Flavin monooxygenases expression

Larsen, B.K. and D. Schlenk. Effect of salinity on flavin-containing monooxygenase expression and activity in rainbow trout (Oncorhynchus mykiss). J. Comp. Physiol. B 171 421-429, 2001. 

KMO is a NADPH-dependant flavin monooxygenase which is localized to the outer membrane of mitochondria [66]. KMO is expressed at high levels in the liver, endothelial cells, and monocytic cells and to a lower extent in the brain. Here, its expression is mainly found in cells of glial nature, specifically in microglial cells and in infiltrating macrophages, whereas little or no expression has been found in astrocytes or in neurons [12, 67]. However, the lack of good antibodies to detect... 

Itagaki, K., Carver, G.T. andPhilpot, R.M. (1996) Expression and characterization ofa modified flavin-containing monooxygenase 4 from humans. The Journal of Biological Chemistry, 271, 2012—20107. 

Using pig and human microsomes and cDNA-expressed human flavin-containing monooxygenase, Lin and Cashman demonstrated a metabolic detoxification pathway that converts tyramine into the HA derivative, 20, and the anti oxime, 21, which was sufficiently stable to permit its chemical characterization". ... 

Koukouritaka SB, Simpson P, Yeung CK, Rettie AE, Hines RN (2002) Human hepatic flavin-containing monooxygenase 1 (FMOl) and 3 (FM03) developmental expression. Pediatr Res 51 236-243... 

Stevens JC, Melton RJ, Zaya MJ, et al. Expression and characterization of functional dog flavin-containing monooxygenase 1. Mol Pharmacol 2003 63 271-275. 

Scharf, M.E., Scharf, D.W., Bennett, G.W., and Pittendrigh, B.R., Catalytic activity and expression of two flavin-containing monooxygenases from Drosophila melanogastcr, Arch. Insect Biochem. Physiol., 57, 28, 2004. 

El-Alfy, A.T. and D. Schlenk. Effect of 17 beta-estradiol and testosterone on the expression of flavin-containing monooxygenase and the toxicity of aldicarb to Japanese medaka, Oryzias latipes. Toxicol. Sci. 68 381-388, 2002. 

Larsen-Su, S. and Williams, D. E., Dietary indole-3-carbinol inhibits FMO activity and the expression of flavin-containing monooxygenase form 1 in rat liver and intestine, Drug Metab. Disposition, 24, 927, 1996. 

Janmohamed, A., Hernandez, D., Phillips, I.R., Shephand, E.A. (2004). Cell, tissue, sex, and developmental stage-specific expression of mouse flavin-containing monooxygenases (FMOs). Biochemical Pharmacology, 68, 73-83. 

This approach, as well as other approaches using chemical inhibitor or inhibitory monoclonal antibodies, assumes that the probe substrates behave like the test compound. A simplified approach is to study the test compound in expressed enzymes only and then assume hepatic metabolism is covered by the several expressed enzymes that have been assayed (Venkatakrishnan et al., 2001). In other words, this simplified approach uses the sum of various supersomal clearances instead of the clearance in liver microsomes as 100% of hepatic metabolic clearance. While in most cases several major CYPs may have covered the majority of hepatic metabolism, other enzymes could also contribute significantly to the overall metabolism. Examples of non-CYP microsomal enzymes often involved in drug metabolism include flavin-containing monooxygenase (FMO), UDP—glucuronosyltransferase (UGT), sulfotransfer-ase (SULT), and many others (Parkinson and Ogilvie, 2008). 

Blazyk JL, Lippard SJ. 2002. Expression and characterization of ferredoxin and flavin adenine dinucleotide binding domains of the reductase component of soluble methane monooxygenase from Methylococcus capsulatus (Bath). Biochemistry 41 15780-15794. 

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