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Drug Metabolism and Disposition Fast Forward
First published on September 23, 2005; DOI: 10.1124/dmd.105.006171

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Received for publication June 29, 2005.
Revised September 21, 2005.
Accepted for publication September 22, 2005.

Quantitative Analysis of FMO Gene mRNA Levels in Human Tissue

Jun Zhang 1 John R. Cashman 2*

1 Human Biomolecular Research Institute 2 Human Biomolecular Research Inst.

* Address correspondence to: E-mail: jcashman{at}hbri.org

Abstract

The developmental- and tissue-specific expression of FMO enzymes has been previously characterized in a number of animal species, including humans, mice, rats, and rabbits. In this study, we used sensitive real-time RT-PCR methodology to systematically quantify the steady-state mRNA levels of FMO1, 2, 3, 4, and 5 in human tissues. We examined the developmental regulation of these enzymes in brain tissue. FMO1 was found to be down-regulated in human adult brain. Amount of other FMO mRNAs in human brains in different age groups was not significantly different. The study also provided a systematic quantitative comparison of the steady-state mRNA levels of FMO1 to 5 in several major human organs (i.e., liver, lung, kidney, small intestine, and brain). The nature of the quantitative analysis allowed a comprehensive comparison of each FMO mRNA in different tissues as well as among FMO isoforms in the same tissue. A comparison between fetal liver and adult liver showed that FMO1 was the only FMO that was down regulated; all other FMOs had greater amounts of mRNA in adult liver. FMO5 was the most prominent FMO form detected in fetal liver. FMO5 mRNA level was nearly as abundant as FMO3 in adult liver. While other FMOs displayed significant dominant tissue-specific mRNA profile (i.e., FMO1 in kidney, FMO2 in lung, FMO3 and FMO5 in adult liver), FMO4 mRNA was observed more broadly at relatively comparable levels in liver, kidney, lung, and small intestine.


Key words: flavin-containing monooxygenase, transcriptional regulation


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T. Borbas, J. Zhang, M. A. Cerny, I. Liko, and J. R. Cashman
Investigation of Structure and Function of a Catalytically Efficient Variant of the Human Flavin-Containing Monooxygenase Form 3
Drug Metab. Dispos., December 1, 2006; 34(12): 1995 - 2002.
[Abstract] [Full Text] [PDF]


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