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Originally published In Press as doi:10.1074/jbc.M002180200 on July 31, 2000

J. Biol. Chem., Vol. 275, Issue 46, 36164-36171, November 17, 2000
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Polymorphic Gene Regulation and Interindividual Variation of UDP-glucuronosyltransferase Activity in Human Small Intestine*

Christian P. StrassburgDagger §, Susanne KneipDagger , Juliane ToppDagger , Petra Obermayer-StraubDagger , Ayse BarutDagger , Robert H. Tukey, and Michael P. MannsDagger

From the Dagger  Department of Gastroenterology and Hepatology, Hannover Medical School, 30625 Hannover, Germany and the  Departments of Chemistry & Biochemistry and Pharmacology, University of California, San Diego, La Jolla, California 92093

UDP-glucuronosyltransferases (UGTs) convert dietary constituents, drugs, and environmental mutagens to inactive hydrophilic glucuronides. Recent studies have shown that the expression of the UGT1 and UGT2 gene families is regulated in a tissue-specific fashion. Human small intestine represents a major site of resorption of dietary constituents and orally administered drugs and plays an important role in extrahepatic UGT directed metabolism. Expression of 13 UGT1A and UGT2B genes coupled with functional and catalytic analyses were studied using 18 small intestinal and 16 hepatic human tissue samples. Hepatic expression of UGT gene transcripts was without interindividual variation. In contrast, a polymorphic expression pattern of all the UGT genes was demonstrated in duodenal, jejunal, and ileal mucosa, with the exception of UGT1A10. To complement these studies, interindividual expression of UGT proteins and catalytic activities were also demonstrated. Hyodeoxycholic acid glucuronidation, catalyzed primarily by UGT2B4 and UGT2B7, showed a 7-fold interindividual variation in small intestinal duodenal samples, in contrast to limited variation in the presence of 4-methylumbelliferone, a substrate glucuronidated by most UGT1A and UGT2B gene products. Linkage of RNA expression patterns to protein abundance were also made with several mono-specific antibodies to the UGTs. These results are in contrast to a total absence of polymorphic variation in gene expression, protein abundance, and catalytic activity in liver. In addition, the small intestine exhibits considerable catalytic activity toward most of the different classes of substrates accepted for glucuronidation by the UGTs, which is supported by immunofluorescence analysis of UGT1A protein in the mucosal cell layer of the small intestine. Thus, tissue-specific and interindividual polymorphic regulation of UGT1A and UGT2B genes in small intestine is identified and implicated as molecular biological determinant contributing to interindividual prehepatic drug and xenobiotic metabolism in humans.

* This work was supported by Deutsche Forschungsgemeinschaft Grant STR493/3-1 (to C. P. S.) and United States Public Health Service Grant GM49135 (to R. H. T).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

§ To whom correspondence should be addressed: Dept. of Gastroenterology and Hepatology, Hannover Medical School, Carl-Neuberg-Str. 1, 30625 Hannover, Germany. Tel.: 49-511-532-2853; Fax: 49-511-532-2093; E-mail: strassburg.christian@mh-hannover.de.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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