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Journal of Histochemistry and Cytochemistry, Vol. 46, 249-256, Copyright © 1998 by The Histochemical Society, Inc.

ARTICLE

Expression and Distribution of Heme Oxygenase-2 mRNA and Protein in Rat Kidney

Ying Hua, Ning Maa, Miao Yangb, and Reiji Sembaa
a Department of Anatomy, Mie University School of Medicine, Mie, Japan
b Department of Biochemistry, Mie University School of Medicine, Mie, Japan

Correspondence to: Reiji Semba, Dept. of Anatomy, Mie U. School of Medicine, Tsu, Mie 514, Japan.

Recent studies suggest that carbon monoxide (CO), which is formed by the enzyme heme oxygenase (HO) during the conversion of heme to biliverdin, shares some of the chemical and biological properties of nitric oxide (NO) and may play roles similar to those of NO. Heme oxygenase activity in the kidney has been reported for many years, and there are some reports on the expression of mRNA for two HO isozymes (HO-1 and HO-2) and cellular localization of HO-1 protein. However, cellular localization of HO-2 protein in the kidney under normal conditions has not been reported. In the present study we examined the expression and distribution of HO-2 mRNA and HO-2 protein in rat kidney using RNA protection assay and light and electron immunocytochemistry. RNA protection assay confirmed constitutive expression of HO-2 transcript in rat kidney. HO-2 immunoreactivity was selectively found in epithelial cells of the thick ascending limb and distal convoluted tubule, connecting tubule cells, and principal cells of the collecting duct. These results suggest that HO-2 is synthesized in the kidney and that HO-2 in the epithelial cells of renal tubules may serve as a source for CO generation under normal conditions. (J Histochem Cytochem 46:249—256, 1998)

Key Words: carbon monoxide, RNA protection assay, Western blot analysis, immunocytochemistry, distal tubule, collecting duct


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