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Tissue Distribution of Human AKR1C3 and Rat Homolog in the Adult Genitourinary System

Joseph Azzarello, Kar-Ming Fung and Hsueh-Kung Lin

Department of Urology (JA,H-KL), Department of Physiology (JA,H-KL), and Department of Pathology (K-MF), University of Oklahoma Health Sciences Center, Oklahoma City, Oklahoma, and Department of Veterans Affairs Medical Center, Oklahoma City, Oklahoma (K-MF,H-KL)

Correspondence to: Hsueh-Kung Lin, PhD, Department of Urology, University of Oklahoma Health Sciences Center, 800 Research Parkway, Room 462, Oklahoma City, OK 73034. E-mail: hk-lin{at}ouhsc.edu

Human aldo-keto reductase (AKR) 1C3 (type 2 3-hydroxysteroid dehydrogenase/type 5 17β-hydroxysteroid dehydrogenase) catalyzes androgen, estrogen, and prostaglandin metabolism. AKR1C3 is therefore implicated in regulating ligand access to the androgen receptor, estrogen receptor, and peroxisome proliferator activating receptor in hormone target tissues. Recent reports on close relationships between ARK1C3 and various cancers including breast and prostate cancers implicate the involvement of AKR1C3 in cancer development or progression. We previously described the characterization of an isoform-specific monoclonal antibody against AKR1C3 that does not cross-react with related, >86% sequence identity, human AKR1C1, AKR1C2, or AKR1C4, human aldehyde reductase AKR1A1, or rat 3-hydroxysteroid dehydrogenase (AKR1C9). In this study, a clone of murine monoclonal antibody raised against AKR1C3 was identified and characterized for its recognition of rat homolog. Tissue distribution of human AKR1C3 and its rat homolog in adult genitourinary systems including kidney, bladder, prostate, and testis was studied by IHC. A strong immunoreactivity was detected not only in classically hormone-associated tissues such as prostate and testis but also in non–hormone-associated tissues such as kidney and bladder in humans and rats. The distribution of these two enzymes was comparable but not identical between the two species. These features warrant future studies of AKR1C3 in both hormone- and non–hormone-associated tissues and identification of the rodent homolog for establishing animal models. (J Histochem Cytochem 56:853–861, 2008)

Key Words: hydroxysteroid dehydrogenase • aldo-keto reductase • bladder • kidney • prostate • testis

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