Faculty with Emeritus Status      Back to Main

Faculty Detail    
Name CHARLES NAPOLEON FALANY
 
Campus Address VH 151 Zip 0019
Phone  (205) 934-9848
E-mail  cfalany@uab.edu
Other websites
     


Faculty Appointment(s)
Appointment Type Department Division Rank
Primary  Pharmacology/Toxicology Chair's Office  Pharmacology/Toxicology Chair's Office Professor Emeritus

Graduate Biomedical Sciences Affiliations
Cancer Biology 
Integrative Biomedical Sciences 
Pathobiology and Molecular Medicine 

Biographical Sketch 
My undergraduate degree was received from the Dept. of Biology at the University of South Florida in 1975. Subsequently I earned a Master’s degree in Zoology from the University of South Florida in 1978. My thesis research was in amino acid metabolism in freshwater bivalves although I also had considerable experience investigating the nematocyst venom of the Portuguese Man O’ War. Next, I received my Ph.D. in Pharmacology in 1984 from the University of Iowa where I purified and characterized UDP-glucuronyltransferases involved in drug metabolism in the lab of Dr. Tom Tephly. Following this I was an American Cancer Society Postdoctoral fellow in the lab of Charles Kasper at the McArdle Cancer Center at the University of Wisconsin-Madison. After two years as a post-doc, I accepted a position as Assistant Professor of Pharmacology in Oncology at the University of Rochester. At this time my research interests were directed towards the biochemistry and molecular biology of human cytosolic sulfotransferase involved in drug metabolism and steroid metabolism in hormone responsive cancers. In 1990, I accepted a position as an Associate Professor in the Dept. of Pharmacology and Toxicology at UAB. Subsequently, I was promoted to Professor in 2000.



Research/Clinical Interest
Title
Biochemical and physiological properties of human cytosolic sulfotransferases
Description
Dr. Falany’s research interests involve the biochemical, molecular and functional analysis of the role of the human cytosolic sulfotransferases (SULT) in drug metabolism, hormone responsive cancer, and genetic diseases. Projects include the role of the induction of estrogen sulfation in cystic fibrosis. A specific isoform of estrogen SULT is induced in mice that are homozygous for the ?F508 mutation. This results in a decrease in active estrogen levels in these animals resulting in changes in the expression of estrogen regulated proteins. The physiological consequences of these changes are being investigated. Pharmacogenetic analysis of the SULT regulating adrenal androgen production is being carried out and similar studies for other SULTs are planned. Several projects investigating the role of specific SULTs in regulating steroid synthesis and metabolism in human prostate and breast. The role of the SULTs in controlling steroid levels and hormone receptor activation is one important aspect. The role of sulfation in regulating the tissue specific activity of tibolone in hormone replacement therapy is also being studied. Basic properties of the human SULTs are also being investigated including the mechanisms involved with nuclear localization in the placenta, the functions of a brain specific SULT which is extremely highly conserved in mammalian an avian species, and the properties of the individual SULTs in the activation of chemical carcinogens. Ongoing research projects also include the molecular and biochemical analysis of the enzymes involved in bile acid amidation in humans and rodents. Two enzymes, bile acid CoA ligase (BAL) and bile acid CoA: amino acid N-acyltransferase (BAT) are responsible for bile acid amidation. Our lab is investigating the molecular regulation, subcellular localization and physiological properties of these enzymes in humans and rodents.

Selected Publications 
Publication PUBMEDID
Wang J, Falany JL & Falany CN. Expression and characterization of a novel thyroid hormone-sulfating form of cytosolic sulfotransferase from human liver. Mol Pharmacol 53:274-282, 1998   
Falany JL & Falany CN. Regulation of estrogen activity by sulfation in human MCF-7 breast cancer cells. Oncol Res 9:589-596, 1998.   
Kotov A, Falany JL, Wang J & Falany CN. Regulation of estrogen activity by sulfation in human Ishikawa endometrial adenocarcinoma cells. J Steroid Biochem Mol Biol 68:137-144, 1999.   
Zhang J, Falany JL, Xie X and Falany CN. Induction of rat hepatic drug metabolizing enzymes by dimethylcyclosiloxanes. Chem. Biol. Interact. 124(2):133-47, 2000.   
Falany CN, Xie X, Wang J, Ferrer J, and Falany JL. Molecular Cloning and Expression of Novel Sulfotransferase-Like cDNAs From Human and Rat Brain. Biochem. J.346:857 64, 2000.   
Zhang H, Varmalova O, Vargas FM, Falany CN & Leyh TS. The catalytic mechanism of the human estrogen sulfotransferase. J Biol Chem 273:10888-10892, 1998.   
Falany CN, Xie X, Wheeler J, Wang J, Smith M, He D and Barnes S. Molecular Cloning and Expression of Rat Liver Bile Acid CoA Ligase. J. Lipid Res. 43:2062-2071, 2002.   
Meloche CA and Falany CN. Cloning and expression of the human 3ß-hydroxysteroid sulfotransferases (SULT 2B1a and SULT 2B1b). J. Steroid Biochem. Mol. Biol. 77:261-269, 2001.   
Falany CN, Xie X, Wheeler J, Wang J, Smith M, He D and Barnes S. Molecular Cloning and Expression of Rat Liver Bile Acid CoA Ligase. J. Lipid Res. 43:2062-2071, 2002   
Falany JL, Macrina N and Falany CN. Regulation of MCF-7 breast cancer cell growth by ß-estradiol sulfation, Breast Cancer Res. Treat. 74:167-176, 2002.