Charles N. Falany, Ph.D.


FALANY

Professor of Pharmacology and Toxicology

 

Education:
BA in Biology, University of South Florida; MA in Zoology, University of South Florida; PhD in Pharmacology, University of Iowa


Research Interests:
My research interests involve the investigation of the functions of sulfation in drug metabolism, chemical carcinogenesis and hormone action and regulation. Conjugation of compounds with a sulfate group is an important mechanism for the metabolism and excretion of many drugs and xenobiotic compounds as well as many endogenous compounds, such as steroids, bile acids and thyroid hormones. Sulfation also has an important role in the synthesis and activity of many small peptides, proteins and proteoglycans and is also involved in the bioactivation of a number of compounds to potent carcinogens. 

My laboratory is investigating the biochemistry and molecular biology of the human cytosolic sulfotransferases involved in drug and steroid sulfation. To date, we have purified or cloned six separate forms of sulfotransferase from human tissues. The pure enzymes and cDNAs are being used as tools to investigate the localization, kinetic, biochemical and molecular properties of these enzymes. Projects are ongoing to investigate the expression and function of the steroid sulfating sulfotransferases in breast and endometrial cancer cells in altering the response of these cells to hormone stimulation and therapeutic drugs. The molecular and gene structure of the individual sulfotransferases in both normal and tumor tissues is being studied as well as the regulation of expression of the enzymes in different tissues. The ability of the cloned enzymes expressed in bacteria to bioactivate hydroxymethyl polyaromatic hydrocarbons and N-hydroxy aromatic amines is also under study. 

In a separate project, we are investigating the molecular and enzymatic properties of bile acid CoA:amino acid N-acyltransferases, the enzymes responsible for the conjugation of bile acids with amino acids. The addition of the amino acid (usually taurine or glycine) to a bile acid increases its detergent properties. The human liver enzyme has been cloned and expressed in bacteria and been shown to utilize both taurine and glycine as substrates for the conjugation of bile acids. To investigate the physiological effects of the inability to conjugate bile acids, studies are underway to create a transgenic mouse which lacks the ability to conjugate bile acids. 


Selected Publications:

Glatt HR, Falany CN, Frieberg T and Bartsch I. Salmonella Strains and Mammalian Genetically Altered for Conjugating Enzymes. Internat. Congress Toxicology VII, Seattle, 1995.

Falany CN, Krasnykh and Falany JL. Substrate reactivity of four expressed human cytosolic sulfotransferases. Toxicologist 15:A1416, 1995.

Ganguly TC, Krasnykh V and Falany CN. Xenobiotic sulfation by expressed human monoamine sulfating form of phenol sulfotranserase (hM-PST): Comparison with phenol sulfating form of phenol sulfotransferase (hP-PST). FASEB J 9:A4000, 1995.

Falany CN and Falany JL. Hormonal regulation of estrogen sulfotransferase (hEST) in human Ishikawa endometrial adenocarcinoma cells. ISSX Proceedings 8:A336, 1995.

Falany JL and Falany CN. Characterization of sulfotransferase Activities in human normal and breast cancers and in normal and breast cancer cell lines. ISSX Proceedings:A247, 1995. 

To contact Dr. Falany:
1670 University Boulevard
VH 151
Birmingham, AL 35294-0019
Phone: (205) 934-9848
Fax: (205) 934-9823
E-mail: cfalany@uab.edu