AI plays different roles in different tissues. The main roles of AI are regulation of arginine concentration by degrading arginine and production of ornithine for polyamine biosynthesis, but AI may not be the principal enzyme for regulating glutamate biosynthesis in tissues and cells. (J Histochem Cytochem 51:1151–1160, 2003)

Key Words: arginase, ornithine decarboxylase, ornithine aminotransferase, in situ hybridization, expression


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